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Database: UniProt
Entry: A0A366Y582_9BACI
LinkDB: A0A366Y582_9BACI
Original site: A0A366Y582_9BACI 
ID   A0A366Y582_9BACI        Unreviewed;       785 AA.
AC   A0A366Y582;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   SubName: Full=Formate dehydrogenase {ECO:0000313|EMBL:RBW71371.1};
GN   ORFNames=DS031_01070 {ECO:0000313|EMBL:RBW71371.1};
OS   Bacillus taeanensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=273032 {ECO:0000313|EMBL:RBW71371.1, ECO:0000313|Proteomes:UP000253314};
RN   [1] {ECO:0000313|EMBL:RBW71371.1, ECO:0000313|Proteomes:UP000253314}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BH030017 {ECO:0000313|EMBL:RBW71371.1,
RC   ECO:0000313|Proteomes:UP000253314};
RA   Liu R., Huang Z.;
RT   "Lottiidibacillus patelloidae gen. nov., sp. nov., isolated from the
RT   intestinal tract of a marine limpet and the reclassification of B.
RT   taeanensis BH030017T, B. algicola KMM 3737T and B. hwajinpoensis SW-72T as
RT   genus Lottiidibacillus.";
RL   Submitted (JUL-2018) 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   -!- 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:RBW71371.1}.
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DR   EMBL; QOCW01000001; RBW71371.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A366Y582; -.
DR   OrthoDB; 9805142at2; -.
DR   Proteomes; UP000253314; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:InterPro.
DR   GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.40.50.740; -; 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; IPR010046; Mopterin_OxRdtse_a_bac.
DR   NCBIfam; TIGR01701; Fdhalpha-like; 1.
DR   PANTHER; PTHR43105:SF4; PROTEIN YDEP; 1.
DR   PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   PIRSF; PIRSF000144; CbbBc; 1.
DR   SUPFAM; SSF50692; ADC-like; 1.
DR   SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000253314}.
FT   DOMAIN          124..579
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          659..735
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
SQ   SEQUENCE   785 AA;  87999 MW;  EEF951F160D70734 CRC64;
     MGKTKHTGPI KISKVPSPEH WVSKVPFGLG KIKPHHFRDT AKIAWKNRDN LGYATRIITK
     GVCDGCALGV SGLYDQTLAG PHVCTTRLNV LRLNTMPAMK EEVVHADIDK LRKYSSSELR
     ELGRIPYPLI RRPGERKFSR ISWDDAMDII AEKMKKLDPK QYAFYLTSRG ITNESYYVAG
     KVSRFLGTNH VDNASRICHS PSKTALKRSI GVGASTANYK DWIGTDVLLF WGSVASNASP
     VSTKYMLAAK KKGTKIIVIN PYREPAMDKY WIPSNAESAL FGTKIADDFY QINIGGDIAF
     MHGIMKYWFE MEEKKHGSAI NHQFVQEHVN GYEELKAAVQ AHSWDEIITS SGIAKERIIE
     LAELLANSKN AVFAWALGLT MHSFATDNIS QVANLALLRG YLGREHNGLM PFRGHSSVQG
     SGEMGADPFV LPGGGWDEAN VKRIEKLWGF KLPKWQGDIV GVTIENAMLP DDHERKLKLY
     YMSGGNFLET MPNPDYIEKA LSALEIRVHQ DIIFNTSTLV DAKEAVIVLP AQTRYEQDGG
     GTSTSTERMV YFSPEIEGNK NRIEEARAEW KIYIDLAKRV KPETAHLVDF KDGQAIRDEI
     GKANPDYDGV QHLEKQGDVF QWGGAWLCED GVCPTPDGKG NLIPVEIPDL NKKDGDFYLT
     TRRGKQFNSM IYNEIDPFNG AERDAVLMHP EDAKKLSIQE GESVVVYNQF GVFQGKAKFA
     DIVKGNLGLH FPEGNFLLPK GRYEKFAGIP DYSIAVKIEK AERFNARKDT QYVEKRIDDL
     EMTAD
//
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