ID A0A1L9VTU1_ASPGL Unreviewed; 495 AA.
AC A0A1L9VTU1;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=ASPGLDRAFT_1158824 {ECO:0000313|EMBL:OJJ87312.1};
OS Aspergillus glaucus CBS 516.65.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Aspergillus.
OX NCBI_TaxID=1160497 {ECO:0000313|EMBL:OJJ87312.1, ECO:0000313|Proteomes:UP000184300};
RN [1] {ECO:0000313|Proteomes:UP000184300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 516.65 {ECO:0000313|Proteomes:UP000184300};
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
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; KV878891; OJJ87312.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L9VTU1; -.
DR STRING; 1160497.A0A1L9VTU1; -.
DR VEuPathDB; FungiDB:ASPGLDRAFT_1158824; -.
DR OrthoDB; 177625at2759; -.
DR Proteomes; UP000184300; Unassembled WGS sequence.
DR GO; GO:0034386; F:4-aminobutyrate:2-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009448; P:gamma-aminobutyric acid metabolic process; IEA:InterPro.
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.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000184300}.
SQ SEQUENCE 495 AA; 54809 MW; 23F62738236EB14A CRC64;
MSALRPGLKL RSFARLPAAR TLSTTPLRAA QPYFSNEPSG PTVSSAIPGP NNKKVAAELN
EVFDVRSLNM LTDYTKSIGN YISDLDGNTL LDVYAQIASI PVGYNNPHLE KVATSPEMIS
SLINRPALGN FPSAEWADVL KTGVLKVAPK GLNQVYTAMA GSDANEIAYK AAFMYRRQME
RGGPEADFSE QELESTMQNQ QPGSPQLSIL SFKSAFHGRL FGSLSTTRSK AIHKLDIPAF
DWPQATFPSL KYPLEEHAQE NAQEEQRCLQ EVERLIKEYH NPVAAVMVEP IQSEGGDNHA
SPAFFQGLRD ITQRTNVLFI VDEVQTGVGA TGKFWAHDHW NLQSPPDMVT FSKKAQTAGY
YYGNPALRPN KPYRQFNTWM GDPSRALIFR GIIEEIERLG LVENTAATGA YLYAGLERLS
QQYPQHFQNL RGKGQGTFIA WDSPKRDEIL AKAKSVGVNI GGSGQSAVRL RPMLIFQNHH
ADILLERLES VIKAL
//
