ID A0A0H3GYJ5_KLEPH Unreviewed; 421 AA.
AC A0A0H3GYJ5;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
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; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; 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).
RN [2] {ECO:0007829|PDB:6WJ8}
RP X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS).
RA Stogios P.J.;
RT "Crystal structure of gamma-aminobutyrate aminotransferase PuuE from
RT Klebsiella pneumoniae in complex with PLP.";
RL Submitted (APR-2020) to the PDB data bank.
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|ARBA:ARBA00008954,
CC 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 PDB; 6WJ8; X-ray; 2.59 A; A/B/C/D=1-421.
DR AlphaFoldDB; A0A0H3GYJ5; -.
DR SMR; A0A0H3GYJ5; -.
DR STRING; 1125630.KPHS_49790; -.
DR GeneID; 11850048; -.
DR KEGG; kpm:KPHS_49790; -.
DR PATRIC; fig|1125630.4.peg.4864; -.
DR HOGENOM; CLU_016922_10_0_6; -.
DR OMA; VMCGFYA; -.
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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR004632; 4NH2But_aminotransferase_bac.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR00700; GABAtrnsam; 1.
DR PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 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 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:6WJ8};
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW ECO:0000313|EMBL:AEW63677.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000007841};
KW Transferase {ECO:0000256|ARBA:ARBA00022576, 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
//