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Database: UniProt/TrEMBL
Entry: A0A0E3VB79_RHOER
LinkDB: A0A0E3VB79_RHOER
Original site: A0A0E3VB79_RHOER 
ID   A0A0E3VB79_RHOER        Unreviewed;       454 AA.
AC   A0A0E3VB79;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   07-JUN-2017, entry version 10.
DE   SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:AKD95872.1};
DE            EC=2.6.1.19 {ECO:0000313|EMBL:AKD95872.1};
GN   ORFNames=XU06_03035 {ECO:0000313|EMBL:AKD95872.1};
OS   Rhodococcus erythropolis (Arthrobacter picolinophilus).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=1833 {ECO:0000313|EMBL:AKD95872.1, ECO:0000313|Proteomes:UP000033069};
RN   [1] {ECO:0000313|EMBL:AKD95872.1, ECO:0000313|Proteomes:UP000033069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 46869 {ECO:0000313|Proteomes:UP000033069};
RA   Ruckert C., Birmes F.S., Niewerth H., Muller C., Fetzner S.,
RA   Kalinowski J.;
RT   "Complete genome sequence of Rhodococcus erythropolis BG43 (DSM
RT   46869), a degrader of Pseudomonas aeruginosa quorum sensing
RT   molecules.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; CP011295; AKD95872.1; -; Genomic_DNA.
DR   RefSeq; WP_046377868.1; NZ_CP011295.1.
DR   EnsemblBacteria; AKD95872; AKD95872; XU06_03035.
DR   KEGG; reb:XU06_03035; -.
DR   PATRIC; fig|1833.80.peg.611; -.
DR   KO; K07250; -.
DR   Proteomes; UP000033069; Chromosome.
DR   GO; GO:0003867; F:4-aminobutyrate 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; -; 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_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:AKD95872.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000033069};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU003560};
KW   Transferase {ECO:0000313|EMBL:AKD95872.1}.
SQ   SEQUENCE   454 AA;  47435 MW;  F451E6D331F1F318 CRC64;
     MSAIEYRLPQ ERRIVTEFPG PRSAALAERR KKVVGAGVAS ILPVYVADAD GGVIVDVDGN
     SLIDLGAGIA VTSVGASNPA VVSAVQDQVA HFTHTCFMVA PYEGYVEVAE RLAELTPGDH
     EKRSVLFNSG AEAVENAVKI ARHATGRDAV VVFDHAYHGR TNLTMALTSK SMPYKSGFGP
     FAPEVYRVPM SYPYREGLNV DGSKITGEQA AQRAITMIEK QVGAANTAAI LIEPIQGEGG
     FIVPAEGFLP TLVAWAKENG VVFIADEVQA GFARTGAWFA SDHEGIVPDL VTLAKGIAGG
     MPLAAVTGRA ELIDAVHPGG LGGTYGGNPV ACAAALASID QMRELDLCGR ARTIESTVVG
     RMNALAKELD VIGDVRGRGA MLAIELVKPG GQEPDADITK KIAAECLAAG VVILTCGTYG
     NVIRLLPPLV ISEELLDDAL TVLETAIRTA AQGN
//
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