SOR_THEKO
ID SOR_THEKO Reviewed; 115 AA.
AC Q5JF09;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Superoxide reductase;
DE Short=SOR;
DE EC=1.15.1.2;
GN Name=sorA; OrderedLocusNames=TK0525;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
CC -!- FUNCTION: Uses electrons from reduced NADP, by way of rubredoxin and an
CC oxidoreductase, to catalyze the reduction of superoxide to hydrogen
CC peroxide. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + reduced [rubredoxin] + superoxide = H2O2 + oxidized
CC [rubredoxin]; Xref=Rhea:RHEA:21324, Rhea:RHEA-COMP:10302, Rhea:RHEA-
CC COMP:10303, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:18421,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.15.1.2;
CC Evidence={ECO:0000250|UniProtKB:P82385};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the desulfoferrodoxin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP006878; BAD84714.1; -; Genomic_DNA.
DR RefSeq; WP_011249480.1; NC_006624.1.
DR AlphaFoldDB; Q5JF09; -.
DR SMR; Q5JF09; -.
DR STRING; 69014.TK0525; -.
DR PRIDE; Q5JF09; -.
DR EnsemblBacteria; BAD84714; BAD84714; TK0525.
DR GeneID; 3235372; -.
DR KEGG; tko:TK0525; -.
DR PATRIC; fig|69014.16.peg.515; -.
DR eggNOG; arCOG02146; Archaea.
DR HOGENOM; CLU_118960_2_1_2; -.
DR InParanoid; Q5JF09; -.
DR OMA; HHIAWIE; -.
DR OrthoDB; 106274at2157; -.
DR PhylomeDB; Q5JF09; -.
DR Proteomes; UP000000536; Chromosome.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0050605; F:superoxide reductase activity; IEA:UniProtKB-EC.
DR Gene3D; 2.60.40.730; -; 1.
DR InterPro; IPR002742; Desulfoferrodoxin_Fe-bd_dom.
DR InterPro; IPR036073; Desulfoferrodoxin_Fe-bd_dom_sf.
DR Pfam; PF01880; Desulfoferrodox; 1.
DR SUPFAM; SSF49367; SSF49367; 1.
DR TIGRFAMs; TIGR00332; neela_ferrous; 1.
PE 3: Inferred from homology;
KW Electron transport; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome; Transport.
FT CHAIN 1..115
FT /note="Superoxide reductase"
FT /id="PRO_0000140875"
FT BINDING 14
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 16
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 41
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 47
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
SQ SEQUENCE 115 AA; 13265 MW; DC2F6D2F1F4FAB7E CRC64;
MLSQTIKSGD WKGEKHVPVI EYEKEGDLVK VEVSVGKEIP HPNTPEHHIA WIQLWFHPED
GAFPILVGKV EFSNHTDPLT EPRAVFFFRT QKKGKLYALS YCNIHGLWEN EVTLE