ID A0A172RZQ6_9ACTN Unreviewed; 126 AA.
AC A0A172RZQ6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Desulfoferrodoxin {ECO:0000256|ARBA:ARBA00014839};
DE EC=1.15.1.2 {ECO:0000256|ARBA:ARBA00012679};
DE AltName: Full=Superoxide reductase {ECO:0000256|ARBA:ARBA00031398};
GN ORFNames=SAMN02910314_00465 {ECO:0000313|EMBL:SEO52925.1};
OS Denitrobacterium detoxificans.
OC Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC Denitrobacterium.
OX NCBI_TaxID=79604 {ECO:0000313|EMBL:SEO52925.1, ECO:0000313|Proteomes:UP000182975};
RN [1] {ECO:0000313|Proteomes:UP000182975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21843 {ECO:0000313|Proteomes:UP000182975};
RA Varghese N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the one-electron reduction of superoxide anion
CC radical to hydrogen peroxide at a nonheme ferrous iron center. Plays a
CC fundamental role in case of oxidative stress via its superoxide
CC detoxification activity. {ECO:0000256|ARBA:ARBA00024690}.
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:0000256|ARBA:ARBA00001133};
CC -!- SIMILARITY: Belongs to the desulfoferrodoxin family.
CC {ECO:0000256|ARBA:ARBA00005941}.
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DR EMBL; FOEC01000002; SEO52925.1; -; Genomic_DNA.
DR RefSeq; WP_066663809.1; NZ_FOEC01000002.1.
DR AlphaFoldDB; A0A172RZQ6; -.
DR STRING; 79604.AAY81_08225; -.
DR KEGG; ddt:AAY81_08225; -.
DR PATRIC; fig|79604.3.peg.1650; -.
DR OrthoDB; 9814936at2; -.
DR Proteomes; UP000182975; Unassembled WGS sequence.
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; SOR catalytic domain; 1.
DR InterPro; IPR002742; Desulfoferrodoxin_Fe-bd_dom.
DR InterPro; IPR036073; Desulfoferrodoxin_Fe-bd_dom_sf.
DR InterPro; IPR004462; Desulfoferrodoxin_N.
DR PANTHER; PTHR36541; SUPEROXIDE REDUCTASE-RELATED; 1.
DR PANTHER; PTHR36541:SF1; SUPEROXIDE REDUCTASE-RELATED; 1.
DR Pfam; PF06397; Desulfoferrod_N; 1.
DR Pfam; PF01880; Desulfoferrodox; 1.
DR SUPFAM; SSF57802; Rubredoxin-like; 1.
DR SUPFAM; SSF49367; Superoxide reductase-like; 1.
PE 3: Inferred from homology;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000182975};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 5..34
FT /note="Desulfoferrodoxin N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06397"
FT DOMAIN 40..124
FT /note="Desulfoferrodoxin ferrous iron-binding"
FT /evidence="ECO:0000259|Pfam:PF01880"
SQ SEQUENCE 126 AA; 13751 MW; 0CC0D5C4DACADDAB CRC64;
MALAFYKCAK CGNIAVKPYD SGAPLSCCGQ KMEELTANTV DAAKEKHVPM VTVNGPQIDV
VVGEVEHPML EEHYITFICL ETQKGYQFAP LKPGMKPAAS FVVADDDAPV AVYEYCNLHG
LWKAEI
//
