ID   SOR_PYRHO               Reviewed;         115 AA.
AC   O58810;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2001, sequence version 2.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Superoxide reductase;
DE            Short=SOR;
DE            EC=1.15.1.2;
GN   Name=sorA; OrderedLocusNames=PH1083; ORFNames=PHCM016;
OS   Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS   100139 / OT-3).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=70601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX   PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA   Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA   Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA   Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA   Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA   Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT   "Complete sequence and gene organization of the genome of a hyper-
RT   thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL   DNA Res. 5:55-76(1998).
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   -!- SEQUENCE CAUTION:
CC       Sequence=BAA30182.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BA000001; BAA30182.1; ALT_INIT; Genomic_DNA.
DR   PIR; H71102; H71102.
DR   RefSeq; WP_048053298.1; NC_000961.1.
DR   PDB; 2HVB; X-ray; 2.50 A; A/B/C/D=1-115.
DR   PDBsum; 2HVB; -.
DR   AlphaFoldDB; O58810; -.
DR   SMR; O58810; -.
DR   STRING; 70601.3257499; -.
DR   EnsemblBacteria; BAA30182; BAA30182; BAA30182.
DR   GeneID; 1443405; -.
DR   KEGG; pho:PH1083; -.
DR   eggNOG; arCOG02146; Archaea.
DR   OMA; HHIAWIE; -.
DR   OrthoDB; 106274at2157; -.
DR   BRENDA; 1.15.1.2; 5244.
DR   EvolutionaryTrace; O58810; -.
DR   Proteomes; UP000000752; 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; Electron transport; Iron; Metal-binding; Oxidoreductase;
KW   Transport.
FT   CHAIN           1..115
FT                   /note="Superoxide reductase"
FT                   /id="PRO_0000140874"
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"
FT   HELIX           3..5
FT                   /evidence="ECO:0007829|PDB:2HVB"
FT   STRAND          19..25
FT                   /evidence="ECO:0007829|PDB:2HVB"
FT   STRAND          28..39
FT                   /evidence="ECO:0007829|PDB:2HVB"
FT   STRAND          44..47
FT                   /evidence="ECO:0007829|PDB:2HVB"
FT   STRAND          49..58
FT                   /evidence="ECO:0007829|PDB:2HVB"
FT   STRAND          65..72
FT                   /evidence="ECO:0007829|PDB:2HVB"
FT   STRAND          75..89
FT                   /evidence="ECO:0007829|PDB:2HVB"
FT   STRAND          94..102
FT                   /evidence="ECO:0007829|PDB:2HVB"
FT   TURN            103..105
FT                   /evidence="ECO:0007829|PDB:2HVB"
FT   STRAND          106..114
FT                   /evidence="ECO:0007829|PDB:2HVB"
SQ   SEQUENCE   115 AA;  13326 MW;  C25ADD9B24E4D1A9 CRC64;
     MLKETIRSGD WKGEKHVPVI EYEREGDLVK VEVSVGKEIP HPNTPEHHIA WIELYFHPEG
     GQFPILVGRV EFTNHSDPLT EPRAVFFFKT SKKGKLYALS YCNIHGLWEN EVQLE