GABAT_EMENI
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 03-AUG-2022, entry version 138.
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; 162425.CADANIAP00008938; -.
DR EnsemblFungi; CBF86462; CBF86462; ANIA_02248.
DR EnsemblFungi; EAA63933; EAA63933; AN2248.2.
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; DPPDMVT; -.
DR OrthoDB; 566705at2759; -.
DR Proteomes; UP000000560; Chromosome VII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
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:cellular 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; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 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 Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR00699; GABAtrns_euk; 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
