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Database: UniProt/TrEMBL
Entry: Q0S508_RHOJR
LinkDB: Q0S508_RHOJR
Original site: Q0S508_RHOJR 
ID   Q0S508_RHOJR            Unreviewed;       446 AA.
AC   Q0S508;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   25-OCT-2017, entry version 72.
DE   SubName: Full=4-aminobutyrate transaminase {ECO:0000313|EMBL:ABG97378.1};
DE            EC=2.6.1.19 {ECO:0000313|EMBL:ABG97378.1};
GN   Name=gabT3 {ECO:0000313|EMBL:ABG97378.1};
GN   OrderedLocusNames=RHA1_ro05598 {ECO:0000313|EMBL:ABG97378.1};
OS   Rhodococcus jostii (strain RHA1).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=101510 {ECO:0000313|EMBL:ABG97378.1, ECO:0000313|Proteomes:UP000008710};
RN   [1] {ECO:0000313|Proteomes:UP000008710}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHA1 {ECO:0000313|Proteomes:UP000008710};
RX   PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA   McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M.,
RA   Fernandes C., Miyazawa D., Wong W., Lillquist A.L., Wang D.,
RA   Dosanjh M., Hara H., Petrescu A., Morin R.D., Yang G., Stott J.M.,
RA   Schein J.E., Shin H., Smailus D., Siddiqui A.S., Marra M.A.,
RA   Jones S.J.M., Holt R., Brinkman F.S.L., Miyauchi K., Fukuda M.,
RA   Davies J.E., Mohn W.W., Eltis L.D.;
RT   "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT   catabolic powerhouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; CP000431; ABG97378.1; -; Genomic_DNA.
DR   RefSeq; WP_005238605.1; NC_008268.1.
DR   ProteinModelPortal; Q0S508; -.
DR   STRING; 101510.RHA1_ro05598; -.
DR   PRIDE; Q0S508; -.
DR   EnsemblBacteria; ABG97378; ABG97378; RHA1_ro05598.
DR   GeneID; 4223149; -.
DR   KEGG; rha:RHA1_ro05598; -.
DR   PATRIC; fig|101510.16.peg.5643; -.
DR   eggNOG; ENOG4108JPW; Bacteria.
DR   eggNOG; COG0160; LUCA.
DR   HOGENOM; HOG000020206; -.
DR   KO; K07250; -.
DR   OMA; RVGNYLT; -.
DR   OrthoDB; POG091H0APS; -.
DR   Proteomes; UP000008710; 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; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 2.
DR   InterPro; IPR004632; 4NH2But_aminotransferase_bac.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR00700; GABAtrnsam; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:ABG97378.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008710};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008710};
KW   Transferase {ECO:0000313|EMBL:ABG97378.1}.
SQ   SEQUENCE   446 AA;  46901 MW;  CBD41E22F5D21E52 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 LAAIDSMRKF DLPARAQHIG DLALPRLKAL
     AADVGVIGDV RGRGAMLAME FVKPGTDEPD AELTKAIAAH ALEQGVILLT CGTYGNVIRL
     LPPLVISDDL LDDALTVIEQ IVRSLV
//
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