ID A0A0E3K419_CLOSL Unreviewed; 124 AA.
AC A0A0E3K419;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=CSCA_4512 {ECO:0000313|EMBL:AKA71637.1};
OS Clostridium scatologenes.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1548 {ECO:0000313|EMBL:AKA71637.1, ECO:0000313|Proteomes:UP000033115};
RN [1] {ECO:0000313|Proteomes:UP000033115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25775 {ECO:0000313|Proteomes:UP000033115};
RA Xie J., Zhu Z., Guo T., Song T.;
RT "Complete Genome Sequence of the Malodorant-Producing Specialist,
RT Clostridium scatologenes ATCC 25775.";
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AKA71637.1, ECO:0000313|Proteomes:UP000033115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25775 {ECO:0000313|EMBL:AKA71637.1,
RC ECO:0000313|Proteomes:UP000033115};
RX PubMed=26210291; DOI=10.1016/j.jbiotec.2015.07.013;
RA Zhu Z., Guo T., Zheng H., Song T., Ouyang P., Xie J.;
RT "Complete genome sequence of a malodorant-producing acetogen, Clostridium
RT scatologenes ATCC 25775(T).";
RL J. Biotechnol. 212:19-20(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 -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000256|ARBA:ARBA00001973};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|PIRSR:PIRSR604793-1};
CC Note=Binds 1 Fe(2+) ion per subunit. The iron ion 2 is coordinated via
CC four histidines and one cysteine residue.
CC {ECO:0000256|PIRSR:PIRSR604793-1};
CC -!- COFACTOR:
CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC Evidence={ECO:0000256|PIRSR:PIRSR604793-1};
CC Note=Binds 1 Fe(3+) ion per subunit. The iron ion 1 is coordinated via
CC 4 cysteine residues. {ECO:0000256|PIRSR:PIRSR604793-1};
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; CP009933; AKA71637.1; -; Genomic_DNA.
DR RefSeq; WP_007059319.1; NZ_CP009933.1.
DR AlphaFoldDB; A0A0E3K419; -.
DR STRING; 1548.CSCA_4512; -.
DR KEGG; csq:CSCA_4512; -.
DR HOGENOM; CLU_118960_1_0_9; -.
DR Proteomes; UP000033115; Chromosome.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0050605; F:superoxide reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0019430; P:removal of superoxide radicals; IEA:InterPro.
DR CDD; cd00974; DSRD; 1.
DR CDD; cd03171; SORL_Dfx_classI; 1.
DR Gene3D; 2.20.28.100; Desulphoferrodoxin, N-terminal domain; 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 InterPro; IPR004462; Desulfoferrodoxin_N.
DR InterPro; IPR038094; Desulfoferrodoxin_N_sf.
DR InterPro; IPR004793; Desulfoferrodoxin_rbo.
DR NCBIfam; TIGR00319; desulf_FeS4; 1.
DR NCBIfam; TIGR00320; dfx_rbo; 1.
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, ECO:0000256|PIRSR:PIRSR604793-1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR604793-1};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 3..37
FT /note="Desulfoferrodoxin N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06397"
FT DOMAIN 42..123
FT /note="Desulfoferrodoxin ferrous iron-binding"
FT /evidence="ECO:0000259|Pfam:PF01880"
FT BINDING 10
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604793-1"
FT BINDING 13
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604793-1"
FT BINDING 29
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604793-1"
FT BINDING 30
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604793-1"
FT BINDING 49
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604793-1"
FT BINDING 69
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604793-1"
FT BINDING 75
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604793-1"
FT BINDING 116
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604793-1"
FT BINDING 119
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR604793-1"
SQ SEQUENCE 124 AA; 14212 MW; 572C62EA48C9BF59 CRC64;
MTDVRQVYKC EICGNMVEVI HKAGGTLVCC GKPMTLLSEN TMDAAVEKHV PVIEKLQDGI
VVKVGEVEHP MLENHYIEWI EVHTANKVYR KYLKPGEKPE AIFKVDEEIL FAREYCNVHG
LWKK
//
