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Y4660_CUPPJ
ID   Y4660_CUPPJ             Reviewed;         227 AA.
AC   Q46S75;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=PKHD-type hydroxylase Reut_B4660 {ECO:0000255|HAMAP-Rule:MF_00657};
DE            EC=1.14.11.- {ECO:0000255|HAMAP-Rule:MF_00657};
GN   OrderedLocusNames=Reut_B4660;
OS   Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS   (strain JMP 134)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=264198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMP134 / LMG 1197;
RX   PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA   Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA   Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA   Kyrpides N.C.;
RT   "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT   versatile pollutant degrader.";
RL   PLoS ONE 5:E9729-E9729(2010).
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; CP000091; AAZ64009.1; -; Genomic_DNA.
DR   RefSeq; WP_011300775.1; NC_007348.1.
DR   AlphaFoldDB; Q46S75; -.
DR   SMR; Q46S75; -.
DR   STRING; 264198.Reut_B4660; -.
DR   DNASU; 3614209; -.
DR   EnsemblBacteria; AAZ64009; AAZ64009; Reut_B4660.
DR   KEGG; reu:Reut_B4660; -.
DR   eggNOG; COG3128; Bacteria.
DR   HOGENOM; CLU_106663_0_0_4; -.
DR   OMA; FPPLFNC; -.
DR   OrthoDB; 1139586at2; -.
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..227
FT                   /note="PKHD-type hydroxylase Reut_B4660"
FT                   /id="PRO_0000346513"
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;  25215 MW;  6CCA7EB13DC868D1 CRC64;
     MMLQIPDVLS KAQVAQCRQM MDVADWTDGN ATSGHQSALA KRNMQLPEGS PVARQIGDLI
     QDALGANATF FSAALPLKVF PPLFNRYEGG QAFDNHVDNA IRYLRGTGFR VRSDLSATLF
     LTEPQDYDGG ELVIEDTYGQ HRVKLPAGYM VLYPATSLHH VTPVTRGARV SSFFWIQSMV
     RDEGQRALLF ELDTRIQQVA EEMGQKDSGV VGLTGVYHNL LRRWADA
 
 
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