Y3084_VEREI
ID Y3084_VEREI Reviewed; 227 AA.
AC A1WMG0;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=PKHD-type hydroxylase Veis_3084 {ECO:0000255|HAMAP-Rule:MF_00657};
DE EC=1.14.11.- {ECO:0000255|HAMAP-Rule:MF_00657};
GN OrderedLocusNames=Veis_3084;
OS Verminephrobacter eiseniae (strain EF01-2).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Verminephrobacter.
OX NCBI_TaxID=391735;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EF01-2;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT "Complete sequence of chromosome 1 of Verminephrobacter eiseniae EF01-2.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000542; ABM58817.1; -; Genomic_DNA.
DR RefSeq; WP_011810812.1; NC_008786.1.
DR AlphaFoldDB; A1WMG0; -.
DR SMR; A1WMG0; -.
DR STRING; 391735.Veis_3084; -.
DR EnsemblBacteria; ABM58817; ABM58817; Veis_3084.
DR KEGG; vei:Veis_3084; -.
DR eggNOG; COG3128; Bacteria.
DR HOGENOM; CLU_106663_0_0_4; -.
DR OMA; VGCYHNL; -.
DR OrthoDB; 1139586at2; -.
DR Proteomes; UP000000374; 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; Reference proteome;
KW Vitamin C.
FT CHAIN 1..227
FT /note="PKHD-type hydroxylase Veis_3084"
FT /id="PRO_1000061745"
FT DOMAIN 78..179
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00657"
FT REGION 27..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 97
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00657"
FT BINDING 99
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00657"
FT BINDING 160
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00657"
FT BINDING 170
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00657"
SQ SEQUENCE 227 AA; 25719 MW; 79B2BE4B706A9351 CRC64;
MLLILADLLS PQELQTARQL LRNARWDDGK DSAGTQARQA KNNQQLPRDS EAGRRIAAMV
LAALERSALF LTATLPKRVF PPRVNRYGGE HNHYGDHVDS AVRQLADRHD RLRTDISCTV
FLSPPDEYDG GELCIDDTFG PQRVKLPAGH AVIYPGTSVH QVRPVTRGYR MACFFWVESL
VRSAEQRRLL YDMDMALLRL RQQHGESPET VALTGSYHNL LRMWADT
