ID B5XPA6_KLEP3 Unreviewed; 220 AA.
AC B5XPA6;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=HAD hydrolase, family IA {ECO:0000313|EMBL:ACI06857.1};
GN OrderedLocusNames=KPK_1625 {ECO:0000313|EMBL:ACI06857.1};
OS Klebsiella pneumoniae (strain 342).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=507522 {ECO:0000313|EMBL:ACI06857.1, ECO:0000313|Proteomes:UP000001734};
RN [1] {ECO:0000313|EMBL:ACI06857.1, ECO:0000313|Proteomes:UP000001734}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=342 {ECO:0000313|EMBL:ACI06857.1,
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).
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DR EMBL; CP000964; ACI06857.1; -; Genomic_DNA.
DR AlphaFoldDB; B5XPA6; -.
DR KEGG; kpe:KPK_1625; -.
DR HOGENOM; CLU_045011_13_1_6; -.
DR BioCyc; KPNE507522:GI0B-1624-MONOMER; -.
DR Proteomes; UP000001734; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd07505; HAD_BPGM-like; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR041492; HAD_2.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR023198; PGP-like_dom2.
DR NCBIfam; TIGR01509; HAD-SF-IA-v3; 1.
DR PANTHER; PTHR46193; 6-PHOSPHOGLUCONATE PHOSPHATASE; 1.
DR PANTHER; PTHR46193:SF22; HEXITOL PHOSPHATASE B; 1.
DR Pfam; PF13419; HAD_2; 1.
DR PRINTS; PR00413; HADHALOGNASE.
DR SFLD; SFLDG01135; C1.5.6:_HAD__Beta-PGM__Phospha; 1.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:ACI06857.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
SQ SEQUENCE 220 AA; 24158 MW; 5465889512E4F458 CRC64;
MSMQAVIFDM DGVIIDSEAL WRQAQIDALA QWGATASVDE CETLTKGKRL DEIAGTWCRY
FQLDLDPQRL EAAILQRITG LIATEGEPMH GVHEALRYFR EAGYQIALAT SSSRQVIAAV
LNKLSLWHFF DVVCSADDEP RGKPHPAVYL TTLRKLNLNA SQCLVIEDSY NGFCAAQAAG
IPTAVVAEDS RQGRYQAAVG RYQTLPELLE ALNAEPTAVA
//