ID A0A0F2SIW3_9FIRM Unreviewed; 693 AA.
AC A0A0F2SIW3;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Dehydrogenase {ECO:0000313|EMBL:KJS49397.1};
GN ORFNames=VR66_08730 {ECO:0000313|EMBL:KJS49397.1};
OS Peptococcaceae bacterium BRH_c23.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX NCBI_TaxID=1629714 {ECO:0000313|EMBL:KJS49397.1, ECO:0000313|Proteomes:UP000033503};
RN [1] {ECO:0000313|EMBL:KJS49397.1, ECO:0000313|Proteomes:UP000033503}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c23 {ECO:0000313|EMBL:KJS49397.1};
RA Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (MAR-2015) 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:KJS49397.1}.
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DR EMBL; LADV01000101; KJS49397.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F2SIW3; -.
DR PATRIC; fig|1629714.3.peg.252; -.
DR Proteomes; UP000033503; 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 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 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}.
FT DOMAIN 21..78
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 693 AA; 75217 MW; 897293914BDE0594 CRC64;
MGSYVRTRAL TQSTKPIEHD EELRTSVCCL CNGGCGIKIS LDQDGKIKAV FGDPDNPYNK
GKICSKPMAI AQTLSGPYRV RYPMKKVNGS FERISWDEAL DLIAQKYNQY IQENGTGSIV
GITSKIGGSY SKLAHGIFSS LTGLVNYGTG PICTDSEANV RKKLFGDGSG TSPLSDVVNS
KILLIVGNNA AQTKAGQFHW ITEAKRTGTR IVVIDTRFTE TAQAADLFIQ IRPGTDTALG
MALLNYVIKN NLYDPTFVSE HTNGFEKLAQ DVSAFTTERA AEITGVPQNV IEKLAQDLAT
LKPGMLFEGR GVVCVNNAGA SVWAFEGLMA ILGNIGKPGA GIISHINNTG GIINLIQAND
VMKPDRKRSS SALYKDMEEG DVKMLLISGN PCVTWPDSAR MSKAIEGLDF VVSHTLVMDD
SAVLADIVLP ATHWLEEAGM QASVHRVLQW KNKVVEIRGE EKSGGDFYRL LAERMGLPSS
YFPDSPEAAW ELERKYNKNV TGISRERMLE TPGGVHFPCA EIGKETVRLF ANCVFKTSSG
KVELTEVSDA PLEYVDTFDA PGNIGSSREE FPYLLSTNKV ASHYHSECQY SDWANEMEQP
YVEMHPLTAL EIGVEKGNQV RVETVTGSIV LAAKITQSVP RGFLSTQPYF GFQSPYGQAP
ANTLFPVAAD PVGGNLVSKN IMCKAKAEGG QGS
//
