ID   GABAT_EMENI             Reviewed;         498 AA.
AC   P14010; C8VMU4; Q5BB32;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   27-MAR-2024, entry version 145.
DE   RecName: Full=4-aminobutyrate aminotransferase;
DE            EC=2.6.1.19;
DE   AltName: Full=GABA aminotransferase;
DE            Short=GABA-AT;
DE   AltName: Full=Gamma-amino-N-butyrate transaminase;
DE            Short=GABA transaminase;
GN   Name=gatA; ORFNames=AN2248;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MH 3010;
RX   PubMed=2505051; DOI=10.1007/bf00330950;
RA   Richardson I.B., Hurley S.K., Hynes M.J.;
RT   "Cloning and molecular characterisation of the amdR controlled gatA gene of
RT   Aspergillus nidulans.";
RL   Mol. Gen. Genet. 217:118-125(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
CC   -!- FUNCTION: Deaminates gamma-aminobutyric acid (GABA) to succinate-
CC       semialdehyde, which in turn is converted to succinate by the succinate
CC       semialdehyde dehydrogenase (By similarity). Required for the
CC       degradation of GABA, which is important for utilization of GABA as
CC       nitrogen source. {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:P17649};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O13837}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; X15647; CAA33674.1; -; Genomic_DNA.
DR   EMBL; AACD01000036; EAA63933.1; -; Genomic_DNA.
DR   EMBL; BN001307; CBF86462.1; -; Genomic_DNA.
DR   PIR; JQ0197; JQ0197.
DR   RefSeq; XP_659852.1; XM_654760.1.
DR   AlphaFoldDB; P14010; -.
DR   SMR; P14010; -.
DR   STRING; 227321.P14010; -.
DR   EnsemblFungi; CBF86462; CBF86462; ANIA_02248.
DR   GeneID; 2875488; -.
DR   KEGG; ani:AN2248.2; -.
DR   VEuPathDB; FungiDB:AN2248; -.
DR   eggNOG; KOG1405; Eukaryota.
DR   HOGENOM; CLU_016922_12_0_1; -.
DR   InParanoid; P14010; -.
DR   OMA; KTQVCGI; -.
DR   OrthoDB; 177625at2759; -.
DR   Proteomes; UP000000560; Chromosome VII.
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:0043605; P:amide catabolic process; IMP:AspGD.
DR   GO; GO:0009450; P:gamma-aminobutyric acid catabolic process; IMP:AspGD.
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; 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; Cytoplasm; Pyridoxal phosphate; Reference proteome;
KW   Transferase.
FT   CHAIN           1..498
FT                   /note="4-aminobutyrate aminotransferase"
FT                   /id="PRO_0000120379"
FT   BINDING         164..165
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000250|UniProtKB:P80147"
FT   BINDING         222
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P80147"
FT   BINDING         381
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:P80147"
FT   MOD_RES         356
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P80147"
SQ   SEQUENCE   498 AA;  55489 MW;  97013EF39D66D5E0 CRC64;
     MASAFRSSLK LRASARLPAV RTITTTPRLR AAEKPYFPNE PTAPKLATAI PGPKNKAASE
     QLNEVFDVRS LNMLADYTKS VGNYIADLDG NMLLDVYAQI ASIPVGYNNP HLLKVAASPE
     MATSLINRPA LGNFPSADWA HILKTGILKV APKGLDQVFT AMAGSDANET AYKAAFMYYR
     QQQRGGPEKE FTEEEIQSSM LNQTPGSPQL SIMSFKAGFH GRLFGSLSTT RSKPIHKLDI
     PAFDWPQAPF PSLKYPLEEH AKENAEEEQR CLQEAERLIK EWHNPVAAII VEPIQSEGGD
     NHASPAFFRG LREITKRNNV LFIVDEVQTG VGATGKFWAH DHWNLETPPD MVTFSKKAQT
     AGYYFGNPAL RPNKPYRQFN TWMGDPSRAL IFRGIIEEIE RLFLVENTAA TGDYLYSGLE
     RLAKQYPEHL QNLRGKGQGT FIAWDTPKRD EFLVKGKGVG INIGGSGQNA VRLRPMLIFQ
     KHHADILLES IEKIIKQL
//