ID SOR_PYRFU Reviewed; 124 AA. AC P82385; DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 27-MAR-2024, entry version 129. DE RecName: Full=Superoxide reductase; DE Short=SOR; DE EC=1.15.1.2; GN Name=sorA; OrderedLocusNames=PF1281; OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1). OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Pyrococcus. OX NCBI_TaxID=186497; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF N-TERMINUS, RP FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR. RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1; RX PubMed=10514376; DOI=10.1126/science.286.5438.306; RA Jenney F.E. Jr., Verhagen M.F.J.M., Cui X., Adams M.W.W.; RT "Anaerobic microbes: oxygen detoxification without superoxide dismutase."; RL Science 286:306-309(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1; RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299; RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., RA DiRuggiero J., Robb F.T.; RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. RT horikoshii inferred from complete genomic sequences."; RL Genetics 152:1299-1305(1999). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS). RX PubMed=10704199; DOI=10.1021/bi992428k; RA Yeh A.P., Hu Y., Jenney F.E. Jr., Adams M.W.W., Rees D.C.; RT "Structures of the superoxide reductase from Pyrococcus furiosus in the RT oxidized and reduced states."; RL Biochemistry 39:2499-2508(2000). 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:0000269|PubMed:10514376}. 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:0000269|PubMed:10514376}; CC -!- COFACTOR: CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; CC Evidence={ECO:0000269|PubMed:10514376}; CC -!- SUBUNIT: Homotetramer. 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; AF156097; AAF03229.1; -; Genomic_DNA. DR EMBL; AE009950; AAL81405.1; -; Genomic_DNA. DR PIR; T44571; T44571. DR RefSeq; WP_011012425.1; NZ_CP023154.1. DR PDB; 1DO6; X-ray; 2.00 A; A/B=1-124. DR PDB; 1DQI; X-ray; 1.70 A; A/B/C/D=1-124. DR PDB; 1DQK; X-ray; 2.00 A; A/B/C/D=1-124. DR PDBsum; 1DO6; -. DR PDBsum; 1DQI; -. DR PDBsum; 1DQK; -. DR AlphaFoldDB; P82385; -. DR SMR; P82385; -. DR STRING; 186497.PF1281; -. DR PaxDb; 186497-PF1281; -. DR GeneID; 41713085; -. DR KEGG; pfu:PF1281; -. DR PATRIC; fig|186497.12.peg.1344; -. DR eggNOG; arCOG02146; Archaea. DR HOGENOM; CLU_118960_2_1_2; -. DR OrthoDB; 30725at2157; -. DR PhylomeDB; P82385; -. DR BRENDA; 1.15.1.2; 5243. DR EvolutionaryTrace; P82385; -. DR Proteomes; UP000001013; Chromosome. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0050605; F:superoxide reductase activity; IEA:UniProtKB-EC. DR CDD; cd03172; SORL_classII; 1. DR Gene3D; 2.60.40.730; SOR catalytic domain; 1. DR InterPro; IPR002742; Desulfoferrodoxin_Fe-bd_dom. DR InterPro; IPR036073; Desulfoferrodoxin_Fe-bd_dom_sf. DR NCBIfam; TIGR00332; neela_ferrous; 1. DR PANTHER; PTHR36541; SUPEROXIDE REDUCTASE-RELATED; 1. DR PANTHER; PTHR36541:SF1; SUPEROXIDE REDUCTASE-RELATED; 1. DR Pfam; PF01880; Desulfoferrodox; 1. DR SUPFAM; SSF49367; Superoxide reductase-like; 1. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Electron transport; Iron; KW Metal-binding; Oxidoreductase; Reference proteome; Transport. FT CHAIN 1..124 FT /note="Superoxide reductase" FT /id="PRO_0000140873" FT BINDING 14 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT BINDING 16 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT BINDING 41 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT BINDING 47 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT BINDING 111 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT BINDING 114 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT HELIX 2..5 FT /evidence="ECO:0007829|PDB:1DQI" FT TURN 11..13 FT /evidence="ECO:0007829|PDB:1DQK" FT STRAND 19..25 FT /evidence="ECO:0007829|PDB:1DQI" FT STRAND 28..35 FT /evidence="ECO:0007829|PDB:1DQI" FT STRAND 37..39 FT /evidence="ECO:0007829|PDB:1DQI" FT STRAND 44..47 FT /evidence="ECO:0007829|PDB:1DQI" FT STRAND 49..58 FT /evidence="ECO:0007829|PDB:1DQI" FT STRAND 65..72 FT /evidence="ECO:0007829|PDB:1DQI" FT STRAND 91..98 FT /evidence="ECO:0007829|PDB:1DQI" FT STRAND 103..111 FT /evidence="ECO:0007829|PDB:1DQI" FT TURN 112..114 FT /evidence="ECO:0007829|PDB:1DQI" FT STRAND 115..123 FT /evidence="ECO:0007829|PDB:1DQI" SQ SEQUENCE 124 AA; 14324 MW; EDD92C7E501C8048 CRC64; MISETIRSGD WKGEKHVPVI EYEREGELVK VKVQVGKEIP HPNTTEHHIR YIELYFLPEG ENFVYQVGRV EFTAHGESVN GPNTSDVYTE PIAYFVLKTK KKGKLYALSY CNIHGLWENE VTLE //