ID B5XTM9_KLEP3 Unreviewed; 421 AA.
AC B5XTM9;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Putative 4-aminobutyrate transaminase {ECO:0000313|EMBL:ACI07595.1};
GN OrderedLocusNames=KPK_0288 {ECO:0000313|EMBL:ACI07595.1};
OS Klebsiella pneumoniae (strain 342).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=507522 {ECO:0000313|EMBL:ACI07595.1, ECO:0000313|Proteomes:UP000001734};
RN [1] {ECO:0000313|EMBL:ACI07595.1, ECO:0000313|Proteomes:UP000001734}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=342 {ECO:0000313|EMBL:ACI07595.1,
RC ECO:0000313|Proteomes:UP000001734};
RX PubMed=18654632; DOI=10.1371/journal.pgen.1000141;
RA Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H.,
RA Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y.,
RA Khouri H., Roesch L.F., Krogfelt K.A., Struve C., Triplett E.W.,
RA Methe B.A.;
RT "Complete genome sequence of the N2-fixing broad host range endophyte
RT Klebsiella pneumoniae 342 and virulence predictions verified in mice.";
RL PLoS Genet. 4:E1000141-E1000141(2008).
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; CP000964; ACI07595.1; -; Genomic_DNA.
DR AlphaFoldDB; B5XTM9; -.
DR KEGG; kpe:KPK_0288; -.
DR HOGENOM; CLU_016922_10_0_6; -.
DR BioCyc; KPNE507522:GI0B-288-MONOMER; -.
DR Proteomes; UP000001734; 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; IPR049704; Aminotrans_3_PPA_site.
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 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Transferase {ECO:0000256|ARBA:ARBA00022576}.
SQ SEQUENCE 421 AA; 44998 MW; 3A0B5D92843DD5A5 CRC64;
MKSSELNQRR QQATPRGVGV MCNYFVEKAE NATLWDIEGN EVIDFAAGIA VLNTGHRHPK
VVAAVADQLQ AFTHTAYQIV PYESYVSLAE RINDLAPIDG PAKTAFFTTG AEAVENAVKI
ARAYTGRPGL ITFGGGFHGR TFMTMALTGK VAPYKIGFGP FPGSVYHGVY PNEAHGVTTA
DALKSLERIF KADIAPDQVA AIILEPIQGE GGFNVAPADF MQALRDLCDT HGILLIADEV
QTGFARTGKL FAMQHYEVKP DLMTMAKSLA GGFPLSGVVG RAEVMDAPAP GGLGGTYAGN
PLAVAAAHAV LDVIAEEQLC QRAEQLGSHL QEVLNQARAT CPAIVDVRGR GSMVAVEFND
PQTGEPSPEF TRLVQQKAQE NGLLLLSCGV YGNVIRFLYP LTIPDAQFSK ALDILARILK
S
//
