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Database: UniProt/TrEMBL
Entry: A0A0H3GYJ5_KLEPH
LinkDB: A0A0H3GYJ5_KLEPH
Original site: A0A0H3GYJ5_KLEPH 
ID   A0A0H3GYJ5_KLEPH        Unreviewed;       421 AA.
AC   A0A0H3GYJ5;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   07-JUN-2017, entry version 11.
DE   SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:AEW63677.1};
GN   OrderedLocusNames=KPHS_49790 {ECO:0000313|EMBL:AEW63677.1};
OS   Klebsiella pneumoniae subsp. pneumoniae (strain HS11286).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella.
OX   NCBI_TaxID=1125630 {ECO:0000313|EMBL:AEW63677.1, ECO:0000313|Proteomes:UP000007841};
RN   [1] {ECO:0000313|EMBL:AEW63677.1, ECO:0000313|Proteomes:UP000007841}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HS11286 {ECO:0000313|EMBL:AEW63677.1,
RC   ECO:0000313|Proteomes:UP000007841};
RX   PubMed=22408243; DOI=10.1128/JB.00043-12;
RA   Liu P., Li P., Jiang X., Bi D., Xie Y., Tai C., Deng Z., Rajakumar K.,
RA   Ou H.Y.;
RT   "Complete genome sequence of Klebsiella pneumoniae subsp. pneumoniae
RT   HS11286, a multidrug-resistant strain Isolated from human sputum.";
RL   J. Bacteriol. 194:1841-1842(2012).
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; CP003200; AEW63677.1; -; Genomic_DNA.
DR   RefSeq; WP_002920814.1; NC_016845.1.
DR   RefSeq; YP_005229279.1; NC_016845.1.
DR   ProteinModelPortal; A0A0H3GYJ5; -.
DR   EnsemblBacteria; AEW63677; AEW63677; KPHS_49790.
DR   GeneID; 11850048; -.
DR   KEGG; kpm:KPHS_49790; -.
DR   PATRIC; fig|1125630.4.peg.4864; -.
DR   KO; K00823; -.
DR   OMA; ICWRAFE; -.
DR   Proteomes; UP000007841; Chromosome.
DR   GO; GO:0003867; F:4-aminobutyrate transaminase activity; IEA:InterPro.
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:AEW63677.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007841};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU003560};
KW   Transferase {ECO:0000313|EMBL:AEW63677.1}.
SQ   SEQUENCE   421 AA;  44926 MW;  3B1F5D8016FDD5A5 CRC64;
     MKSSELNQRR QQATPRGVGV MCNYFVEKAE NATLWDIEGN EVIDFAAGIA VLNTGHRHPK
     VVAAVADQLQ AFTHTAYQIV PYESYVSLAE RINDLAPIDG PAKTAFFTTG AEAVENAVKI
     ARAYTGRPGL ITFGGGFHGR TFMTMALTGK VAPYKIGFGP FPGSVYHGVY PNAAHGVTTA
     DALKSLERIF KADIAPDQVA AIILEPIQGE GGFNVAPADF MQALRDLCDT HGILLIADEV
     QTGFARTGKL FAMQHYEVKP DLMTMAKSLA GGFPLSGVVG RAEVMDAPAP GGLGGTYAGN
     PLAVAAAHAV LDVIAEEQLC QRAEQLGSHL QEVLNQARAT CPAIVDVRGR GSMVAVEFND
     PQTGEPSPEF TRLVQQKAQE NGLLLLSCGV YGNVIRFLYP LTIPDAQFSK ALDILARVLK
     S
//
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