SOR_METJA
ID SOR_METJA Reviewed; 116 AA.
AC Q58151;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Putative superoxide reductase;
DE Short=SOR;
DE EC=1.15.1.2;
GN OrderedLocusNames=MJ0741;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
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; L77117; AAB98735.1; -; Genomic_DNA.
DR PIR; E64392; E64392.
DR RefSeq; WP_010870246.1; NC_000909.1.
DR AlphaFoldDB; Q58151; -.
DR SMR; Q58151; -.
DR STRING; 243232.MJ_0741; -.
DR EnsemblBacteria; AAB98735; AAB98735; MJ_0741.
DR GeneID; 1451618; -.
DR KEGG; mja:MJ_0741; -.
DR eggNOG; arCOG02146; Archaea.
DR HOGENOM; CLU_118960_2_1_2; -.
DR InParanoid; Q58151; -.
DR OMA; FEKKHTP; -.
DR OrthoDB; 106274at2157; -.
DR PhylomeDB; Q58151; -.
DR Proteomes; UP000000805; 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..116
FT /note="Putative superoxide reductase"
FT /id="PRO_0000140871"
FT BINDING 20
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 46
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 52
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
SQ SEQUENCE 116 AA; 13950 MW; 4CF2C76237DE0673 CRC64;
MTHYCGINRM KEGTDFEKKH TPFIECKDRV KANDYFEVKI STGIPHPMED NHFIHWIELY
MGDLYLARVD FTQFMKPEVK LMVKAPSKEH EKFILRALMR CNLHGVWEYE KEILLE