ID G5R1W6_SALSE Unreviewed; 444 AA.
AC G5R1W6;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Thiosulfate reductase {ECO:0000313|EMBL:EHC86554.1};
GN ORFNames=LTSESEN_3346 {ECO:0000313|EMBL:EHC86554.1};
OS Salmonella enterica subsp. enterica serovar Senftenberg str. A4-543.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=913082 {ECO:0000313|EMBL:EHC86554.1, ECO:0000313|Proteomes:UP000005065};
RN [1] {ECO:0000313|EMBL:EHC86554.1, ECO:0000313|Proteomes:UP000005065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A4-543 {ECO:0000313|EMBL:EHC86554.1,
RC ECO:0000313|Proteomes:UP000005065};
RX PubMed=21859443; DOI=10.1186/1471-2164-12-425;
RA den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., Ranieri M.L.,
RA Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., Brown S., Bolchacova E.,
RA Furtado M.R., Wiedmann M.;
RT "Genome sequencing reveals diversification of virulence factor content and
RT possible host adaptation in distinct subpopulations of Salmonella
RT enterica.";
RL BMC Genomics 12:425-425(2011).
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHC86554.1}.
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DR EMBL; AFCU01001091; EHC86554.1; -; Genomic_DNA.
DR AlphaFoldDB; G5R1W6; -.
DR PATRIC; fig|913082.3.peg.2568; -.
DR BioCyc; SENT913082:G120J-2589-MONOMER; -.
DR Proteomes; UP000005065; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd02755; MopB_Thiosulfate-R-like; 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 InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
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 SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR PROSITE; PS51318; TAT; 1.
PE 4: Predicted;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00023014};
KW Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 41..97
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 444 AA; 47852 MW; DFDF035380FB5F87 CRC64;
MSISRRSFLQ GVGIGCSACA LGAFPPGALA RNPIAGINGK TTLTPSLCEM CSFRCPIQAQ
VVNNKTVFIQ GNPSAPQQGT RICARGGSGV SLVNDPQRIV KPMKRTGPRG DGEWQVISWQ
QAYQEIAAKM NAIKAQHGPE SVAFSSKSGS LSSHLFHLAT AFGSPNTFTH ASTCPAGKAI
AAKVMMGGDL AMDIANTRYL VSFGHNLYEG IEVADTHELM TAQEKGAKMV SFDPRLSIFS
SKADEWHAIR PGGDLAVLLA MCHVMIDEQL YDASFVERYT SGFEQLAQAV KETTPEWAAA
QADVPADVIV RVTRELAACA PHAIVSPGHR ATFSQEEIDM RRMIFTLNVL LGNIEREGGL
YQKKNASVYN KLAGEKVAPT LAKLNIKNMP KPTAQRIDLI APQFKYIAAG GGVVQSIIDA
VLTEKPYPIK AWIMSRHITP KGTQ
//
