Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
DETAILED ACTION
This application is a 371 of PCT/KR2022/008156.
The amendment filed on April 14, 2026 has been entered.
Election/Restrictions
Applicant’s election without traverse of Group I (claims 1-4 and 17) with a species election of a single substitution F43I in SEQ ID NO:1 in the reply filed on April 14, 2026 is acknowledged.
Claims 5-15 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on April 14, 2026.
Status of Claims
Claims 1-15 and 17 are pending.
Claims 5-15 are withdrawn.
Claims 1-4 and 17 are under examination.
Foreign Priority
Receipt is acknowledged of certified copies of papers required by 37 CFR 1.55.
Information Disclosure Statement
The information disclosure statement (IDS) submitted on December 8, 2023, December 5, 2024, and August 6, 2025 are compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statements are being considered by the examiner.
Claim Rejections - 35 USC § 112
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
Claims 1-4 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for pre-AIA the inventor(s), at the time the application was filed, had possession of the claimed invention.
MPEP 2111.01 states that "[d]uring examination, the claims must be interpreted as broadly as their terms reasonably allow.". In the instant case, the claims have been broadly interpreted to encompass any geranylgeranyl pyrophosphate synthase variant of any geranylgeranyl pyrophosphate synthase or the geranylgeranyl pyrophosphate synthase of SEQ ID NO:1, wherein the geranylgeranyl pyrophosphate synthase variant comprises an amino acid substitution at the position corresponding to F43 of SEQ ID NO:1 and having any other amino modification compared to any geranylgeranyl pyrophosphate synthase or the geranylgeranyl pyrophosphate synthase of SEQ ID NO:1. Thus, the claims are directed to a genus of polypeptides having unknown structure except not having a Phe residue at the position corresponding to 43 of SEQ ID NO:1, but having geranylgeranyl pyrophosphate synthase activity.
MPEP 2163 I. states that to “satisfy the written description requirement, a patent specification must describe the claimed invention in sufficient detail that one skilled in the art can reasonably conclude that the inventor had possession of the claimed invention.
MPEP 2163. II.A.3.(a) sates that “Possession may be shown in many ways. For example, possession may be shown by describing an actual reduction to practice of the claimed invention. Possession may also be shown by a clear depiction of the invention in detailed drawings or in structural chemical formulas which permit a person skilled in the art to clearly recognize that inventor had possession of the claimed invention. An adequate written description of the invention may be shown by any description of sufficient, relevant, identifying characteristics so long as a person skilled in the art would recognize that the inventor had possession of the claimed invention.
According to MPEP 2163.II.A.3.(a).ii), “Satisfactory disclosure of a ‘representative number’ depends on whether one of skill in the art would recognize that the applicant was in possession of the necessary common attributes or features possessed by the members of the genus in view of the species disclosed. For inventions in an unpredictable art, adequate written description of a genus which embraces widely variant species cannot be achieved by disclosing only one species within the genus…Instead, the disclosure must adequately reflect the structural diversity of the claimed genus, either through the disclosure of sufficient species that are ‘representative of the full variety or scope of the genus,’ or by the establishment of ‘a reasonable structure-function correlation.’"
The recitation of “geranylgeranyl pyrophosphate synthase” fails to provide a sufficient description of the genus of geranylgeranyl pyrophosphate synthase variants as it merely describes the functional features of the genus without providing any definition of the structural features of the species within the genus. The specification does not specifically define any of the species that fall within the genus. The specification does not define any structural features commonly possessed by members of the genus that distinguish them from others. One skilled in the art therefore cannot, as one can do with a fully described genus, visualize or recognize the identity of the members of the genus.
Boer (US 11,225,647 – form PTO-892) discloses wildtype Yarrowia lipolytica
geranylgeranyl pyrophosphate synthase of SEQ ID NO:1 having 100% sequence identity to the geranylgeranyl pyrophosphate synthase of SEQ ID NO:1 of the instant application (abstract and see the sequence alignment below). Boer also discloses geranylgeranyl pyrophosphate synthase variants of SEQ ID NO:1, wherein the variants have G92, A100, and/or S235 amino acid substitutions. However, geranylgeranyl pyrophosphate synthase variants having unknown structure, except not having a Phe residue at the position corresponding to 43 of SEQ ID NO:1 were not known in the art.
Fransceus (J Ind Microbiol Biotechnol. 2017 May;44(4-5):687-695. – form PTO-892) reviews protein engineering techniques, such as random mutagenesis and recombination, directed evolution and iterative or combinatory saturation “hotspots”. Fransceus states that “a recurring problem, however, is choosing which amino acid positions should be targeted. Answering this question is not an easy feat and requires substantial insight in the relationship between an enzyme’s sequence or structure and its properties.” Sanavia (Computational and Structural Biotechnology Journal, Volume 18, 2020, Pages 1968-1979. – form PTO-892) discloses challenges in the prediction of protein stability in the occurrence of multiple mutations. “Multiple-point mutations are common variations of the protein sequence that may be needed in protein engineering when a single-point mutation is not enough to yield the desired stability change. Dealing with multiple-site variations adds another level of complexity beyond the prediction of the effect of a single variant on protein stability, since it requires the learning of many types of combinatorial effects”.
The specification is limited to description of a geranylgeranyl pyrophosphate synthase variant of a single geranylgeranyl pyrophosphate synthase of SEQ ID NO:1, wherein the variant consists of N29, F43, L90, M103, I122, or R141 amino acid substitution. While MPEP 2163 acknowledges that in certain situations “one species adequately supports a genus,” it also acknowledges that “[f]or inventions in an unpredictable art, adequate written description of a genus which embraces widely variant species cannot be achieved by disclosing only one species within the genus.” In view of the widely variant species encompassed by the genus, the examples described above are not enough and does not constitute a representative number of species to describe the whole genus of polypeptides having unknown structure, except at the recited amino acid substitution, and having geranylgeranyl pyrophosphate synthase activity. Therefore, the specification fails to describe a representative species of the claimed genus.
Further, one of skill in the art could identify variants of a geranylgeranyl pyrophosphate synthase or geranylgeranyl pyrophosphate synthase of SEQ ID NO:1. However, there is no teaching regarding which amino acids, other than those recited in claim 1, can vary from any geranylgeranyl pyrophosphate synthase or the geranylgeranyl pyrophosphate synthase of SEQ ID NO:1 and result in polypeptide having geranylgeranyl pyrophosphate synthase activity. An important consideration is that structure is not necessarily a reliable indicator of function. In the instant case, there is no disclosure relating similarity of structure to conservation of function. Conservation of structure is not necessarily a surrogate for conservation of function. Since the claimed invention is that of an enzyme, and there is no disclosure of the domains responsible for geranylgeranyl pyrophosphate synthase activity, the absence of information may be persuasive that those of skill in the art would not take the disclosure as generic.
Given this lack of description of the representative species encompassed by the genus of the claims, the specification fails to sufficiently describe the claimed invention in such full, clear, concise, and exact terms that a skilled artisan would recognize that applicants were in possession of the inventions of claims 1-4.
Claims 1-4 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, because the specification, while being enabling for a geranylgeranyl pyrophosphate synthase variant of a single geranylgeranyl pyrophosphate synthase of SEQ ID NO:1, wherein the variant consists of N29, F43, L90, M103, I122, or R141 amino acid substitution, does not reasonably provide enablement any polypeptide having unknown structure except not having an Phe residue at the position corresponding to 43 of SEQ ID NO:1, but having geranylgeranyl pyrophosphate synthase activity. The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the invention commensurate in scope with these claims.
Factors to be considered in determining whether undue experimentation is required are summarized in In re Wands 858 F.2d 731, 8 USPQ2nd 1400 (Fed. Cir, 1988). They include (1) the quantity of experimentation necessary, (2) the amount of direction or guidance presented, (3) the presence or absence of working examples, (4) the nature of the invention, (5) the state of the prior art, (6) the relative skill of those in the art, (7) the predictability or unpredictability of the art, and (8) the breadth of the claims.
The breadth of the claims.
MPEP 2111.01 states that "[d]uring examination, the claims must be interpreted as broadly as their terms reasonably allow." In the instant case, the claims have been broadly interpreted to encompass any geranylgeranyl pyrophosphate synthase variant of any geranylgeranyl pyrophosphate synthase or the geranylgeranyl pyrophosphate synthase of SEQ ID NO:1, wherein the geranylgeranyl pyrophosphate synthase variant comprises an amino acid substitution at the position corresponding to F43 of SEQ ID NO:3 and having any other amino modification compared to any geranylgeranyl pyrophosphate synthase or the geranylgeranyl pyrophosphate synthase of SEQ ID NO:1. Thus, the claims are directed to any polypeptide having unknown structure except not having an Phe residue at the position corresponding to 43 of SEQ ID NO:1, but having geranylgeranyl pyrophosphate synthase activity.
The claims are not commensurate with the enablement provided by the disclosure with regard to the extremely large number of polypeptides having geranylgeranyl pyrophosphate synthase activity. In the instant case, the specification is limited to a geranylgeranyl pyrophosphate synthase variant of a single geranylgeranyl pyrophosphate synthase of SEQ ID NO:1, wherein the variant consists of N29, F43, L90, M103, I122, or R141 amino acid substitution.
The quantity of experimentation required to practice the claimed invention based on the teachings of the specification.
While enzyme isolation techniques, recombinant and mutagenesis techniques were known in the art at the time of the invention, e.g. mutagenesis, and it is routine in the art to screen for variants comprising multiple substitutions or multiple modifications as encompassed by the instant claims, the specific amino acid positions within the protein's sequence where amino acid modifications can be made with a reasonable expectation of success in obtaining the desired activity/utility are limited in any protein and the result of such modifications is unpredictable. In addition, one skilled in the art would expect any tolerance to modification for a given protein to diminish with each further and additional modification, e.g. multiple substitutions.
In the absence of: (a) rational and predictable scheme for making any polypeptides having geranylgeranyl pyrophosphate synthase activity, and (b) a correlation between structure and the function of having geranylgeranyl pyrophosphate synthase activity, the specification provides insufficient guidance as to which of the essentially infinite possible choices is likely to be successful. One of skill in the art would have to test these infinite possible polypeptide to determine which polypeptides have geranylgeranyl pyrophosphate synthase activity. While enablement is not precluded by the necessity for routine screening, if a large amount of screening is required, as is the case herein, the specification must provide a reasonable amount of guidance which respect to the direction in which the experimentation should proceed so that a reasonable number of species can be selected for testing. In view of the fact that such guidance has not been provided in the instant specification, it would require undue experimentation to enable the full scope of the claims.
The state of prior art, the relative skill of those in the art, and predictability or unpredictability of the art.
Since the amino acid sequence of the mutant determines its structural and functional properties, predictability of which changes can be tolerated in a protein's amino acid sequence and obtain the desired activity requires a knowledge of and guidance with regard to which amino acids in the protein's sequence, if any, are tolerant of modification and which are conserved (i.e. expectedly intolerant to modification), and detailed knowledge of the ways in which the proteins' structure relates to its function. In the instant case, neither the specification or the art provide a correlation between structure and activity such that one of skill in the art can envision the structure of any polypeptides having galactose oxidase activity or predict said function of a polypeptide from its primary structure. In addition, the art does not provide any teaching or guidance as to (1) which amino acids within the polypeptide of SEQ ID NO:1 or any geranylgeranyl pyrophosphate synthase that can be modified and which ones are conserved such that one of skill in the art can make the recited polypeptides having geranylgeranyl pyrophosphate synthase activity, (2) which segments of the polypeptide of SEQ ID NO:1 or any geranylgeranyl pyrophosphate synthase that are essential for polypeptides having geranylgeranyl pyrophosphate synthase activity, and (3) the general tolerance of the polypeptide of SEQ ID NO:1 or any geranylgeranyl pyrophosphate synthase to structural modifications and the extent of such tolerance. The art clearly teaches that changes in a protein's amino acid sequence to obtain the desired activity without any guidance/knowledge as to which amino acids in a protein are required for that activity is highly unpredictable. At the time of the invention there was a high level of unpredictability associated with altering a polypeptide sequence with an expectation that the polypeptide will maintain the desired activity. For example, Studer (Residue mutations and their impact on protein structure and function: detecting beneficial and pathogenic changes. Biochem. J. (2013) 449, 581–594. – form PTO-892 teach that (1) protein engineers are frequently surprised by the range of effects caused by single mutations that they hoped would change only one specific and simple property in enzymes, (2) the often surprising results obtained by experiments where single mutations are made reveal how little is known about the rules of protein stability, and (3) the difficulties in designing de novo stable proteins with specific functions.
Boer (US 11,225,647 – form PTO-892) discloses wildtype Yarrowia lipolytica
geranylgeranyl pyrophosphate synthase of SEQ ID NO:1 having 100% sequence identity to the geranylgeranyl pyrophosphate synthase of SEQ ID NO:1 of the instant application (abstract and see the sequence alignment below). Boer also discloses geranylgeranyl pyrophosphate synthase variants of SEQ ID NO:1, wherein the variants have G92, A100, and/or S235 amino acid substitutions. However, geranylgeranyl pyrophosphate synthase variants having unknown structure, except not having a Phe residue at the position corresponding to 43 of SEQ ID NO:1 were not known in the art.
Fransceus (J Ind Microbiol Biotechnol. 2017 May;44(4-5):687-695. – form PTO-892) reviews protein engineering techniques, such as random mutagenesis and recombination, directed evolution and iterative or combinatory saturation “hotspots”. Fransceus states that “a recurring problem, however, is choosing which amino acid positions should be targeted. Answering this question is not an easy feat and requires substantial insight in the relationship between an enzyme’s sequence or structure and its properties.” Sanavia (Computational and Structural Biotechnology Journal, Volume 18, 2020, Pages 1968-1979. – form PTO-892) discloses challenges in the prediction of protein stability in the occurrence of multiple mutations. “Multiple-point mutations are common variations of the protein sequence that may be needed in protein engineering when a single-point mutation is not enough to yield the desired stability change. Dealing with multiple-site variations adds another level of complexity beyond the prediction of the effect of a single variant on protein stability, since it requires the learning of many types of combinatorial effects”.
The amount of direction or guidance presented and the existence of working examples.
The specification is limited to a geranylgeranyl pyrophosphate synthase variant of a single geranylgeranyl pyrophosphate synthase of SEQ ID NO:1, wherein the variant consists of N29, F43, L90, M103, I122, or R141 amino acid substitution. However, the speciation fails to provide any information as to (1) specific substrates associated with any geranylgeranyl pyrophosphate synthase variant having unknown structure except having the amino acid substitution recited in claim 1 or (2) structural elements required in a polypeptide having geranylgeranyl pyrophosphate synthase activity. No correlation between structure and function of having geranylgeranyl pyrophosphate synthase activity has been presented. There is no information or guidance as to which amino acid residues in the polypeptide SEQ ID NO:1 or any geranylgeranyl pyrophosphate synthase that can be modified and which ones are to be conserved to create a polypeptide having geranylgeranyl pyrophosphate synthase activity.
Thus, in view of the overly broad scope of the claims, the lack of guidance and working examples provided in the specification, the high level of unpredictability of the prior art in regard to structural changes and their effect on function and the lack of knowledge about a correlation between structure and function, an undue experimentation would be necessary one having ordinary skill in the art to make and use the claimed invention in a manner reasonably correlated with the scope of the claims. The scope of the claims must bear a reasonable correlation with the scope of enablement (In re Fisher, 166 USPQ 19 24 (CCPA 1970)). Without sufficient guidance, determination of polypeptides having the desired biological characteristics recited in the claims are unpredictable and the experimentation left to those skilled in the art is unnecessarily, and improperly, extensive and undue. See In re Wands 858 F.2d 731, 8 USPQ2nd 1400 (Fed. Cir, 1988).
Claim Rejections - 35 USC § 102
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale or otherwise available to the public before the effective filing date of the claimed invention.
Claim(s) 1-4 is/are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Jiang (BTS1 encodes a geranylgeranyl diphosphate synthase in Saccharomyces cerevisiae. J Biol Chem. 1995 Sep 15;270(37):21793-9 - form PTO-892)
MPEP 2113 states that “[t]he patentability of a product does not depend on its method of production.”. In the instant case, the structure of the claimed geranylgeranyl pyrophosphate synthase variant implied is the same whether the geranylgeranyl pyrophosphate synthase is obtained from any recombinant engineering or is obtained from any source (including wild type proteins), as long as the resulting product has the structural limitations recited in the claims, not having a Asn, Phe, and Leu at the positions corresponding to N29, F43I and L90, respectively, of SEQ ID NO:1.
Regarding claims 1-2, Jiang discloses a Saccharomyces cerevisiae geranylgeranyl pyrophosphate synthase (Abstract and Fig 4. at page 21796). The geranylgeranyl pyrophosphate synthase of Jiang does not have Asn, Phe, and Leu at the positions corresponding to N29, F43I and L90, respectively, of SEQ ID NO:1 (Fig 4. at page 21796 and see the sequence alignment below).
Regarding claims 3-4, geranylgeranyl pyrophosphate synthase of Jiang has a Leu (nonpolar), Ile (nonpolar), and Ile (nonpolar) residues at the positions corresponding to N29, F43 and L90, respectively (Fig 4. at page 21796 and see the sequence alignment below).
Therefore, the reference of Jiang anticipates claims 1-4.
Claim Rejections - 35 USC § 101
35 U.S.C. 101 reads as follows:
Whoever invents or discovers any new and useful process, machine, manufacture, or composition of matter, or any new and useful improvement thereof, may obtain a patent therefor, subject to the conditions and requirements of this title.
Claims 1-4 are rejected under 35 U.S.C. 101 because the claimed invention is directed to a judicial exception (i.e., a law of nature, a natural phenomenon, or an abstract idea) without significantly more.
Claim interpretation
MPEP 2113 states that “[t]he patentability of a product does not depend on its method of production.”. In the instant case, the structure of the claimed geranylgeranyl pyrophosphate synthase variant implied is the same whether the geranylgeranyl pyrophosphate synthase is obtained from any recombinant engineering or is obtained from any source (including wild type proteins), as long as the resulting product has the structural limitations recited in the claims, not having a Asn, Phe, and Leu at the positions corresponding to N29, F43I and L90, respectively, of SEQ ID NO:1.
Jiang (BTS1 encodes a geranylgeranyl diphosphate synthase in Saccharomyces cerevisiae. J Biol Chem. 1995 Sep 15;270(37):21793-9 - form PTO-892) discloses a Saccharomyces cerevisiae geranylgeranyl pyrophosphate synthase (Abstract and Fig 4. at page 21796). The geranylgeranyl pyrophosphate synthase of Jiang does not have Asn, Phe, and Leu at the positions corresponding to N29, F43I and L900, respectively, of SEQ ID NO:1 (Fig 4. at page 21796 and see the sequence alignment below). The geranylgeranyl pyrophosphate synthase of Jiang has a Leu (nonpolar), Ile (nonpolar), and Ile (nonpolar) residues at the positions corresponding to N29, F43I and L90, respectively, (see the sequence alignment below).
Therefore, claims 1-4 are directed to a product of nature.
Step 1: This part of the eligibility analysis evaluates whether the claim falls within any statutory category (see MPEP 2106.03). Since the claims are directed to a protease mutant, the claims are directed to a composition of matter, which is one of the statutory categories of invention. (Step 1: YES)
Step 2A Prong 1: This part of the eligibility analysis evaluates whether the claim recites a judicial exception (see MPEP 2106.04). The claimed geranylgeranyl pyrophosphate synthase variants are not considered to have markedly different characteristics from what occurs in nature, S. cerevisiae geranylgeranyl pyrophosphate synthases discussed above and is considered to be a law of nature exception. Because there is no difference in characteristics (structural, functional, or otherwise) between the claimed geranylgeranyl pyrophosphate synthase variants and the naturally occurring S. cerevisiae geranylgeranyl pyrophosphate synthase, the claimed geranylgeranyl pyrophosphate synthase variants are directed to a judicial exception.
Step 2A Prong 2: This part of the eligibility analysis evaluates whether the claim as a whole integrates the recited judicial exception into a practical application (see MPEP 2106.04(d)). This evaluation is performed by (a) identifying whether there are any additional recited elements in the claim beyond the judicial exception and (b) evaluating those additional elements individually and in combination to determine whether the claim as a whole integrates the exception into a practical application. There are no additional elements recited in the claim beyond the judicial exception. The claims do not include additional elements that are sufficient to amount to significantly more than the judicial exception because the claimed geranylgeranyl pyrophosphate synthase is found naturally occurring in nature (S. cerevisiae geranylgeranyl pyrophosphate synthase). (Step2 A: YES)
Step 2B: This part of the eligibility analysis evaluates whether the claim as a whole amounts to significantly more than the recited exception, i.e., whether any additional element, or combination of additional elements, adds an inventive concept to the claim (see MPEP § 2106.05). The claims only recite the laws of nature and do not include any additional elements that could add significantly more to the judicial exceptions. (Step 2B: NO)
As such, the claims do not qualify as eligible subject matter.
Conclusion
Claims 1-15 and 17 are pending.
Claims 5-15 are withdrawn.
Claims 1-4 are rejected.
Claim 17 is objected to as being dependent upon a rejected base claim, but would be allowable if rewritten in independent form including all of the limitations of the base claim and any intervening claims.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to YONG D PAK whose telephone number is (571)272-0935. The examiner can normally be reached M-Th: 5:30 am - 3:30 pm.
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If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Robert Mondesi can be reached on 408-918-7584. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/YONG D PAK/Primary Examiner, Art Unit 1652
Sequence alignment between the geranylgeranyl pyrophosphate synthase of SEQ ID NO:1 of the instant application (“Qy”) and the geranylgeranyl pyrophosphate synthase of SEQ ID NO:1 of Boer(“Db”)
US-16-345-129-1
Filing date in PALM: 2019-04-25
Sequence 1, US/16345129
Patent No. 11225647
GENERAL INFORMATION
APPLICANT: DSM IP ASSETS B.V.
TITLE OF INVENTION: GERANYLGERANYL PYROPHOSPHATE SYNTHASES
FILE REFERENCE: 32211-WO-PCT; 2919208-501000
CURRENT APPLICATION NUMBER: US/16/345,129
CURRENT FILING DATE: 2019-04-25
PRIOR APPLICATION NUMBER: EP 16196095.0
PRIOR FILING DATE: 2016-10-27
PRIOR APPLICATION NUMBER: PCT/EP2017/077439
PRIOR FILING DATE: 2017-10-26
NUMBER OF SEQ ID NOS: 33
SEQ ID NO 1
LENGTH: 327
TYPE: PRT
ORGANISM: Yarrowia lipolytica
Query Match 100.0%; Score 1695; Length 327;
Best Local Similarity 100.0%;
Matches 327; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 MDYNSADFKEIWGKAADTALLGPYNYLANNRGHNIREHLIAAFGAVIKVDKSDLETISHI 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 MDYNSADFKEIWGKAADTALLGPYNYLANNRGHNIREHLIAAFGAVIKVDKSDLETISHI 60
Qy 61 TKILHNSSLLVDDVEDNSMLRRGLPAAHCLFGVPQTINSANYMYFVALQEVLKLKSYDAV 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 TKILHNSSLLVDDVEDNSMLRRGLPAAHCLFGVPQTINSANYMYFVALQEVLKLKSYDAV 120
Qy 121 SIFTEEMINLHRGQGMDLYWRETLTCPSEDEYLEMVVHKTGGLFRLALRLMLSVASKQED 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 SIFTEEMINLHRGQGMDLYWRETLTCPSEDEYLEMVVHKTGGLFRLALRLMLSVASKQED 180
Qy 181 HEKINFDLTHLTDTLGVIYQILDDYLNLQSTELTENKGFCEDISEGKFSFPLIHSIRTNP 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 HEKINFDLTHLTDTLGVIYQILDDYLNLQSTELTENKGFCEDISEGKFSFPLIHSIRTNP 240
Qy 241 DNHEILNILKQRTSDASLKKYAVDYMRTETKSFDYCLKRIQAMSLKASSYIDDLAAAGHD 300
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 241 DNHEILNILKQRTSDASLKKYAVDYMRTETKSFDYCLKRIQAMSLKASSYIDDLAAAGHD 300
Qy 301 VSKLRAILHYFVSTSDCEERKYFEDAQ 327
|||||||||||||||||||||||||||
Db 301 VSKLRAILHYFVSTSDCEERKYFEDAQ 327
Sequence alignment between the geranylgeranyl pyrophosphate synthase of SEQ ID NO:1 of the instant application (“Qy”) and the geranylgeranyl pyrophosphate synthase of Jiang (“Db”)
GGPPS_YEAST
ID GGPPS_YEAST Reviewed; 335 AA.
AC Q12051; D6W3U6;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 28-JAN-2026, entry version 183.
DE RecName: Full=Geranylgeranyl pyrophosphate synthase BTS1 {ECO:0000303|PubMed:7665600};
DE Short=GGPP synthase;
DE Short=GGPPSase;
DE EC=2.5.1.-;
DE AltName: Full=(2E,6E)-farnesyl diphosphate synthase;
DE AltName: Full=BET2 suppressor protein 1;
DE AltName: Full=Dimethylallyltranstransferase;
DE EC=2.5.1.1;
DE AltName: Full=Farnesyl diphosphate synthase;
DE AltName: Full=Farnesyltranstransferase;
DE EC=2.5.1.29;
DE AltName: Full=Geranylgeranyl diphosphate synthase;
DE AltName: Full=Geranyltranstransferase;
DE EC=2.5.1.10;
GN Name=BTS1; OrderedLocusNames=YPL069C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=7665600; DOI=10.1074/jbc.270.37.21793;
RA Jiang Y., Proteau P., Poulter D., Ferro-Novick S.;
RT "BTS1 encodes a geranylgeranyl diphosphate synthase in Saccharomyces
RT cerevisiae.";
RL J. Biol. Chem. 270:21793-21799(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875; DOI=10.1038/387s103;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP FUNCTION.
RX PubMed=15296494; DOI=10.1111/j.1600-0854.2004.00213.x;
RA Shiflett S.L., Vaughn M.B., Huynh D., Kaplan J., McVey Ward D.;
RT "Bph1p, the Saccharomyces cerevisiae homologue of CHS1/beige, functions in
RT cell wall formation and protein sorting.";
RL Traffic 5:700-710(2004).
RN [7]
RP SUBUNIT, AND MUTAGENESIS OF GLU-7; LEU-8 AND ILE-9.
RX PubMed=19245203; DOI=10.1021/ja808699c;
RA Lo C.-H., Chang Y.-H., Wright J.D., Chen S.-H., Kan D., Lim C.,
RA Liang P.-H.;
RT "Combined experimental and theoretical study of long-range interactions
RT modulating dimerization and activity of yeast geranylgeranyl diphosphate
RT synthase.";
RL J. Am. Chem. Soc. 131:4051-4062(2009).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS, AND
RP SUBUNIT.
RX PubMed=16554305; DOI=10.1074/jbc.m512886200;
RA Chang T.-H., Guo R.-T., Ko T.-P., Wang A.H.-J., Liang P.-H.;
RT "Crystal structure of type-III geranylgeranyl pyrophosphate synthase from
RT Saccharomyces cerevisiae and the mechanism of product chain length
RT determination.";
RL J. Biol. Chem. 281:14991-15000(2006).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEXES WITH ISOPENTENYL
RP DIPHOSPHATE; FARNESYL DIPHOSPHATE AND MAGNESIUM, COFACTOR, AND SUBUNIT.
RX PubMed=17535895; DOI=10.1073/pnas.0702254104;
RA Guo R.-T., Cao R., Liang P.-H., Ko T.-P., Chang T.-H., Hudock M.P.,
RA Jeng W.-Y., Chen C.K.-M., Zhang Y., Song Y., Kuo C.-J., Yin F.,
RA Oldfield E., Wang A.H.-J.;
RT "Bisphosphonates target multiple sites in both cis- and trans-
RT prenyltransferases.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10022-10027(2007).
CC -!- FUNCTION: Catalyzes the trans-addition of the 3 molecules of IPP onto
CC DMAPP to form geranylgeranyl pyrophosphate. Required for the membrane
CC attachment of YPT1 and SEC4. May be involved in vesicle trafficking and
CC protein sorting. {ECO:0000269|PubMed:15296494,
CC ECO:0000269|PubMed:7665600}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=isopentenyl diphosphate + dimethylallyl diphosphate = (2E)-
CC geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057,
CC ChEBI:CHEBI:128769; EC=2.5.1.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=isopentenyl diphosphate + (2E)-geranyl diphosphate = (2E,6E)-
CC farnesyl diphosphate + diphosphate; Xref=Rhea:RHEA:19361,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769,
CC ChEBI:CHEBI:175763; EC=2.5.1.10;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=isopentenyl diphosphate + (2E,6E)-farnesyl diphosphate =
CC (2E,6E,10E)-geranylgeranyl diphosphate + diphosphate;
CC Xref=Rhea:RHEA:17653, ChEBI:CHEBI:33019, ChEBI:CHEBI:58756,
CC ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.29;
CC Evidence={ECO:0000269|PubMed:7665600};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:17535895};
CC Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000269|PubMed:17535895};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.2 uM for farnesyl diphosphate;
CC KM=0.8 uM for isopentenyl diphosphate;
CC -!- PATHWAY: Isoprenoid biosynthesis; farnesyl diphosphate biosynthesis;
CC farnesyl diphosphate from geranyl diphosphate and isopentenyl
CC diphosphate: step 1/1.
CC -!- PATHWAY: Isoprenoid biosynthesis; geranyl diphosphate biosynthesis;
CC geranyl diphosphate from dimethylallyl diphosphate and isopentenyl
CC diphosphate: step 1/1.
CC -!- PATHWAY: Isoprenoid biosynthesis; geranylgeranyl diphosphate
CC biosynthesis; geranylgeranyl diphosphate from farnesyl diphosphate and
CC isopentenyl diphosphate: step 1/1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- MISCELLANEOUS: Present with 2840 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR EMBL; U39205; AAB68296.1; -; Genomic_DNA.
DR EMBL; U31632; AAA83262.1; -; Genomic_DNA.
DR EMBL; AY692852; AAT92871.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11362.1; -; Genomic_DNA.
DR PIR; S60921; S60921.
DR RefSeq; NP_015256.1; NM_001183883.1.
DR PDB; 2DH4; X-ray; 1.98 A; A/B=1-335.
DR PDB; 2E8T; X-ray; 2.13 A; A/B=1-335.
DR PDB; 2E8U; X-ray; 2.08 A; A/B=1-335.
DR PDB; 2E8V; X-ray; 1.80 A; A/B=1-335.
DR PDB; 2E8W; X-ray; 2.35 A; A/B=1-335.
DR PDB; 2E8X; X-ray; 2.04 A; A/B=1-335.
DR PDB; 2E90; X-ray; 2.55 A; A/B=1-335.
DR PDB; 2E91; X-ray; 2.14 A; A/B=1-335.
DR PDB; 2E92; X-ray; 2.31 A; A/B=1-335.
DR PDB; 2E93; X-ray; 2.12 A; A/B=1-335.
DR PDB; 2E94; X-ray; 2.18 A; A/B=1-335.
DR PDB; 2E95; X-ray; 2.20 A; A/B=1-335.
DR PDB; 2Z4V; X-ray; 1.86 A; A/B=1-335.
DR PDB; 2Z4W; X-ray; 2.45 A; A/B=1-335.
DR PDB; 2Z4X; X-ray; 1.90 A; A/B=1-335.
DR PDB; 2Z4Y; X-ray; 2.10 A; A/B=1-335.
DR PDB; 2Z4Z; X-ray; 2.09 A; A/B=1-335.
DR PDB; 2Z50; X-ray; 2.01 A; A/B=1-335.
DR PDB; 2Z52; X-ray; 2.13 A; A/B=1-335.
DR PDB; 2Z78; X-ray; 2.10 A; A/B=1-335.
DR PDB; 2Z7H; X-ray; 2.08 A; A/B=1-335.
DR PDB; 2Z7I; X-ray; 2.10 A; A/B=1-335.
DR PDB; 2ZEU; X-ray; 2.00 A; A/B=1-335.
DR PDB; 2ZEV; X-ray; 2.23 A; A/B=1-335.
DR PDBsum; 2DH4; -.
DR PDBsum; 2E8T; -.
DR PDBsum; 2E8U; -.
DR PDBsum; 2E8V; -.
DR PDBsum; 2E8W; -.
DR PDBsum; 2E8X; -.
DR PDBsum; 2E90; -.
DR PDBsum; 2E91; -.
DR PDBsum; 2E92; -.
DR PDBsum; 2E93; -.
DR PDBsum; 2E94; -.
DR PDBsum; 2E95; -.
DR PDBsum; 2Z4V; -.
DR PDBsum; 2Z4W; -.
DR PDBsum; 2Z4X; -.
DR PDBsum; 2Z4Y; -.
DR PDBsum; 2Z4Z; -.
DR PDBsum; 2Z50; -.
DR PDBsum; 2Z52; -.
DR PDBsum; 2Z78; -.
DR PDBsum; 2Z7H; -.
DR PDBsum; 2Z7I; -.
DR PDBsum; 2ZEU; -.
DR PDBsum; 2ZEV; -.
DR AlphaFoldDB; Q12051; -.
DR SMR; Q12051; -.
DR BioGRID; 36110; 1035.
DR DIP; DIP-8889N; -.
DR FunCoup; Q12051; 534.
DR IntAct; Q12051; 13.
DR STRING; 4932.YPL069C; -.
DR BindingDB; Q12051; -.
DR ChEMBL; CHEMBL1075251; -.
DR DrugCentral; Q12051; -.
DR GlyGen; Q12051; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q12051; -.
DR PaxDb; 4932-YPL069C; -.
DR PeptideAtlas; Q12051; -.
DR EnsemblFungi; YPL069C_mRNA; YPL069C; YPL069C.
DR GeneID; 856036; -.
DR KEGG; sce:YPL069C; -.
DR AGR; SGD:S000005990; -.
DR SGD; S000005990; BTS1.
DR VEuPathDB; FungiDB:YPL069C; -.
DR eggNOG; KOG0777; Eukaryota.
DR HOGENOM; CLU_014015_6_0_1; -.
DR InParanoid; Q12051; -.
DR OMA; ANFAYFW; -.
DR OrthoDB; 6921389at2759; -.
DR BioCyc; MetaCyc:YPL069C-MONOMER; -.
DR BioCyc; YEAST:YPL069C-MONOMER; -.
DR BRENDA; 2.5.1.29; 984.
DR Reactome; R-SCE-191273; Cholesterol biosynthesis.
DR SABIO-RK; Q12051; -.
DR UniPathway; UPA00259; UER00368.
DR UniPathway; UPA00260; UER00369.
DR UniPathway; UPA00389; UER00564.
DR BioGRID-ORCS; 856036; 0 hits in 10 CRISPR screens.
DR EvolutionaryTrace; Q12051; -.
DR PRO; PR:Q12051; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q12051; protein.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0004337; F:(2E,6E)-farnesyl diphosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0004161; F:dimethylallyltranstransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004311; F:geranylgeranyl diphosphate synthase activity; IDA:CACAO.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045337; P:farnesyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0033384; P:geranyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0033386; P:geranylgeranyl diphosphate biosynthetic process; IDA:CACAO.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IDA:SGD.
DR CDD; cd00685; Trans_IPPS_HT; 1.
DR DisProt; DP03620; -.
DR FunFam; 1.10.600.10:FF:000030; Geranylgeranyl pyrophosphate synthase; 1.
DR Gene3D; 1.10.600.10; Farnesyl Diphosphate Synthase; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR000092; Polyprenyl_synt.
DR InterPro; IPR033749; Polyprenyl_synt_CS.
DR PANTHER; PTHR12001; GERANYLGERANYL PYROPHOSPHATE SYNTHASE; 1.
DR PANTHER; PTHR12001:SF44; GERANYLGERANYL PYROPHOSPHATE SYNTHASE; 1.
DR Pfam; PF00348; polyprenyl_synt; 1.
DR SFLD; SFLDS00005; Isoprenoid_Synthase_Type_I; 1.
DR SFLD; SFLDG01017; Polyprenyl_Transferase_Like; 1.
DR SUPFAM; SSF48576; Terpenoid synthases; 1.
DR PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1.
DR PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carotenoid biosynthesis; Cytoplasm; Isoprene biosynthesis;
KW Magnesium; Metal-binding; Protein transport; Reference proteome;
KW Transferase; Transport.
FT CHAIN 1..335
FT /note="Geranylgeranyl pyrophosphate synthase BTS1"
FT /id="PRO_0000228139"
FT BINDING 36
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000269|PubMed:17535895"
FT BINDING 39
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000269|PubMed:17535895"
FT BINDING 68
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000269|PubMed:17535895"
FT BINDING 75
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:16554305,
FT ECO:0000269|PubMed:17535895"
FT BINDING 75
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:16554305,
FT ECO:0000269|PubMed:17535895"
FT BINDING 79
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:16554305,
FT ECO:0000269|PubMed:17535895"
FT BINDING 79
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:16554305,
FT ECO:0000269|PubMed:17535895"
FT BINDING 84
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000269|PubMed:17535895"
FT BINDING 85
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000269|PubMed:17535895"
FT BINDING 169
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000269|PubMed:17535895"
FT BINDING 170
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000269|PubMed:17535895"
FT BINDING 206
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000269|PubMed:17535895"
FT BINDING 213
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000269|PubMed:17535895"
FT BINDING 223
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000305|PubMed:17535895"
FT BINDING 233
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000269|PubMed:17535895"
FT SITE 107
FT /note="Important for determining product chain length"
FT MUTAGEN 7
FT /note="E->G: No effect. Monomer; when associated with G-8."
FT /evidence="ECO:0000269|PubMed:19245203"
FT MUTAGEN 8
FT /note="L->G: Monomer and homodimer. Monomer; when
FT associated with G-7."
FT /evidence="ECO:0000269|PubMed:19245203"
FT MUTAGEN 9
FT /note="I->G: Mostly monomer. Exclusively monomer; when
FT associated with G-8. Reduces enzyme activity 1000-fold."
FT /evidence="ECO:0000269|PubMed:19245203"
FT MUTAGEN 107
FT /note="Y->A: Reduced affinity for isopentenyl diphosphate
FT (IPP)."
FT MUTAGEN 108
FT /note="F->A: Reduced affinity for isopentenyl diphosphate
FT (IPP)."
FT MUTAGEN 139
FT /note="H->A: Reduced affinity for isopentenyl diphosphate
FT (IPP)."
FT HELIX 1..9
FT /evidence="ECO:0007829|PDB:2E8V"
FT HELIX 17..31
FT /evidence="ECO:0007829|PDB:2E8V"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:2E8X"
FT HELIX 38..50
FT /evidence="ECO:0007829|PDB:2E8V"
FT HELIX 54..78
FT /evidence="ECO:0007829|PDB:2E8V"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:2E8V"
FT HELIX 90..93
FT /evidence="ECO:0007829|PDB:2E8V"
FT HELIX 96..113
FT /evidence="ECO:0007829|PDB:2E8V"
FT HELIX 114..117
FT /evidence="ECO:0007829|PDB:2E8V"
FT HELIX 121..150
FT /evidence="ECO:0007829|PDB:2E8V"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:2Z4V"
FT HELIX 159..169
FT /evidence="ECO:0007829|PDB:2E8V"
FT HELIX 171..184
FT /evidence="ECO:0007829|PDB:2E8V"
FT HELIX 195..215
FT /evidence="ECO:0007829|PDB:2E8V"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:2DH4"
FT HELIX 227..230
FT /evidence="ECO:0007829|PDB:2E8V"
FT HELIX 236..247
FT /evidence="ECO:0007829|PDB:2E8V"
FT HELIX 251..263
FT /evidence="ECO:0007829|PDB:2E8V"
FT HELIX 268..280
FT /evidence="ECO:0007829|PDB:2E8V"
FT HELIX 284..300
FT /evidence="ECO:0007829|PDB:2E8V"
FT HELIX 325..330
FT /evidence="ECO:0007829|PDB:2Z4V"
FT TURN 331..333
FT /evidence="ECO:0007829|PDB:2Z4V"
SQ SEQUENCE 335 AA; 38651 MW; 4C7D6527FF29F157 CRC64;
Query Match 37.1%; Score 629; Length 335;
Best Local Similarity 40.8%;
Matches 131; Conservative 62; Mismatches 104; Indels 24; Gaps 6;
Qy 11 IWGKAADTALLGPYNYLANNRGHNIREHLIAAFGAVIKVDKSDLETISHITKILHNSSLL 70
:| :: : |||:: | | | :|| |: : | | :| | ::|||||||
Db 14 VWSSQNESLISKPYNHILLKPGKNFRLNLIVQINRVMNLPKDQLAIVSQIVELLHNSSLL 73
Qy 71 VDDVEDNSMLRRGLPAAHCLFGVPQTINSANYMYFVALQEVLKLKS-----YDAVSIFTE 125
:||:|||: |||| :| :|||| |||:|||||| |:| | :| : :: ::|| |
Db 74 IDDIEDNAPLRRGQTTSHLIFGVPSTINTANYMYFRAMQLVSQLTTKEPLYHNLITIFNE 133
Qy 126 EMINLHRGQGMDLYWRETL--TCPSEDEYLEMVVHKTGGLFRLALRLMLSVA-SKQEDHE 182
|:||||||||:|:|||: | |::: || ||::|||||||| |||| ::: | |
Db 134 ELINLHRGQGLDIYWRDFLPEIIPTQEMYLNMVMNKTGGLFRLTLRLMEALSPSSHHGHS 193
Qy 183 KINFDLTHLTDTLGVIYQILDDYLNLQSTELTENKGFCEDISEGKFSFPLIHSIR----- 237
: | : ||:|||| ||||||: ::: ||| |||:||| |||::|::
Db 194 LVPF-----INLLGIIYQIRDDYLNLKDFQMSSEKGFAEDITEGKLSFPIVHALNFTKTK 248
Qy 238 -TNPDNHEILNILKQRTSDASLKKYAVDYMRTETKSFDYCLKRIQAM-----SLKASSYI 291
::||| || |||| :| : : :| | | | : : : |:
Db 249 GQTEQHNEILRILLLRTSDKDIKLKLIQILEFDTNSLAYTKNFINQLVNMIKNDNENKYL 308
Qy 292 DDLAAAGHDVSKLRAILHYFV 312
|||: : | | | :
Db 309 PDLASHSDTATNLHDELLYII 329
Prosecution Insights