SOR_ARCFU
ID SOR_ARCFU Reviewed; 125 AA.
AC O29903;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Putative superoxide reductase;
DE Short=SOR;
DE EC=1.15.1.2;
GN OrderedLocusNames=AF_0344;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
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; AE000782; AAB90892.1; -; Genomic_DNA.
DR PIR; H69292; H69292.
DR RefSeq; WP_010877851.1; NC_000917.1.
DR PDB; 4BFF; X-ray; 2.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=1-125.
DR PDB; 4BFJ; X-ray; 2.80 A; A/B=1-125.
DR PDB; 4BFK; X-ray; 2.10 A; A/B/C/D=1-125.
DR PDB; 4BGL; X-ray; 1.90 A; A/B/C/D=1-125.
DR PDB; 4C4B; X-ray; 2.50 A; A/B=1-125.
DR PDB; 4C4U; X-ray; 2.58 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=1-125.
DR PDBsum; 4BFF; -.
DR PDBsum; 4BFJ; -.
DR PDBsum; 4BFK; -.
DR PDBsum; 4BGL; -.
DR PDBsum; 4C4B; -.
DR PDBsum; 4C4U; -.
DR AlphaFoldDB; O29903; -.
DR SMR; O29903; -.
DR STRING; 224325.AF_0344; -.
DR EnsemblBacteria; AAB90892; AAB90892; AF_0344.
DR GeneID; 24793883; -.
DR KEGG; afu:AF_0344; -.
DR eggNOG; arCOG02146; Archaea.
DR HOGENOM; CLU_118960_2_1_2; -.
DR OMA; HHIAWIE; -.
DR OrthoDB; 106274at2157; -.
DR PhylomeDB; O29903; -.
DR BRENDA; 1.15.1.1; 414.
DR BRENDA; 1.15.1.2; 414.
DR Proteomes; UP000002199; 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..125
FT /note="Putative superoxide reductase"
FT /id="PRO_0000140870"
FT BINDING 12
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 14
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 40
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 110
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:4BGL"
FT STRAND 17..24
FT /evidence="ECO:0007829|PDB:4BGL"
FT STRAND 27..34
FT /evidence="ECO:0007829|PDB:4BGL"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:4BGL"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:4BFF"
FT STRAND 48..57
FT /evidence="ECO:0007829|PDB:4BGL"
FT STRAND 64..71
FT /evidence="ECO:0007829|PDB:4BGL"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:4BFJ"
FT STRAND 90..97
FT /evidence="ECO:0007829|PDB:4BGL"
FT STRAND 102..110
FT /evidence="ECO:0007829|PDB:4BGL"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:4BGL"
FT STRAND 114..122
FT /evidence="ECO:0007829|PDB:4BGL"
SQ SEQUENCE 125 AA; 13696 MW; D288A5615CD0DAA7 CRC64;
MELFQTADWK KEKHVPVIEV LRAEGGVVEV KVSVGKEIPH PNTTEHHIAW IELVFQPEGS
KFPYVVGRAE FAAHGASVDG PNTSGVYTDP VAVFAFKAEK SGKLTAFSYC NIHGLWMGEA
TLSLE
