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Database: UniProt
Entry: A0A366XR39_9BACI
LinkDB: A0A366XR39_9BACI
Original site: A0A366XR39_9BACI 
ID   A0A366XR39_9BACI        Unreviewed;       707 AA.
AC   A0A366XR39;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Formate dehydrogenase subunit alpha {ECO:0000313|EMBL:RBW68357.1};
GN   ORFNames=DS031_16965 {ECO:0000313|EMBL:RBW68357.1};
OS   Bacillus taeanensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=273032 {ECO:0000313|EMBL:RBW68357.1, ECO:0000313|Proteomes:UP000253314};
RN   [1] {ECO:0000313|EMBL:RBW68357.1, ECO:0000313|Proteomes:UP000253314}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BH030017 {ECO:0000313|EMBL:RBW68357.1,
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   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
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:RBW68357.1}.
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DR   EMBL; QOCW01000021; RBW68357.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A366XR39; -.
DR   OrthoDB; 9805142at2; -.
DR   Proteomes; UP000253314; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR   GO; GO:0015942; P:formate metabolic process; IEA:InterPro.
DR   CDD; cd00508; MopB_CT_Fdh-Nap-like; 1.
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; IPR006478; Formate_DH_asu.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR   InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR   NCBIfam; TIGR01591; Fdh-alpha; 1.
DR   PANTHER; PTHR43105:SF15; FORMATE DEHYDROGENASE H; 1.
DR   PANTHER; PTHR43105; RESPIRATORY NITRATE 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.
DR   PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
PE   4: Predicted;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000253314}.
FT   DOMAIN          18..76
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   707 AA;  79589 MW;  D1D1A05BB1BBA623 CRC64;
     MAEFVVKPGV KNLQHKDEKL ITTHCSYCGM QCGMHIRVHK KTGKVMGVEP RYDWPVTMGK
     MCPKGVTAYQ QIDHKDRITR PLIKKNGKFV EASWDEALDL IEKNFKGLQK KYGKDTLSVF
     GGVSMTTEKC YLVGKYARVA LGTRYLDYNG RFCMSSAAGG FIKTFGIDRG STLPWPELEH
     SDCFFMAGTN TAECHPTSIQ WFWRAKDKGA KLIVADPRET PTARIADVHL DLKPGTDSAL
     ANGMMHLIIK EGYVDEAYVS ERCNNYEELK DMVKKFTPEY TSEITGIAVE KIIKAAHIYG
     RSPRSVMMFA RGVEQQSKGV DNVTLYSSMA LLRGQIGKFA SGVATFTGQG NGQGGREHGQ
     KSDLLPGYRK LTDPKAVEYI SKVWGIDPKE MPEPGVSAYE MFDEIQKGNI RAMHVICSNP
     AVSAPNTEYI WEGFRKLDFM VVSDFFLSET AEFADVVLPA ATWAEDEGTT TNLEGRVIRI
     RKVKEPLGES KTDWEIMSEI AKRMGKGEHF QYHNPKEIFE ELRIASKGGK ADYSGITYER
     IEKEDGVFWP CPSVDHPGTP TMFKEKFETP DGKANLAVVD WKPAGETPTK EYPHLLTTGR
     VVFHYLSGNQ TRRIDFLMEQ CPLPYVEIHP ELASQYNLSN GEKVKLTTSR SQMTLDVRLT
     KAIRKDTVFV PYHWGKELAV NQLTNPCLDP VSRMPEFKVC AVKIEKL
//
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