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Database: UniProt/TrEMBL
Entry: C1AWY7_RHOOB
LinkDB: C1AWY7_RHOOB
Original site: C1AWY7_RHOOB 
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}.
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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
//
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