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Database: UniProt
Entry: A0A0A8X0D0_9BACI
LinkDB: A0A0A8X0D0_9BACI
Original site: A0A0A8X0D0_9BACI 
ID   A0A0A8X0D0_9BACI        Unreviewed;       749 AA.
AC   A0A0A8X0D0;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Anaerobic dehydrogenases, typically selenocysteine-containing {ECO:0000313|EMBL:GAM13405.1};
GN   ORFNames=SAMD00020551_1549 {ECO:0000313|EMBL:GAM13405.1};
OS   Mesobacillus selenatarsenatis SF-1.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Mesobacillus.
OX   NCBI_TaxID=1321606 {ECO:0000313|EMBL:GAM13405.1, ECO:0000313|Proteomes:UP000031014};
RN   [1] {ECO:0000313|EMBL:GAM13405.1, ECO:0000313|Proteomes:UP000031014}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SF-1 {ECO:0000313|EMBL:GAM13405.1,
RC   ECO:0000313|Proteomes:UP000031014};
RA   Kuroda M., Sei K., Yamashita M., Ike M.;
RT   "Whole genome shotgun sequence of Bacillus selenatarsenatis SF-1.";
RL   Submitted (JUN-2013) 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}.
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:GAM13405.1}.
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DR   EMBL; BASE01000031; GAM13405.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A8X0D0; -.
DR   STRING; 1321606.SAMD00020551_1549; -.
DR   OrthoDB; 9803192at2; -.
DR   Proteomes; UP000031014; 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:UniProtKB-KW.
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   PANTHER; PTHR43742:SF9; TETRATHIONATE REDUCTASE SUBUNIT A; 1.
DR   PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 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   Reference proteome {ECO:0000313|Proteomes:UP000031014};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          46..117
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   749 AA;  84221 MW;  B7FCE882B074C5A2 CRC64;
     MMTLNKTFKW FDCNRREFLV GTAALGTSLL LGDSLKPKAD SLRVGEEVTI PTCCHMCGGG
     TGVIATVRDG VVSKLEPNVD NPIGVCNTST GYYENSKYGA AMCPRGLSAI MSLYDPDRIK
     KPMLRTNPKK GISIDPEWQE ISWEEALEII QDKLKKLLDE NRPEALITFS ENSLFTDVQR
     DFCHLFGTPN VSFHTNICSV TRKSAAKSVL GVEEPLGDYQ HCKFMLLFGW NPLSAVKWAH
     LPQIILNGKQ NGSKLVVIDP RFSETAAKAD KWLPILPGTD GALALALAHV IVKENLHNER
     FINDWTEGFK EYKEFLTDKT PEWAEKICGI PSDEIQILAR EFASNQPAIA DVWVGPGQQS
     NGFNASRAIF LLNVLVGNVD QPGGMMLTEE FKLGNSPIQT SQSKTKRFDG LENFPFGHRS
     GVYVEAIRHL YHQSGPYPLE VAFFTMSNPV LSLPNSNIVV DALKKLNFIV VIDNYISETA
     LLADLVLPGT IYMERSGLVT RGTNWKYVAL RQPVVEPLFG QLPEVDIFIE LANRLELKDI
     QGKVAFKDIS YEDYMDYRLQ KSDAGITLAE LKSFSGAVWR SNEETQFEKY KLRNNKFHFS
     ISTLDLGNVD KFPVFRQRKW MPDSNYPFYL ISWKHISHTH SRTQNNPYLS ELKNQNFLYI
     NPETAKSLSF NDGDRIRVNS PYGRVTATLR ITPGIHPKVL GTEWGFGHKG FGKYAKDKGF
     SVNHLNGLLS DEITGQALHK EICVNIEKL
//
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