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Database: UniProt/TrEMBL
Entry: A0A0E1CBV8_KLEPN
LinkDB: A0A0E1CBV8_KLEPN
Original site: A0A0E1CBV8_KLEPN 
ID   A0A0E1CBV8_KLEPN        Unreviewed;       430 AA.
AC   A0A0E1CBV8;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   28-FEB-2018, entry version 13.
DE   SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:AHM82708.1};
DE            EC=2.6.1.19 {ECO:0000313|EMBL:AHM82708.1};
DE            EC=2.6.1.22 {ECO:0000313|EMBL:AHM82708.1};
GN   ORFNames=KPNJ1_00302 {ECO:0000313|EMBL:AHM82708.1};
OS   Klebsiella pneumoniae 30660/NJST258_1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella.
OX   NCBI_TaxID=1420012 {ECO:0000313|EMBL:AHM82708.1, ECO:0000313|Proteomes:UP000019583};
RN   [1] {ECO:0000313|EMBL:AHM82708.1, ECO:0000313|Proteomes:UP000019583}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=30660/NJST258_1 {ECO:0000313|EMBL:AHM82708.1,
RC   ECO:0000313|Proteomes:UP000019583};
RX   PubMed=24639510; DOI=10.1073/pnas.1321364111;
RA   Deleo F.R., Chen L., Porcella S.F., Martens C.A., Kobayashi S.D.,
RA   Porter A.R., Chavda K.D., Jacobs M.R., Mathema B., Olsen R.J.,
RA   Bonomo R.A., Musser J.M., Kreiswirth B.N.;
RT   "Molecular dissection of the evolution of carbapenem-resistant
RT   multilocus sequence type 258 Klebsiella pneumoniae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:4988-4993(2014).
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; CP006923; AHM82708.1; -; Genomic_DNA.
DR   ProteinModelPortal; A0A0E1CBV8; -.
DR   EnsemblBacteria; AHM82708; AHM82708; KPNJ1_00302.
DR   KEGG; kpa:KPNJ1_00302; -.
DR   PATRIC; fig|1420012.3.peg.292; -.
DR   KO; K00823; -.
DR   Proteomes; UP000019583; Chromosome.
DR   GO; GO:0047298; F:(S)-3-amino-2-methylpropionate transaminase activity; IEA:UniProtKB-EC.
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; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
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:AHM82708.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000019583};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU003560};
KW   Transferase {ECO:0000313|EMBL:AHM82708.1}.
SQ   SEQUENCE   430 AA;  45879 MW;  2BBDE24A664F8171 CRC64;
     MTYTTGDSQV KSSELNQRRQ QATPRGVGVM CNYFVEKAEN ATLWDIEGNE VIDFAAGIAV
     LNTGHRHPKV VAAVADQLQA FTHTAYQIVP YESYVSLAER INDLAPIDGP AKTAFFTTGA
     EAVENAVKIA RAYTGRPGLI TFGGGFHGRT FMTMALTGKV APYKIGFGPF PGSVYHGVYP
     NAAHGVTTAD ALKSLERIFK ADIAPDQVAA IILEPIQGEG GFNVAPADFM QALRDLCDTH
     GILLIADEVQ TGFARTGKLF AMQHYEVKPD LMTMAKSLAG GFPLSGVVGR AEVMDAPAPG
     GLGGTYAGNP LAVAAAHAVL DVIAEEQLCQ RAEQLGSHLQ EVLNQARATC PAIVDVRGRG
     SMVAVEFNDP QTGEPSPEFT RLVQQKAQEN GLLLLSCGVY GNVIRFLYPL TIPDAQFSKA
     LDILARVLKS
//
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