ID B5YL66_THEYD Unreviewed; 730 AA.
AC B5YL66;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE SubName: Full=Thiosulfate reductase {ECO:0000313|EMBL:ACI21892.1};
DE EC=1.-.-.- {ECO:0000313|EMBL:ACI21892.1};
GN OrderedLocusNames=THEYE_A1157 {ECO:0000313|EMBL:ACI21892.1};
OS Thermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 / YP87).
OC Bacteria; Nitrospirota; Thermodesulfovibrionia; Thermodesulfovibrionales;
OC Thermodesulfovibrionaceae; Thermodesulfovibrio.
OX NCBI_TaxID=289376 {ECO:0000313|EMBL:ACI21892.1, ECO:0000313|Proteomes:UP000000718};
RN [1] {ECO:0000313|Proteomes:UP000000718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51303 / DSM 11347 / YP87
RC {ECO:0000313|Proteomes:UP000000718};
RA Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.;
RT "The complete genome sequence of Thermodesulfovibrio yellowstonii strain
RT ATCC 51303 / DSM 11347 / YP87.";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACI21892.1, ECO:0000313|Proteomes:UP000000718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51303 / DSM 11347 / YP87
RC {ECO:0000313|Proteomes:UP000000718};
RX PubMed=25635016;
RA Bhatnagar S., Badger J.H., Madupu R., Khouri H.M., O'Connor E.M.,
RA Robb F.T., Ward N.L., Eisen J.A.;
RT "Genome Sequence of the Sulfate-Reducing Thermophilic Bacterium
RT Thermodesulfovibrio yellowstonii Strain DSM 11347T (Phylum Nitrospirae).";
RL Genome Announc. 3:0-0(2015).
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; CP001147; ACI21892.1; -; Genomic_DNA.
DR RefSeq; WP_012546592.1; NC_011296.1.
DR RefSeq; YP_002248981.1; NC_011296.1.
DR AlphaFoldDB; B5YL66; -.
DR STRING; 289376.THEYE_A1157; -.
DR EnsemblBacteria; ACI21892; ACI21892; THEYE_A1157.
DR KEGG; tye:THEYE_A1157; -.
DR PATRIC; fig|289376.4.peg.1135; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_3_0; -.
DR InParanoid; B5YL66; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000000718; Chromosome.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd02778; MopB_CT_Thiosulfate-R-like; 1.
DR CDD; cd02755; MopB_Thiosulfate-R-like; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR Gene3D; 3.30.2070.10; Formate dehydrogenase/DMSO reductase; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR019546; TAT_signal_bac_arc.
DR NCBIfam; TIGR01409; TAT_signal_seq; 1.
DR PANTHER; PTHR43742:SF9; TETRATHIONATE REDUCTASE SUBUNIT A; 1.
DR PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ACI21892.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000718};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 40..96
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 730 AA; 81443 MW; 15E8944BE2A40F6A CRC64;
MSITRRDFLK IAAVTGGVAA ASTPVVKSVL ALGKKPVSLP QYVPTTCEMC FWRCGVIAKV
VDGKVVKLDG NPLHPNSRGK LCARGHGGIG LLYDSDRLKT PLINTGSRGE AKFKKASWDE
ALGYVADRMQ KIKEKYGAES VGLLTHGTVS TYFMHLLQAF GSPNFAMPSF ALCRGARGVA
FELTFGEDVG NPERLDLQNS KAIVLIGSHL GENAHNSQCQ EFAEAVGKGA TVIVLDPRFS
TAAGKAKYWL PIKPTTDLAI LLAWINIIIN EGLYDKDYVA KYTTGFNEVS QAVKEYTPEW
AEKETEIPAG RIVETARVLG KNKPNVLIHP GRHTAWYSDN VQRQRAVAIL TAILGAYGRP
GGIYLNPKKK LEPVFLSDKD YPEPQKPAIN KGNYPFAGEE GVTHAIVKAT LTEDPYPIKA
WFITGTNIMK AMPNQRDTLN AVQRLDLLVA VDMMPYDGVM LADVVLPECT YLERHDDFFT
VKERSFGISF RQPVVQPMYD TKPGWWIAKE LGKRLGLEEY FPWNTFDDFL KAKAEAWGID
YAELGQKGYI DFPESAKPYL SQGEDYKFKT PSGKIELYSN ELKKHGFDPI PKYTKHEQPS
EGWFRLIYGR APVHTFSRTT NNPSLWELME ENVAWINAKV AKRMGLKHGD YIVLVNQDGV
KSNKVRAKVT ERIRPDCIYL VHGFCSTSKL LHRAYLRGAD DQQLITKYAI DPISGSVGMR
VNFVKITKEV
//