ID A0A0H3GXZ5_KLEPH Unreviewed; 461 AA.
AC A0A0H3GXZ5;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Diaminobutyrate--2-oxoglutarate aminotransferase {ECO:0000313|EMBL:AEW61454.1};
GN OrderedLocusNames=KPHS_27560 {ECO:0000313|EMBL:AEW61454.1};
OS Klebsiella pneumoniae subsp. pneumoniae (strain HS11286).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=1125630 {ECO:0000313|EMBL:AEW61454.1, ECO:0000313|Proteomes:UP000007841};
RN [1] {ECO:0000313|EMBL:AEW61454.1, ECO:0000313|Proteomes:UP000007841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HS11286 {ECO:0000313|EMBL:AEW61454.1,
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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR EMBL; CP003200; AEW61454.1; -; Genomic_DNA.
DR RefSeq; WP_004199985.1; NC_016845.1.
DR RefSeq; YP_005227056.1; NC_016845.1.
DR AlphaFoldDB; A0A0H3GXZ5; -.
DR STRING; 1125630.KPHS_27560; -.
DR GeneID; 11847774; -.
DR KEGG; kpm:KPHS_27560; -.
DR PATRIC; fig|1125630.4.peg.2677; -.
DR HOGENOM; CLU_016922_10_0_6; -.
DR Proteomes; UP000007841; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR004637; Dat.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR00709; dat; 1.
DR PANTHER; PTHR43552; DIAMINOBUTYRATE--2-OXOGLUTARATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR43552:SF1; DIAMINOBUTYRATE--2-OXOGLUTARATE AMINOTRANSFERASE; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:AEW61454.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000007841};
KW Transferase {ECO:0000313|EMBL:AEW61454.1}.
SQ SEQUENCE 461 AA; 49911 MW; 5761332E29412CAC CRC64;
MMTDKVRIDT LRADLLDANN ETFLARQAEF ESNVRSYPRK LPLAITKAEG VWLTDADNKQ
YLDCLAGAGT LALGHNHPDV LQSIQSVITS GLPLHTLDLT TPLKDRFSEY LLSCLPGEGK
EYCLQFTGPS GADAVEAALK LAKKYTGRTA VISFSGGYHG MTHGALSVTG NLSPKAAVNG
MMPEVQFMPY PHLYRCPLGI GGEAGVKALT YYFENLINDV ESGVRKPAAV ILEAVQGEGG
VNPAPVEWQQ RIRKVTEEHG ILLIVDEVQA GFARTGKFFA FEHAGIQPDI IVMSKAVGGG
LPLAVLGIKK QFDAWEPGHH TGTFRGNQLA MATGLTTLRH LRDNKIADKV AAQGEWLKGK
LAELQKRYPV IGHVRGLGLM IGIEIVKPNE AQDHMGCYPA DGELSALLQK KCFEAGLILE
RGGRHGCVLR LLPSLLISDA ELDVFLDKFE QALLAAGVKP V
//
