ID C1AWY7_RHOOB Unreviewed; 446 AA.
AC C1AWY7;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 88.
DE SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:BAH53910.1};
DE EC=2.6.1.19 {ECO:0000313|EMBL:BAH53910.1};
GN Name=gabT {ECO:0000313|EMBL:BAH53910.1};
GN OrderedLocusNames=ROP_56630 {ECO:0000313|EMBL:BAH53910.1};
OS Rhodococcus opacus (strain B4).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH53910.1, ECO:0000313|Proteomes:UP000002212};
RN [1] {ECO:0000313|EMBL:BAH53910.1, ECO:0000313|Proteomes:UP000002212}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4 {ECO:0000313|EMBL:BAH53910.1,
RC ECO:0000313|Proteomes:UP000002212};
RA Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT PR4 and Rhodococcus opacus B4.";
RL Submitted (MAR-2009) 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; AP011115; BAH53910.1; -; Genomic_DNA.
DR RefSeq; WP_015889408.1; NC_012522.1.
DR AlphaFoldDB; C1AWY7; -.
DR STRING; 632772.ROP_56630; -.
DR KEGG; rop:ROP_56630; -.
DR PATRIC; fig|632772.20.peg.5913; -.
DR HOGENOM; CLU_016922_10_0_11; -.
DR OMA; GAIETMK; -.
DR OrthoDB; 9801052at2; -.
DR Proteomes; UP000002212; 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; 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; ORNITHINE AMINOTRANSFERASE; 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:BAH53910.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:BAH53910.1}.
SQ SEQUENCE 446 AA; 46942 MW; 9693A8F5884DFB81 CRC64;
MNDIQYRLPQ KRALVTELPG PKSAALTARR RATVAAGVGS SVPVYAADAD GGVVVDVDGN
SLIDLGSGIA VTSVGASDPA VAEAVREQVG HFTHTCFMVT PYEGYVRVAE ELAALTPGDH
EKRTVLFNSG AEAVENAIKV ARLATGRDAV VAFDHAYHGR TNLTMALTAK SMPYKAHFGP
FAPEVYRLPM SYPYRDQDGL TGEQAAQRAI SQMEKQIGAD SLAAIIIEPI QGEGGFIVPA
EGFLPTLVNW ARANGVVFIA DEVQTGFSRT GAWFACEHEE IVPDIITMAK GMAGGMPLSA
ITGRAELLDK VHPGGLGGTY GGNPVACAAA LAALDSMRKF DLPARAQHIG DTVLPRLRAL
AAEVEVIGDV RGRGAMLAME FVKPGTNEPD AELTKAIAAH ALAQGVILLT CGTYGNVIRL
LPPLVIGDDL LDDALTVIEQ IVRSLV
//