ID YBIX_ESCF3 Reviewed; 225 AA.
AC B7LJV5;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 01-MAY-2013, entry version 32.
DE RecName: Full=PKHD-type hydroxylase YbiX;
DE EC=1.14.11.-;
GN Name=ybiX; OrderedLocusNames=EFER_2304;
OS Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CDC 0568-73).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585054;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35469 / DSM 13698 / CDC 0568-73;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A.,
RA Chiapello H., Clermont O., Cruveiller S., Danchin A., Diard M.,
RA Dossat C., Karoui M.E., Frapy E., Garry L., Ghigo J.M., Gilles A.M.,
RA Johnson J., Le Bouguenec C., Lescat M., Mangenot S.,
RA Martinez-Jehanne V., Matic I., Nassif X., Oztas S., Petit M.A.,
RA Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., Vacherie B.,
RA Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
CC -!- COFACTOR: Binds 1 Fe(2+) ion per subunit (By similarity).
CC -!- COFACTOR: Ascorbate (By similarity).
CC -!- SIMILARITY: Contains 1 Fe2OG dioxygenase domain.
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DR EMBL; CU928158; CAQ89805.1; -; Genomic_DNA.
DR RefSeq; YP_002383420.1; NC_011740.1.
DR ProteinModelPortal; B7LJV5; -.
DR STRING; 585054.EFER_2304; -.
DR PRIDE; B7LJV5; -.
DR EnsemblBacteria; CAQ89805; CAQ89805; EFER_2304.
DR GeneID; 7123629; -.
DR KEGG; efe:EFER_2304; -.
DR PATRIC; 32128954; VBIEscFer122920_2220.
DR eggNOG; COG3128; -.
DR HOGENOM; HOG000236239; -.
DR KO; K07336; -.
DR ProtClustDB; PRK05467; -.
DR BioCyc; EFER585054:GJJM-2297-MONOMER; -.
DR GO; GO:0005506; F:iron ion binding; IEA:HAMAP.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0016706; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors; IEA:HAMAP.
DR GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:UniProtKB-KW.
DR HAMAP; MF_00657; Hydroxyl_YbiX; 1; -.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR023550; PKHD_hydroxylase.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR SMART; SM00702; P4Hc; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 3: Inferred from homology;
KW Complete proteome; Dioxygenase; Iron; Metal-binding; Oxidoreductase;
KW Vitamin C.
FT CHAIN 1 225 PKHD-type hydroxylase YbiX.
FT /FTId=PRO_1000131214.
FT DOMAIN 78 177 Fe2OG dioxygenase.
FT METAL 96 96 Iron (By similarity).
FT METAL 98 98 Iron (By similarity).
FT METAL 158 158 Iron (By similarity).
FT BINDING 168 168 2-oxoglutarate (Potential).
SQ SEQUENCE 225 AA; 25460 MW; AA5CF7C327535E9C CRC64;
MMYHIPGVLS PKDVARFREQ LEQAEWVDGR VTTGAQGAQV KNNQQVDTRS ALYAALQNEV
LNAVNQHALF FAAALPRTLS TPLFNRYQNN ETYGFHVDGA VRSHPQNGWM RTDLSATLFL
SDPQSYDGGE LVVNDTFGQH RVKLPAGDLV LYPSSSLHCV TPVTRGVRVA SFMWIQSMIR
DDKKRAMLFE LDTNIQSLKS RHGESEEILS LLNLYHNLLR EWSEI
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