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Database: UniProt/TrEMBL
Entry: B2GGI0_KOCRD
LinkDB: B2GGI0_KOCRD
Original site: B2GGI0_KOCRD 
ID   B2GGI0_KOCRD            Unreviewed;       447 AA.
AC   B2GGI0;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   07-JUN-2017, entry version 49.
DE   SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:BAG30296.1};
DE            EC=2.6.1.19 {ECO:0000313|EMBL:BAG30296.1};
GN   Name=gabT {ECO:0000313|EMBL:BAG30296.1};
GN   OrderedLocusNames=KRH_19490 {ECO:0000313|EMBL:BAG30296.1};
OS   Kocuria rhizophila (strain ATCC 9341 / DSM 348 / NBRC 103217 /
OS   DC2201).
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Kocuria.
OX   NCBI_TaxID=378753 {ECO:0000313|EMBL:BAG30296.1, ECO:0000313|Proteomes:UP000008838};
RN   [1] {ECO:0000313|EMBL:BAG30296.1, ECO:0000313|Proteomes:UP000008838}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9341 / DSM 348 / NBRC 103217 / DC2201
RC   {ECO:0000313|Proteomes:UP000008838};
RX   PubMed=18408034; DOI=10.1128/JB.01853-07;
RA   Takarada H., Sekine M., Kosugi H., Matsuo Y., Fujisawa T., Omata S.,
RA   Kishi E., Shimizu A., Tsukatani N., Tanikawa S., Fujita N.,
RA   Harayama S.;
RT   "Complete genome sequence of the soil actinomycete Kocuria
RT   rhizophila.";
RL   J. Bacteriol. 190:4139-4146(2008).
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; AP009152; BAG30296.1; -; Genomic_DNA.
DR   RefSeq; WP_012399017.1; NC_010617.1.
DR   ProteinModelPortal; B2GGI0; -.
DR   STRING; 378753.KRH_19490; -.
DR   EnsemblBacteria; BAG30296; BAG30296; KRH_19490.
DR   KEGG; krh:KRH_19490; -.
DR   eggNOG; ENOG4108JPW; Bacteria.
DR   eggNOG; COG0160; LUCA.
DR   HOGENOM; HOG000020206; -.
DR   KO; K07250; -.
DR   OMA; RVGNYLT; -.
DR   OrthoDB; POG091H0APS; -.
DR   Proteomes; UP000008838; 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:BAG30296.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008838};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008838};
KW   Transferase {ECO:0000313|EMBL:BAG30296.1}.
SQ   SEQUENCE   447 AA;  47075 MW;  0D251D8642406D8D CRC64;
     MAEIEYRLPQ KRELVTSIPG PKSQSLAERR AQTVAAGVAS SLPVFADELD GGVIKDVDGN
     QMVDLGSGIA VTSVGASNPK VVARVQDAVA KFTHTCFMVT PYEDYVAVGE KMAQLTPGSF
     DKRTALFTSG SEAVENAVKI ARVRTKRQAV VVFDHAYHGR TNLTMAMTAK VMPYKQGFGP
     FANEVYRVPM SYPFRDPEGM TGTEAAKRAL TMVEKQVGAE NVAAVVIEPI QGEGGFIVPA
     EGFLPALSSW CRENGAVFVA DEVQAGIART GAWFASEHEG VEPDLVTFAK GIAGGMPLSG
     VVGRAEIMDA VHPGGLGGTY GGNPVACAAA LGALEAIEEW DLVARAQEIE KVIREELGSV
     AESSPVVGDL RGRGAMIALE FVKPGTTEPN PDAAKQIAAR CLEQGVAILT CGTYGNIVRL
     LPPLVIDMDL LRDALGVFAA AIQEVGA
//
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