ID A0A0S7BVC9_9CHLR Unreviewed; 125 AA.
AC A0A0S7BVC9;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=ATC1_131122 {ECO:0000313|EMBL:GAP41140.1};
OS Flexilinea flocculi.
OC Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC Flexilinea.
OX NCBI_TaxID=1678840 {ECO:0000313|EMBL:GAP41140.1};
RN [1] {ECO:0000313|EMBL:GAP41140.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TC1 {ECO:0000313|EMBL:GAP41140.1};
RA Matsuura N., Tourlousse D.M., Sun L., Toyonaga M., Kuroda K., Ohashi A.,
RA Cruz R., Yamaguchi T., Sekiguchi Y.;
RT "Draft Genome Sequence of Anaerolineae Strain TC1, a Novel Isolate from a
RT Methanogenic Wastewater Treatment System.";
RL Genome Announc. 3:e01104-15(2015).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DF968181; GAP41140.1; -; Genomic_DNA.
DR RefSeq; WP_062281766.1; NZ_DF968181.1.
DR AlphaFoldDB; A0A0S7BVC9; -.
DR STRING; 1678840.ATC1_131122; -.
DR PATRIC; fig|1678840.3.peg.2550; -.
DR OrthoDB; 9814936at2; -.
DR Proteomes; UP000053370; 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 NCBIfam; TIGR00332; neela_ferrous; 1.
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:UP000053370};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 5..34
FT /note="Desulfoferrodoxin N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06397"
FT DOMAIN 40..123
FT /note="Desulfoferrodoxin ferrous iron-binding"
FT /evidence="ECO:0000259|Pfam:PF01880"
SQ SEQUENCE 125 AA; 13997 MW; A307D445323176EC CRC64;
MEQKFFYCKH CGKIIGMIFD SGTPTICCGE PMQELVPNTT DGAMEKHVPV VKVAGDTVEV
SVGSVLHPMA LEHYIQWIYL QTKKGGQRKR LSPGDEPKAV FVLKDDEPVT VFEYCNLHGL
WKADI
//
