ID   A5CYQ4_PELTS            Unreviewed;       767 AA.
AC   A5CYQ4;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   SubName: Full=Anaerobic dehydrogenases {ECO:0000313|EMBL:BAF60888.1};
GN   Name=BisC {ECO:0000313|EMBL:BAF60888.1};
GN   OrderedLocusNames=PTH_2707 {ECO:0000313|EMBL:BAF60888.1};
OS   Pelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC   Pelotomaculum.
OX   NCBI_TaxID=370438 {ECO:0000313|EMBL:BAF60888.1, ECO:0000313|Proteomes:UP000006556};
RN   [1] {ECO:0000313|Proteomes:UP000006556}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13744 / JCM 10971 / SI {ECO:0000313|Proteomes:UP000006556};
RX   PubMed=18218977; DOI=10.1101/gr.7136508;
RA   Kosaka T., Kato S., Shimoyama T., Ishii S., Abe T., Watanabe K.;
RT   "The genome of Pelotomaculum thermopropionicum reveals niche-associated
RT   evolution in anaerobic microbiota.";
RL   Genome Res. 18:442-448(2008).
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; AP009389; BAF60888.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5CYQ4; -.
DR   STRING; 370438.PTH_2707; -.
DR   KEGG; pth:PTH_2707; -.
DR   eggNOG; COG0243; Bacteria.
DR   HOGENOM; CLU_000422_13_3_9; -.
DR   Proteomes; UP000006556; Chromosome.
DR   GO; GO:0018818; F:acetylene hydratase activity; IEA:InterPro.
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   CDD; cd02781; MopB_CT_Acetylene-hydratase; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.40.50.740; -; 2.
DR   Gene3D; 2.20.25.90; ADC-like domains; 1.
DR   Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 2.
DR   Gene3D; 3.30.2070.10; Formate dehydrogenase/DMSO reductase; 1.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR037949; MopB_CT_Acetylene-hydratase.
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:UP000006556}.
FT   DOMAIN          4..60
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   767 AA;  86756 MW;  08B48848BA49F057 CRC64;
     MQNIRIIKSA CRMCHGVCQV LVHMEGERVV KITGDPESPT SRGYICRKGA ASAELLYHPD
     RVLQPLRRAG KRGENKWTPI SWDEALDEMA ERLLKIKRES GPQYFAMMHG TGRPYENLGA
     RFANAFGTPN FTGVGHICFW PRVYANIFTQ GMSEMPVCDV YGQGGVEPQC VLIWGCNITG
     PKGHNSSDGM CGALLQKVIK NAQKVIVVDP RRISPAENAD HWLQLRPGTD GALALAMINV
     IIVEDLIDRE FVNNYTVGFD RLKEHIKPFT PEWAEEIVGV GAEDIRAAAR TYATVKPACM
     QWGNAVDHSM CNFHTARSLL ILRAITGNLH VPGGDIVFER PQGLRVKFPY LDIDFAGFRF
     MPLQNYQYAL DGNHGKQNIS STKRFIQDRT LQFLDFLKYN FYPLLRKFSQ GEGQALKLMA
     ELKGARYPLS PVIHPPTFWK SIVNNDPYRI RALWIIGANP LLTMSNSLLI EEALKLIEYI
     VVSDFFLTPT AHYADLFLPA STWLEYDEVH NSGAHTFSVF PRKKVVKIGD TLDDQEVMIR
     LAHRLGMHDA FPWRSHQELT DWMLKGTGLS FEEFCEKGIL TGKARYYAYE KEKHFFRTPS
     GKFEIYSDTL ASMGISPLPI YREPAFSPVS TPQVAEKYPL ILIGGVKMAD YFHSEGRQIS
     SLRRRNPDPL VEINPKTAAS IGCSEGDWVW IETPHGRVKM RAKLFDGIAE NVVCAQYAWW
     FPEEAPPEHG WKKSNINLTF GEMDYDPETG SESLKSMLCR IYPVGNN
//