Y559_GLUOX
ID Y559_GLUOX Reviewed; 227 AA.
AC Q5FTF9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=PKHD-type hydroxylase GOX0559 {ECO:0000255|HAMAP-Rule:MF_00657};
DE EC=1.14.11.- {ECO:0000255|HAMAP-Rule:MF_00657};
GN OrderedLocusNames=GOX0559;
OS Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Gluconobacter.
OX NCBI_TaxID=290633;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=621H;
RX PubMed=15665824; DOI=10.1038/nbt1062;
RA Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT oxydans.";
RL Nat. Biotechnol. 23:195-200(2005).
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; CP000009; AAW60337.1; -; Genomic_DNA.
DR RefSeq; WP_011252136.1; NZ_LT900338.1.
DR AlphaFoldDB; Q5FTF9; -.
DR SMR; Q5FTF9; -.
DR STRING; 290633.GOX0559; -.
DR EnsemblBacteria; AAW60337; AAW60337; GOX0559.
DR KEGG; gox:GOX0559; -.
DR eggNOG; COG3128; Bacteria.
DR HOGENOM; CLU_106663_0_0_5; -.
DR OMA; VGCYHNL; -.
DR Proteomes; UP000006375; 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 GOX0559"
FT /id="PRO_1000061720"
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; 25714 MW; 49D8A573E8259A0B CRC64;
MLLHIPNVLS PEEVRYFRDR LEDAEWTDGR VTAGEQSAKA KLNLQIPQDS AECRELGEFV
LRALGRNPTF NSAALPLRVY PPLFNRYDTG MHFDAHVDNA IRPIPGAGMR IRTDVSSTLF
LTGPDEYDGG ELVIQDTYGT QSVKLPAGDM VLYPSTSLHS VNRITRGSRW ASFFWSQSMV
RDDTKRRLLY EFDCSIIETR KALPDSHPAV LGLTSTYHNL LRQWAEL
