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 continuation of PCT/KR2021/018520.
The amendment filed on November 3, 2025 has been entered.
Election/Restrictions
Applicant’s election without traverse of Group I with a species election of (1) SEQ ID NO:1 as the parent gamma(λ)-aminobutyrate permease and (2) 114F as the amino acid modification made in said gamma(λ)-aminobutyrate permease in the reply filed on November 3, 2025 is acknowledged. Applicant’s request for rejoinder of claims depending from the elected invention has been noted.
Claims 2-13 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected invention there being no allowable generic or linking claim.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 November 3 2025.
Status of Claims
Claims 1-13 and 16-19 are pending.
Claims 2-13 are withdrawn.
Claims 1 and 16-19 are under examination.
Claim for 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 June 9, 2023, May 15, 2024, and June 18, 2024 are in 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 and 6-18 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.'' The claims have been broadly interpreted to encompass polypeptides having at least 80-95% sequence identity to SEQ ID NO:1, wherein the polypeptides have a Phe residue at the position corresponding to 114 of SEQ ID NO:1 and have gamma(λ)-aminobutyrate permease activity. Therefore, the claims are drawn to a genus of polypeptides having 80-95% sequence identity to SEQ ID NO:1 and a Phe residue at the position corresponding to 114 of SEQ ID NO:1, but having the function of gamma(λ)-aminobutyrate permease 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 “gamma(λ)-aminobutyrate permease” fails to provide a sufficient description of the genus of the polypeptides 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.
Prior art discloses that the polypeptide having the amino acid sequence of SEQ ID NO:1 of the instant application is a general aromatic amino acid transporter (AroPCg). Wehrman (Functional analysis of sequences adjacent to dapE of Corynebacterium glutamicum reveals the presence of aroP, which encodes the aromatic amino acid transporter. J Bacteriol. 1995 Oct;177(20):5991-3. – form PTO-892) discloses a general aromatic amino acid transporter (AroPCg) having 100% sequence identity to SEQ ID NO:1 of the instant application, (abstract, FIG.2, page 5992, and see the sequence alignment below). AROP_CORGL (UniprotKB/Swiss-Prot Database. December 2, 2020 – form PTO-892) also discloses that the AroPCg of Wehrman is an aromatic amino acid transporter (page 1). However, the prior art does not disclose the polypeptide having the amino acid sequence of SEQ ID NO:1 of the instant application as a gamma(λ)-aminobutyrate permease. A BLAST search SEQ ID NO:1 of the instant application did not result in polypeptides having any significant similarity to SEQ ID NO:1 of the instant application and having gamma(λ)-aminobutyrate permease activity, as shown below.
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The specification is limited to description of three specific variants of a single parent polypeptide having the amino acid sequence of SEQ ID NO:1, wherein the variants consist of single point mutations of A28V, I114F, or G212T and wherein the variants have gamma(λ)-aminobutyrate permease activity. 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 three examples described above is not enough and does not constitute a representative number of species to describe the whole genus. Therefore, the specification fails to describe a representative species of the claimed genus.
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”.
Further, one of skill in the art could identify variants of SEQ ID NO:1 having 80-95% sequence identity to SEQ ID NO:1. However, there is no teaching regarding which amino acids can vary from SEQ ID NO:1, other than A28, I114, or G212, and result in polypeptide having gamma(λ)-aminobutyrate permease 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 having gamma(λ)-aminobutyrate permease 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 and 16-18.
Claims 1 and 16-18 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 three specific variants of a single parent polypeptide having the amino acid sequence of SEQ ID NO:1, wherein the variants consist of single point mutations of A28V, I114F, or G212T and wherein the variants have gamma(λ)-aminobutyrate permease activity, does not reasonably provide enablement any polypeptide having 80-95% sequence identity to SEQ ID NO:1 and having a Phe residue at the position corresponding to 114 of SEQ ID NO:1, but having the function of gamma(λ)-aminobutyrate permease 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.
The claims have been broadly interpreted to encompass polypeptides having at least 80-95% sequence identity to SEQ ID NO:1, wherein the polypeptides have a Phe residue at the position corresponding to 114 of SEQ ID NO:1 and have gamma(λ)-aminobutyrate permease activity. Therefore, the claims are drawn to any polypeptide having 80-95% sequence identity to SEQ ID NO:1 and a Phe residue at the position corresponding to 114 of SEQ ID NO:1, but having the function of gamma(λ)-aminobutyrate permease activity.
The claims are not commensurate with the enablement provided by the disclosure with regard to the extremely large number of polypeptides having gamma(λ)-aminobutyrate permease activity. In the instant case, the specification is limited to three specific variants of a single parent polypeptide having the amino acid sequence of SEQ ID NO:1, wherein the variants consist of single point mutations of A28V, I114F, or G212T and wherein the variants have gamma(λ)-aminobutyrate permease activity.
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 variant of SEQ ID NO:1 having at least 80-95% sequence identity to SEQ ID NO:1 and having gamma(λ)-aminobutyrate permease activity and (b) a correlation between structure and the function of having gamma(λ)-aminobutyrate permease 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 polypeptides to determine which polypeptides have gamma(λ)-aminobutyrate permease 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 polypeptide having at least 80-95% sequence identity and having gamma(λ)-aminobutyrate permease activity. In addition, the art does not provide any teaching or guidance as to (1) which segments of the polypeptide of SEQ ID NO:1 that are essential for polypeptides having gamma(λ)-aminobutyrate permease activity, (2) which amino acids of SEQ ID NO:1, other than the amino acid position 212, 114, or 28, can be modified and result in a polypeptide having gamma(λ)-aminobutyrate permease activity, and (3) the general tolerance of the polypeptide of SEQ ID NO:1 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.
Prior art discloses that the polypeptide having the amino acid sequence of SEQ ID NO:1 of the instant application is a general aromatic amino acid transporter (AroPCg). Wehrman (Functional analysis of sequences adjacent to dapE of Corynebacterium glutamicum reveals the presence of aroP, which encodes the aromatic amino acid transporter. J Bacteriol. 1995 Oct;177(20):5991-3. – form PTO-892) discloses a general aromatic amino acid transporter (AroPCg) having 100% sequence identity to SEQ ID NO:1 of the instant application, (abstract, FIG.2, page 5992, and see the sequence alignment below). AROP_CORGL (UniprotKB/Swiss-Prot Database. December 2, 2020 – form PTO-892) also discloses that the AroPCg of Wehrman is an aromatic amino acid transporter (page 1). However, the prior art does not disclose the polypeptide having the amino acid sequence of SEQ ID NO:1 of the instant application as a gamma(λ)-aminobutyrate permease. A BLAST search SEQ ID NO:1 of the instant application did not result in polypeptides having any significant similarity to SEQ ID NO:1 of the instant application and having gamma(λ)-aminobutyrate permease activity, as shown below.
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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 three specific variants of a single parent polypeptide having the amino acid sequence of SEQ ID NO:1, wherein the variants consist of single point mutations of A28V, I114F, or G212T and wherein the variants have gamma(λ)-aminobutyrate permease activity. However, the speciation fails to provide any information as to (1) specific substrates associated with any polypeptide having at least 80-95% sequence identity and having gamma(λ)-aminobutyrate permease activity or (2) structural elements required in a polypeptide having gamma(λ)-aminobutyrate permease activity. No correlation between structure and function of having gamma(λ)-aminobutyrate permease activity has been presented.
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).
Conclusion
Claims 1-13 and 16-19 are pending.
Claims 2-13 are withdrawn.
Claims 1 and 16-18 are rejected.
Claim 19 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 polypeptide of SEQ ID NO:1 of the instant application (“Qy”) and the AroPCg of Wehrmann/AROP_CORGL (“Db”)
AROP_CORGL
ID AROP_CORGL Reviewed; 463 AA.
AC Q46065;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 05-FEB-2025, entry version 133.
DE RecName: Full=Aromatic amino acid transport protein AroP;
DE AltName: Full=General aromatic amino acid permease;
GN Name=aroP {ECO:0000303|PubMed:7592354}; OrderedLocusNames=Cgl1107, cg1257;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC
OS 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 /
OS 534).
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG
RC 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534;
RX PubMed=7592354; DOI=10.1128/jb.177.20.5991-5993.1995;
RA Wehrmann A., Morakkabati S., Kraemer R., Sahm H., Eggeling L.;
RT "Functional analysis of sequences adjacent to dapE of Corynebacterium
RT glutamicum reveals the presence of aroP, which encodes the aromatic amino
RT acid transporter.";
RL J. Bacteriol. 177:5991-5993(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG
RC 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG
RC 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
CC -!- FUNCTION: Permease that is involved in the active transport across the
CC cytoplasmic membrane of all three aromatic amino acids, phenylalanine,
CC tyrosine and tryptophan. {ECO:0000305|PubMed:7592354}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-phenylalanine(in) + H(+)(in) = L-phenylalanine(out) +
CC H(+)(out); Xref=Rhea:RHEA:28923, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58095; Evidence={ECO:0000305|PubMed:7592354};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28925;
CC Evidence={ECO:0000305|PubMed:7592354};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tryptophan(in) + H(+)(in) = L-tryptophan(out) + H(+)(out);
CC Xref=Rhea:RHEA:28879, ChEBI:CHEBI:15378, ChEBI:CHEBI:57912;
CC Evidence={ECO:0000305|PubMed:7592354};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28881;
CC Evidence={ECO:0000305|PubMed:7592354};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tyrosine(in) + H(+)(in) = L-tyrosine(out) + H(+)(out);
CC Xref=Rhea:RHEA:28875, ChEBI:CHEBI:15378, ChEBI:CHEBI:58315;
CC Evidence={ECO:0000305|PubMed:7592354};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28877;
CC Evidence={ECO:0000305|PubMed:7592354};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Mutants show reduced aromatic amino acids uptake.
CC {ECO:0000269|PubMed:7592354}.
CC -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC superfamily. Amino acid transporter (AAT) (TC 2.A.3.1) family.
CC {ECO:0000305}.
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DR EMBL; X85965; CAA59950.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB98500.1; -; Genomic_DNA.
DR EMBL; BX927151; CAF19813.1; -; Genomic_DNA.
DR PIR; S52754; S52754.
DR RefSeq; NP_600335.2; NC_003450.3.
DR RefSeq; WP_011014125.1; NC_006958.1.
DR AlphaFoldDB; Q46065; -.
DR SMR; Q46065; -.
DR STRING; 196627.cg1257; -.
DR TCDB; 2.A.3.1.12; the amino acid-polyamine-organocation (apc) family.
DR GeneID; 1019092; -.
DR KEGG; cgb:cg1257; -.
DR KEGG; cgl:Cgl1107; -.
DR PATRIC; fig|196627.13.peg.1086; -.
DR eggNOG; COG1113; Bacteria.
DR HOGENOM; CLU_007946_9_2_11; -.
DR OrthoDB; 5297508at2; -.
DR BioCyc; CORYNE:G18NG-10679-MONOMER; -.
DR Proteomes; UP000000582; Chromosome.
DR Proteomes; UP000001009; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR FunFam; 1.20.1740.10:FF:000001; Amino acid permease; 1.
DR Gene3D; 1.20.1740.10; Amino acid/polyamine transporter I; 1.
DR InterPro; IPR004841; AA-permease/SLC12A_dom.
DR InterPro; IPR004840; Amino_acid_permease_CS.
DR PANTHER; PTHR43495; GABA PERMEASE; 1.
DR PANTHER; PTHR43495:SF5; GAMMA-AMINOBUTYRIC ACID PERMEASE; 1.
DR Pfam; PF00324; AA_permease; 1.
DR PIRSF; PIRSF006060; AA_transporter; 1.
DR PROSITE; PS00218; AMINO_ACID_PERMEASE_1; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..463
FT /note="Aromatic amino acid transport protein AroP"
FT /id="PRO_0000054192"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 337..357
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 358..378
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 402..422
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 431..451
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 463 AA; 49268 MW; 3071063590264F08 CRC64;
Query Match 100.0%; Score 2338; Length 463;
Best Local Similarity 100.0%;
Matches 463; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 MAKSNEGLGTGLRTRHLTMMGLGSAIGAGLFLGTGVGIRAAGPAVLLAYIIAGAIVVLVM 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 MAKSNEGLGTGLRTRHLTMMGLGSAIGAGLFLGTGVGIRAAGPAVLLAYIIAGAIVVLVM 60
Qy 61 QMLGEMAAARPASGSFSRYGEDAFGHWAGFSLGWLYWFMLIMVMGAEMTGAAAIMGAWFG 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 QMLGEMAAARPASGSFSRYGEDAFGHWAGFSLGWLYWFMLIMVMGAEMTGAAAIMGAWFG 120
Qy 121 VEPWIPSLVCVVFFAVVNLVAVRGFGEFEYWFAFIKVAVIIAFLIIGIALIFGWLPGSTF 180
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Db 121 VEPWIPSLVCVVFFAVVNLVAVRGFGEFEYWFAFIKVAVIIAFLIIGIALIFGWLPGSTF 180
Qy 181 VGTSNFIGDHGFMPNGISGVAAGLLAVAFAFGGIEIVTIAAAESDKPREAISLAVRAVIW 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 VGTSNFIGDHGFMPNGISGVAAGLLAVAFAFGGIEIVTIAAAESDKPREAISLAVRAVIW 240
Qy 241 RISVFYLGSVLVITFLMPYESINGADTAAESPFTQILAMANIPGTVGFMEAIIVLALLSA 300
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 241 RISVFYLGSVLVITFLMPYESINGADTAAESPFTQILAMANIPGTVGFMEAIIVLALLSA 300
Qy 301 FNAQIYATSRLVFSMANRQDAPRVFSKLSTSHVPTNAVLLSMFFAFVSVGLQYWNPAGLL 360
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 301 FNAQIYATSRLVFSMANRQDAPRVFSKLSTSHVPTNAVLLSMFFAFVSVGLQYWNPAGLL 360
Qy 361 DFLLNAVGGCLIVVWAMITLSQLKLRKELQANDEISTVRMWAHPWLGILTLVLLAGLVAL 420
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 361 DFLLNAVGGCLIVVWAMITLSQLKLRKELQANDEISTVRMWAHPWLGILTLVLLAGLVAL 420
Qy 421 MLGDAASRSQVYSVAIVYGFLVLLSFVTVNSPLRGGRTPSDLN 463
|||||||||||||||||||||||||||||||||||||||||||
Db 421 MLGDAASRSQVYSVAIVYGFLVLLSFVTVNSPLRGGRTPSDLN 463