Y4677_PARDP
ID Y4677_PARDP Reviewed; 227 AA.
AC A1BB44;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=PKHD-type hydroxylase Pden_4677 {ECO:0000255|HAMAP-Rule:MF_00657};
DE EC=1.14.11.- {ECO:0000255|HAMAP-Rule:MF_00657};
GN OrderedLocusNames=Pden_4677;
OS Paracoccus denitrificans (strain Pd 1222).
OG Plasmid pPD1222.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Paracoccus.
OX NCBI_TaxID=318586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pd 1222;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA Richardson P.;
RT "Complete sequence of plasmid 1 of Paracoccus denitrificans PD1222.";
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; CP000491; ABL72738.1; -; Genomic_DNA.
DR RefSeq; WP_011750897.1; NC_008688.1.
DR AlphaFoldDB; A1BB44; -.
DR SMR; A1BB44; -.
DR STRING; 318586.Pden_4677; -.
DR PRIDE; A1BB44; -.
DR EnsemblBacteria; ABL72738; ABL72738; Pden_4677.
DR KEGG; pde:Pden_4677; -.
DR eggNOG; COG3128; Bacteria.
DR HOGENOM; CLU_106663_0_0_5; -.
DR OMA; VGCYHNL; -.
DR Proteomes; UP000000361; Plasmid pPD1222.
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; Plasmid;
KW Reference proteome; Vitamin C.
FT CHAIN 1..227
FT /note="PKHD-type hydroxylase Pden_4677"
FT /id="PRO_0000346496"
FT DOMAIN 78..178
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 159
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00657"
FT BINDING 169
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00657"
SQ SEQUENCE 227 AA; 25324 MW; 2F7AA3870E762416 CRC64;
MLITIPDLLT PEEVAYMRQI LEGTAWVDGR STAGDQAGKV KRNLQVPVDS PEARELGNIV
LRALGRSPVY SSAALPAHIL PPMFNRYDEG MTFGAHVDGS IRVVPGTGQR IRTDVSTTVF
LTPPEDYDGG ELVMHDTYGQ HSVKLPAGHA VVYPATSLHS VTPVTRGSRW ASFFWAQSMV
RDDWRRHMLY DLDMSIMRIR SMLPDDDPAV TGITAHYHNM IRHWAET
