ID A5IJC9_THEP1 Unreviewed; 131 AA.
AC A5IJC9;
DT 26-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Superoxide reductase {ECO:0000313|EMBL:ABQ46302.1};
DE EC=1.15.1.2 {ECO:0000313|EMBL:ABQ46302.1};
GN OrderedLocusNames=Tpet_0273 {ECO:0000313|EMBL:ABQ46302.1};
OS Thermotoga petrophila (strain ATCC BAA-488 / DSM 13995 / JCM 10881 /
OS RKU-1).
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae;
OC Thermotoga.
OX NCBI_TaxID=390874 {ECO:0000313|EMBL:ABQ46302.1, ECO:0000313|Proteomes:UP000006558};
RN [1] {ECO:0000313|Proteomes:UP000006558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-488 / DSM 13995 / JCM 10881 / RKU-1
RC {ECO:0000313|Proteomes:UP000006558};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Detter J.C., Han C.,
RA Tapia R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.;
RT "Complete sequence of Thermotoga petrophila RKU-1.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABQ46302.1, ECO:0000313|Proteomes:UP000006558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-488 / DSM 13995 / JCM 10881 / RKU-1
RC {ECO:0000313|Proteomes:UP000006558};
RX PubMed=19307556; DOI=10.1073/pnas.0901260106;
RA Zhaxybayeva O., Swithers K.S., Lapierre P., Fournier G.P., Bickhart D.M.,
RA DeBoy R.T., Nelson K.E., Nesbo C.L., Doolittle W.F., Gogarten J.P.,
RA Noll K.M.;
RT "On the chimeric nature, thermophilic origin, and phylogenetic placement of
RT the Thermotogales.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:5865-5870(2009).
CC -!- SIMILARITY: Belongs to the desulfoferrodoxin family.
CC {ECO:0000256|ARBA:ARBA00005941}.
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DR EMBL; CP000702; ABQ46302.1; -; Genomic_DNA.
DR RefSeq; WP_004081116.1; NC_009486.1.
DR AlphaFoldDB; A5IJC9; -.
DR SMR; A5IJC9; -.
DR STRING; 390874.Tpet_0273; -.
DR KEGG; tpt:Tpet_0273; -.
DR eggNOG; COG2033; Bacteria.
DR HOGENOM; CLU_118960_2_1_0; -.
DR Proteomes; UP000006558; 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 {ECO:0000256|ARBA:ARBA00022982};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000313|EMBL:ABQ46302.1};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 10..123
FT /note="Desulfoferrodoxin ferrous iron-binding"
FT /evidence="ECO:0000259|Pfam:PF01880"
SQ SEQUENCE 131 AA; 14935 MW; C5380BF586F124CE CRC64;
MKLSDFIKTE DFKKEKHVPV IEAPEKVKKD EKVQIVVTVG KEIPHPNTTE HHIRWIKVFF
QPDGDPYVYE VGRYEFNAHG ESVQGPNIGA VYTEPTVTTV VKLNRSGTII ALSYCNIHGL
WESSQKITVE E
//
