ID A0A1T4PEP1_9FIRM Unreviewed; 717 AA.
AC A0A1T4PEP1;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Thiosulfate reductase / polysulfide reductase chain A {ECO:0000313|EMBL:SJZ89949.1};
GN ORFNames=SAMN02745118_02152 {ECO:0000313|EMBL:SJZ89949.1};
OS Selenihalanaerobacter shriftii.
OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Halobacteroidaceae;
OC Selenihalanaerobacter.
OX NCBI_TaxID=142842 {ECO:0000313|EMBL:SJZ89949.1, ECO:0000313|Proteomes:UP000190625};
RN [1] {ECO:0000313|Proteomes:UP000190625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-73 {ECO:0000313|Proteomes:UP000190625};
RA Varghese N., Submissions S.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; FUWM01000018; SJZ89949.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T4PEP1; -.
DR STRING; 142842.SAMN02745118_02152; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000190625; Unassembled WGS sequence.
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:InterPro.
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 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 PANTHER; PTHR43742:SF6; OXIDOREDUCTASE YYAE-RELATED; 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.
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 Reference proteome {ECO:0000313|Proteomes:UP000190625}.
FT DOMAIN 4..61
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 717 AA; 80805 MW; 8574DD26332D5061 CRC64;
MIDKNKVFSS CVMCQGGKCG IEVTIEDEKA TKINGNKLHP FNEGRLCPKG LAGLEQLYDP
DRLLIPKQKV AKDKWQKITW DDALQLITKN MQEIKRKYGA ESFLFMWGPT PPYKELFQGL
AKSYGTPNQF AHTSICDANR RLAKKLTYND YRPLPDFKNS DYILLFGANP LEAHKWFYFY
KDVKGALKRG AKLVVIDPRQ TKSAKNADLW LSIKPGTDGA LALSLAHIII KEELYNKEFI
NKYSRGFASF KAEVMQEKYN PENVSQITGI NTKIIYTIAR QFAKSKQQLA DSWTGLDNQK
QGINAHRAVA CLNALVGSVD ALGGMVFREE GRLKSPEFTN NIKAKPLHEE VGFSNLTAGY
GCRGLIPEAI LTPDHVPTGP LLEKEITSLY KGQGIKGAFI YFTNPILADA NSERWRKALG
NLDFAVGYDI YQTDTLEAFP VGSIILPDTT YLERSEVVKQ YSNGALLTMY QKVVEPKGEA
KSGYWTFVKL GKLLGFDSFQ NFDEGDIESY LKMRLDIEQV DGSQVQLEEL KRKGIWLANN
FDEPKYYRYD QLLNGKFNFA LDLDMESDLV KEFLRVGGNQ TPIYKLQESN NKLKLITTGK
LRCHTHSTTQ NLPALMARKG KNSLLINPED AKKREIRDGE KVIVNSEIDT VRLTAKVTNE
IREGVVQSSH GFGHTSEKLR IAKGQGANIN RLVDNLKLDP ISGVSYLNEM EVVIKPI
//