ID A0A494SYF3_9NOCA Unreviewed; 452 AA.
AC A0A494SYF3;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=4-aminobutyrate--2-oxoglutarate transaminase {ECO:0000313|EMBL:AYJ51626.1};
DE EC=2.6.1.19 {ECO:0000313|EMBL:AYJ51626.1};
GN Name=gabT {ECO:0000313|EMBL:AYJ51626.1};
GN ORFNames=D8W71_07875 {ECO:0000313|EMBL:AYJ51626.1};
OS Rhodococcus sp. P1Y.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1302308 {ECO:0000313|EMBL:AYJ51626.1, ECO:0000313|Proteomes:UP000277147};
RN [1] {ECO:0000313|Proteomes:UP000277147}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1Y {ECO:0000313|Proteomes:UP000277147};
RA Belimov A., Safronova V.I., Ismailov T.;
RT "Complete genome sequence of the abscisic acid utilizing strain Rhodococcus
RT sp. P1Y.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000277147}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1Y {ECO:0000313|Proteomes:UP000277147};
RA Nikolaichik Y.A., Gogoleva N.E., Khlopko Y.A., Gogolev Y.V.;
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP032762; AYJ51626.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A494SYF3; -.
DR KEGG; rhop:D8W71_07875; -.
DR OrthoDB; 9801052at2; -.
DR Proteomes; UP000277147; Chromosome.
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; IPR004632; 4NH2But_aminotransferase_bac.
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; TIGR00700; GABAtrnsam; 1.
DR PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR PANTHER; PTHR11986:SF58; LEUCINE_METHIONINE RACEMASE; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:AYJ51626.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000277147};
KW Transferase {ECO:0000313|EMBL:AYJ51626.1}.
SQ SEQUENCE 452 AA; 47641 MW; 1C3413FDF4553C60 CRC64;
MKDIHYRLPQ HRALVTELPG PASTALTARR RAAVAAGVGS SVPVYTADAD GGVIVDVDGN
SLVDLGSGIA VTSVGASDPA VVEAVREQVG HFTHTCFMVT PYEGYVRVAE ELAALTPGDH
EKRTVLFNSG AEAVENAVKV ARLATGRDAI VAFDHAYHGR TNLTMALTAK SMPYKAHFGP
FAPEVYRLPM SYPYRDADGL SGEQAAQRAI DQMEKQIGAD SLAAIIIEPI QGEGGFIVPA
DGFLPTLATW AREHGVVFIA DEVQTGFCRT GSWFASDHEG IVPDIITMAK GMAGGMPLSA
ITGRADLLDK VHPGGLGGTY GGNPVACAAA LAAIDTMREY DLPARARRIE GLVLPRLRAL
ADEVGVIGDI RGRGAMLAME FVQPGTDKPD PELTKAIAAG ALTQGVIVLT CGTYGNVIRL
LPPLVIGDEL LDDALTVIEE TVRSLVREKS LV
//
