ID   Y3192_KLEP3             Reviewed;         225 AA.
AC   B5XT12;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=PKHD-type hydroxylase KPK_3192 {ECO:0000255|HAMAP-Rule:MF_00657};
DE            EC=1.14.11.- {ECO:0000255|HAMAP-Rule:MF_00657};
GN   OrderedLocusNames=KPK_3192;
OS   Klebsiella pneumoniae (strain 342).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=507522;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=342;
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.W., 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=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00657};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00657};
CC   -!- COFACTOR:
CC       Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00657};
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DR   EMBL; CP000964; ACI09681.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5XT12; -.
DR   SMR; B5XT12; -.
DR   EnsemblBacteria; ACI09681; ACI09681; KPK_3192.
DR   KEGG; kpe:KPK_3192; -.
DR   HOGENOM; CLU_106663_0_0_6; -.
DR   OMA; FPPLFNC; -.
DR   OrthoDB; 1139586at2; -.
DR   BioCyc; KPNE507522:GI0B-3178-MON; -.
DR   Proteomes; UP000001734; Chromosome.
DR   GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR   HAMAP; MF_00657; Hydroxyl_YbiX; 1.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   InterPro; IPR041097; PKHD_C.
DR   InterPro; IPR023550; PKHD_hydroxylase.
DR   InterPro; IPR006620; Pro_4_hyd_alph.
DR   InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR   PANTHER; PTHR41536; PTHR41536; 1.
DR   Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR   Pfam; PF18331; PKHD_C; 1.
DR   SMART; SM00702; P4Hc; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   3: Inferred from homology;
KW   Dioxygenase; Iron; Metal-binding; Oxidoreductase; Vitamin C.
FT   CHAIN           1..225
FT                   /note="PKHD-type hydroxylase KPK_3192"
FT                   /id="PRO_1000131215"
FT   DOMAIN          78..177
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00657"
FT   BINDING         96
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00657"
FT   BINDING         98
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00657"
FT   BINDING         158
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00657"
FT   BINDING         168
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00657"
SQ   SEQUENCE   225 AA;  25260 MW;  BB87BAA07D69CBF2 CRC64;
     MMYHIPDVLS ADQVAEFTRQ LAQAEWVDGR VTVGNQGAAV KQNQQIDTRT PLYARLQAAV
     LDALRGHPQF FSAALPRTIS APLFNRYGPG ETYGFHVDGA VRQNAEAGWM RTDLSATLFL
     CDPESYEGGE LVIEDTYGQH RVKLPAGHLV LYPASSLHCV TPVTHGVRQA SFLWIQSMVR
     DDKQRATLYD LDRTIQSLKA RFGDGEEVLS LLNMYHNLLR QWTEV