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Y612_SHEFN
ID   Y612_SHEFN              Reviewed;         226 AA.
AC   Q087U3;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=PKHD-type hydroxylase Sfri_0612 {ECO:0000255|HAMAP-Rule:MF_00657};
DE            EC=1.14.11.- {ECO:0000255|HAMAP-Rule:MF_00657};
GN   OrderedLocusNames=Sfri_0612;
OS   Shewanella frigidimarina (strain NCIMB 400).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318167;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCIMB 400;
RG   US DOE Joint Genome Institute;
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   Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., Nealson K.H.,
RA   Newman D., Tiedje J.M., Zhou J., Romine M.F., Culley D.E., Serres M.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT   "Complete sequence of Shewanella frigidimarina NCIMB 400.";
RL   Submitted (AUG-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; CP000447; ABI70472.1; -; Genomic_DNA.
DR   RefSeq; WP_011636099.1; NC_008345.1.
DR   AlphaFoldDB; Q087U3; -.
DR   SMR; Q087U3; -.
DR   STRING; 318167.Sfri_0612; -.
DR   DNASU; 4278534; -.
DR   EnsemblBacteria; ABI70472; ABI70472; Sfri_0612.
DR   KEGG; sfr:Sfri_0612; -.
DR   eggNOG; COG3128; Bacteria.
DR   HOGENOM; CLU_106663_0_0_6; -.
DR   OMA; FPPLFNC; -.
DR   OrthoDB; 1139586at2; -.
DR   Proteomes; UP000000684; 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..226
FT                   /note="PKHD-type hydroxylase Sfri_0612"
FT                   /id="PRO_0000346519"
FT   DOMAIN          77..177
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00657"
FT   BINDING         95
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00657"
FT   BINDING         97
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00657"
FT   BINDING         158
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00657"
FT   BINDING         168
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00657"
SQ   SEQUENCE   226 AA;  25332 MW;  825DBB57E7275476 CRC64;
     MIVIEQILSK QDVGAYRQQL AECPWGDGRK TAMGMAASVK NNNQADAQHA NVRQLANQLL
     ARIGETPKIV SAALPHKIFP PCFNRYNETE EYGYHVDAAI MRIPNTSEVI RSDVSMTVFL
     SEPEEYDGGE LVIATEFGQQ QIKLPAGYAV VYPSSSLHKV TAVTRGQRIA AITWMQSMVA
     DVTLRQTLYQ LDQSIQNLIK ANNTDRAELD NLHNVYHNLI RQFTQL
 
 
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