Y717_SHESA
ID Y717_SHESA Reviewed; 224 AA.
AC A0KT36;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=PKHD-type hydroxylase Shewana3_0717 {ECO:0000255|HAMAP-Rule:MF_00657};
DE EC=1.14.11.- {ECO:0000255|HAMAP-Rule:MF_00657};
GN OrderedLocusNames=Shewana3_0717;
OS Shewanella sp. (strain ANA-3).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=94122;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANA-3;
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 Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Newman D.,
RA Salticov C., Konstantinidis K., Klappenback J., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Shewanella sp. ANA-3.";
RL Submitted (SEP-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; CP000469; ABK46955.1; -; Genomic_DNA.
DR RefSeq; WP_011715881.1; NC_008577.1.
DR AlphaFoldDB; A0KT36; -.
DR SMR; A0KT36; -.
DR STRING; 94122.Shewana3_0717; -.
DR EnsemblBacteria; ABK46955; ABK46955; Shewana3_0717.
DR KEGG; shn:Shewana3_0717; -.
DR eggNOG; COG3128; Bacteria.
DR HOGENOM; CLU_106663_0_0_6; -.
DR OMA; FPPLFNC; -.
DR OrthoDB; 1139586at2; -.
DR Proteomes; UP000002589; 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..224
FT /note="PKHD-type hydroxylase Shewana3_0717"
FT /id="PRO_1000061740"
FT DOMAIN 78..176
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 157
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00657"
FT BINDING 167
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00657"
SQ SEQUENCE 224 AA; 25248 MW; A7BC10B5F3106591 CRC64;
MLIEIPNVFS KEEVNQLREQ LDARTWIDGN QTSGVMASTR KRNQQLDKDD PVALQIGELI
MARLLAHPLF VSAALPLQFY PPLFNRYQGG ETFGYHIDNA IRSTSEGMVR TDLSATLFLS
EPDTYQGGEL VIQDTYGQQS IKLAAGSLVL YPSTSLHQVT PVTSGERTAA FMWLQSMVRD
EGQRRLLFQL DQSIQSLTAQ AAPEQELFNL TGVYHNLLRR WSEL
