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Database: UniProt/TrEMBL
Entry: U9W589_NEUCR
LinkDB: U9W589_NEUCR
Original site: U9W589_NEUCR 
ID   U9W589_NEUCR            Unreviewed;       515 AA.
AC   U9W589;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=4-aminobutyrate aminotransferase {ECO:0000256|ARBA:ARBA00018543};
DE            EC=2.6.1.19 {ECO:0000256|ARBA:ARBA00012912};
DE   AltName: Full=GABA aminotransferase {ECO:0000256|ARBA:ARBA00031787};
DE   AltName: Full=Gamma-amino-N-butyrate transaminase {ECO:0000256|ARBA:ARBA00030204};
GN   ORFNames=NCU08998 {ECO:0000313|EMBL:ESA43414.1};
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110 {ECO:0000313|EMBL:ESA43414.1, ECO:0000313|Proteomes:UP000001805};
RN   [1] {ECO:0000313|EMBL:ESA43414.1, ECO:0000313|Proteomes:UP000001805}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987
RC   {ECO:0000313|Proteomes:UP000001805}, and OR74A
RC   {ECO:0000313|EMBL:ESA43414.1};
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.,
RA   FitzHugh W., Ma L.J., Smirnov S., Purcell S., Rehman B., Elkins T.,
RA   Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D.,
RA   Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P., Glass L., Orbach M.J., Berglund J.A., Voelker R., Yarden O.,
RA   Plamann M., Seiler S., Dunlap J., Radford A., Aramayo R., Natvig D.O.,
RA   Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S.,
RA   Lander E.S., Nusbaum C., Birren B.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
RN   [2] {ECO:0000313|EMBL:ESA43414.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=OR74A {ECO:0000313|EMBL:ESA43414.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Galagan J., Henn M.R., Hood H., Radford A., Collins R.A., Walker B.,
RA   Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A.,
RA   Allen A.W., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B., Chen Z.,
RA   Gainer-Dewar J., Gnerre S., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J.B., McCowan C., Murphy C.,
RA   Pearson M.D., Poon T.W., Priest M., Roberts A., Saif S., Shea T.D.,
RA   Sisk P., Shea T., Sykes S., Zucker J., Kodira C., Bowman B., Colot H.,
RA   Ebbole D., Rasmussen C., Baker C., Kalkman E., Chen C.-H., Shi M.,
RA   Mathur R., Lambreghts R., Collopy P., Mehra A., Schweredtfeger C., Hong C.,
RA   Belden W., Glass N.L., Borkovich K., Dunlap J., Lander E., Wortman J.,
RA   Nusbaum C., Sachs M., Birren B.;
RT   "The Genome Sequence of Neurospora crassa strain OR74A.";
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + 4-aminobutanoate = L-glutamate + succinate
CC         semialdehyde; Xref=Rhea:RHEA:23352, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:57706, ChEBI:CHEBI:59888; EC=2.6.1.19;
CC         Evidence={ECO:0000256|ARBA:ARBA00000442};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC       ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; CM002238; ESA43413.1; -; Genomic_DNA.
DR   EMBL; CM002238; ESA43414.1; -; Genomic_DNA.
DR   RefSeq; XP_011393979.1; XM_011395677.1.
DR   RefSeq; XP_011393980.1; XM_011395678.1.
DR   AlphaFoldDB; U9W589; -.
DR   STRING; 367110.U9W589; -.
DR   EnsemblFungi; ESA43413; ESA43413; NCU08998.
DR   EnsemblFungi; ESA43414; ESA43414; NCU08998.
DR   GeneID; 3875148; -.
DR   KEGG; ncr:NCU08998; -.
DR   VEuPathDB; FungiDB:NCU08998; -.
DR   InParanoid; U9W589; -.
DR   OrthoDB; 177625at2759; -.
DR   Proteomes; UP000001805; Chromosome 3, Linkage Group III.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0003867; F:4-aminobutyrate transaminase activity; IBA:GO_Central.
DR   GO; GO:0034386; F:4-aminobutyrate:2-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR   GO; GO:0009450; P:gamma-aminobutyric acid catabolic process; IBA:GO_Central.
DR   GO; GO:0006536; P:glutamate metabolic process; IEA:EnsemblFungi.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR004631; 4NH2But_aminotransferase_euk.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR049704; Aminotrans_3_PPA_site.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR00699; GABAtrns_euk; 1.
DR   PANTHER; PTHR43206:SF1; 4-AMINOBUTYRATE AMINOTRANSFERASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43206; AMINOTRANSFERASE; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW   ECO:0000313|EMBL:ESA43414.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001805};
KW   Transferase {ECO:0000256|ARBA:ARBA00022576, ECO:0000313|EMBL:ESA43414.1}.
SQ   SEQUENCE   515 AA;  56801 MW;  BCF4EFEE88713221 CRC64;
     MASRLLRSSY SGSLRAVSTA STVRPAAVSA VHQFSNRRQF TASSSKMASS FYKDWEPEGP
     TVKTEIPGPK AKEAIKELDE VFDTRSLNML TDYHKSVGNY IADPDGNVLL DVYAQIASIP
     IGYNNPVLQD AARSSDMVNS IINRPALGNF PPTDWASVLK TGILKVAPKG LNQVFTAMAG
     SDANETAYKA AFMWRRQKER GGPQVEFTAE EMESAMINQS PGASSLSILS FKSAFHGRLF
     GSLSTTRSKP IHKLDIPAFD WPQATFPLLK YPLEEHAEEN AAAEQAALDE VEHLIKNYHI
     PPAAVIIEPI QSEGGDNHAS PAFFRGLRAI TKKHGVLLIV DEVQTGVGAT GKFWAHEHWD
     LQDPPDMVTF SKKAQTAGYY FGNPELRPNK PYRQFNTWMG DPARALLFKA IIGEIERLGL
     VEHTARVGDY LYGKLEGLAQ KYPGQFANLR GKGQGTFIAF DNPRRDEFLA RAKKFGVNIG
     GSGQSAVRLR PMLIFEEKHA DILVDALEKI VKSFQ
//
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