SOR_PYRFU
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 03-AUG-2022, entry version 122.
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}.
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DR EMBL; AF156097; AAF03229.1; -; Genomic_DNA.
DR EMBL; AE009950; AAL81405.1; -; Genomic_DNA.
DR PIR; T44571; T44571.
DR RefSeq; WP_011012425.1; NC_018092.1.
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 PRIDE; P82385; -.
DR EnsemblBacteria; AAL81405; AAL81405; 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 OMA; HHIAWIE; -.
DR OrthoDB; 106274at2157; -.
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 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 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
