ID SOR_PYRAB Reviewed; 115 AA.
AC Q9V098; G8ZI59;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2001, sequence version 2.
DT 27-MAR-2024, entry version 118.
DE RecName: Full=Superoxide reductase;
DE Short=SOR;
DE EC=1.15.1.2;
GN Name=sorA; OrderedLocusNames=PYRAB08930; ORFNames=PAB0599;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
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=CAB49807.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CCE70300.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ248285; CAB49807.1; ALT_INIT; Genomic_DNA.
DR EMBL; HE613800; CCE70300.1; ALT_INIT; Genomic_DNA.
DR PIR; F75136; F75136.
DR RefSeq; WP_048146718.1; NC_000868.1.
DR AlphaFoldDB; Q9V098; -.
DR SMR; Q9V098; -.
DR STRING; 272844.PAB0599; -.
DR GeneID; 1496244; -.
DR KEGG; pab:PAB0599; -.
DR PATRIC; fig|272844.11.peg.945; -.
DR eggNOG; arCOG02146; Archaea.
DR HOGENOM; CLU_118960_2_1_2; -.
DR OrthoDB; 30725at2157; -.
DR PhylomeDB; Q9V098; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; Chromosome.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0050605; F:superoxide reductase activity; IEA:UniProtKB-EC.
DR CDD; cd03172; SORL_classII; 1.
DR Gene3D; 2.60.40.730; SOR catalytic domain; 1.
DR InterPro; IPR002742; Desulfoferrodoxin_Fe-bd_dom.
DR InterPro; IPR036073; Desulfoferrodoxin_Fe-bd_dom_sf.
DR NCBIfam; TIGR00332; neela_ferrous; 1.
DR PANTHER; PTHR36541; SUPEROXIDE REDUCTASE-RELATED; 1.
DR PANTHER; PTHR36541:SF1; SUPEROXIDE REDUCTASE-RELATED; 1.
DR Pfam; PF01880; Desulfoferrodox; 1.
DR SUPFAM; SSF49367; Superoxide reductase-like; 1.
PE 3: Inferred from homology;
KW Electron transport; Iron; Metal-binding; Oxidoreductase; Transport.
FT CHAIN 1..115
FT /note="Superoxide reductase"
FT /id="PRO_0000140872"
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"
SQ SEQUENCE 115 AA; 13298 MW; 7DD80F4B92DFBBD6 CRC64;
MLKDTIKSGD WKGEKHVPVI EYEKEGDLVK VEVSVGKEIP HPNTPEHHIA WIELYFHPED
GQFPILVGRV AFTSHDDPLT EPRAVFFFKT KKKGKLYALS YCNIHGLWEN EVQLE
//
