ID   SOR_THEMA               Reviewed;         131 AA.
AC   Q9WZC6;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Putative superoxide reductase;
DE            Short=SOR;
DE            EC=1.15.1.2;
GN   OrderedLocusNames=TM_0658;
OS   Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS   / MSB8).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=243274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX   PubMed=10360571; DOI=10.1038/20601;
RA   Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA   Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA   Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA   Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA   Smith H.O., Venter J.C., Fraser C.M.;
RT   "Evidence for lateral gene transfer between Archaea and Bacteria from
RT   genome sequence of Thermotoga maritima.";
RL   Nature 399:323-329(1999).
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   -!- SIMILARITY: Belongs to the desulfoferrodoxin family. {ECO:0000305}.
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DR   EMBL; AE000512; AAD35742.1; -; Genomic_DNA.
DR   PIR; G72348; G72348.
DR   RefSeq; NP_228467.1; NC_000853.1.
DR   RefSeq; WP_004081116.1; NZ_CP011107.1.
DR   PDB; 2AMU; X-ray; 2.00 A; A=1-131.
DR   PDB; 3QZB; X-ray; 1.10 A; A=1-131.
DR   PDBsum; 2AMU; -.
DR   PDBsum; 3QZB; -.
DR   AlphaFoldDB; Q9WZC6; -.
DR   SMR; Q9WZC6; -.
DR   STRING; 243274.THEMA_01375; -.
DR   EnsemblBacteria; AAD35742; AAD35742; TM_0658.
DR   KEGG; tma:TM0658; -.
DR   eggNOG; COG2033; Bacteria.
DR   InParanoid; Q9WZC6; -.
DR   OMA; HHIAWIE; -.
DR   OrthoDB; 1496450at2; -.
DR   BRENDA; 1.15.1.2; 6331.
DR   EvolutionaryTrace; Q9WZC6; -.
DR   Proteomes; UP000008183; 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   Reference proteome; Transport.
FT   CHAIN           1..131
FT                   /note="Putative superoxide reductase"
FT                   /id="PRO_0000140876"
FT   BINDING         15
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         17
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         45
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         51
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         115
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         118
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   HELIX           3..6
FT                   /evidence="ECO:0007829|PDB:3QZB"
FT   TURN            12..14
FT                   /evidence="ECO:0007829|PDB:3QZB"
FT   STRAND          19..22
FT                   /evidence="ECO:0007829|PDB:3QZB"
FT   STRAND          25..27
FT                   /evidence="ECO:0007829|PDB:3QZB"
FT   STRAND          32..43
FT                   /evidence="ECO:0007829|PDB:3QZB"
FT   STRAND          48..51
FT                   /evidence="ECO:0007829|PDB:3QZB"
FT   STRAND          53..62
FT                   /evidence="ECO:0007829|PDB:3QZB"
FT   STRAND          69..75
FT                   /evidence="ECO:0007829|PDB:3QZB"
FT   STRAND          95..102
FT                   /evidence="ECO:0007829|PDB:3QZB"
FT   STRAND          107..115
FT                   /evidence="ECO:0007829|PDB:3QZB"
FT   TURN            116..118
FT                   /evidence="ECO:0007829|PDB:3QZB"
FT   STRAND          119..129
FT                   /evidence="ECO:0007829|PDB:3QZB"
SQ   SEQUENCE   131 AA;  14935 MW;  C5380BF586F124CE CRC64;
     MKLSDFIKTE DFKKEKHVPV IEAPEKVKKD EKVQIVVTVG KEIPHPNTTE HHIRWIKVFF
     QPDGDPYVYE VGRYEFNAHG ESVQGPNIGA VYTEPTVTTV VKLNRSGTII ALSYCNIHGL
     WESSQKITVE E