ID   B9L5D0_THERP            Unreviewed;       826 AA.
AC   B9L5D0;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   SubName: Full=Formate dehydrogenase, nitrate-inducible, major subunit (Formate dehydrogenase-N subunit alpha) (FDH-N subunit alpha)(Anaerobic formate dehydrogenase major subunit) {ECO:0000313|EMBL:ACM07001.1};
DE            EC=1.2.1.2 {ECO:0000313|EMBL:ACM07001.1};
GN   OrderedLocusNames=trd_A0057 {ECO:0000313|EMBL:ACM07001.1};
OS   Thermomicrobium roseum (strain ATCC 27502 / DSM 5159 / P-2).
OG   Plasmid Tros {ECO:0000313|Proteomes:UP000000447}.
OC   Bacteria; Thermomicrobiota; Thermomicrobia; Thermomicrobiales;
OC   Thermomicrobiaceae; Thermomicrobium.
OX   NCBI_TaxID=309801 {ECO:0000313|EMBL:ACM07001.1, ECO:0000313|Proteomes:UP000000447};
RN   [1] {ECO:0000313|EMBL:ACM07001.1, ECO:0000313|Proteomes:UP000000447}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27502 / DSM 5159 / P-2
RC   {ECO:0000313|Proteomes:UP000000447};
RC   PLASMID=Tros {ECO:0000313|Proteomes:UP000000447};
RX   PubMed=19148287; DOI=10.1371/journal.pone.0004207;
RA   Wu D., Raymond J., Wu M., Chatterji S., Ren Q., Graham J.E., Bryant D.A.,
RA   Robb F., Colman A., Tallon L.J., Badger J.H., Madupu R., Ward N.L.,
RA   Eisen J.A.;
RT   "Complete genome sequence of the aerobic CO-oxidizing thermophile
RT   Thermomicrobium roseum.";
RL   PLoS ONE 4:E4207-E4207(2009).
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001276; ACM07001.1; -; Genomic_DNA.
DR   AlphaFoldDB; B9L5D0; -.
DR   KEGG; tro:trd_A0057; -.
DR   eggNOG; COG0243; Bacteria.
DR   eggNOG; COG3383; Bacteria.
DR   HOGENOM; CLU_000422_1_2_0; -.
DR   Proteomes; UP000000447; Plasmid Tros.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0047111; F:formate dehydrogenase (cytochrome-c-553) activity; IEA:InterPro.
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:0045333; P:cellular respiration; IEA:InterPro.
DR   CDD; cd02792; MopB_CT_Formate-Dh-Na-like; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.40.50.740; -; 1.
DR   Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 2.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR006443; Formate-DH-alph_fdnG.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR   NCBIfam; TIGR01553; formate-DH-alph; 1.
DR   PANTHER; PTHR43598:SF1; FORMATE DEHYDROGENASE, NITRATE-INDUCIBLE, MAJOR SUBUNIT; 1.
DR   PANTHER; PTHR43598; TUNGSTEN-CONTAINING FORMYLMETHANOFURAN DEHYDROGENASE 2 SUBUNIT B; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   SUPFAM; SSF50692; ADC-like; 1.
DR   SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR   PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW   Iron {ECO:0000256|ARBA:ARBA00022485};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00022485};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:ACM07001.1}; Plasmid {ECO:0000313|EMBL:ACM07001.1}.
FT   DOMAIN          8..376
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          700..816
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
SQ   SEQUENCE   826 AA;  93319 MW;  C9B339123A1F69CC CRC64;
     MAFRWVAEAK RRGAKLIHVD PRFTRTSAMA DLYVPLRSGT DIAFLGGLIR YMIENEKYFK
     DYVVNYTNAA TIIRDDFQDT EDLEGVFSGL KEAPQGTNQK YVYDNATWQY KRTAPFDAAK
     AREEAIKAAT FAEMIQKMVP PPAEKDPTLQ HPQTVFQIMR RHFSRYTPEM VEQICGTPKE
     LFLRVAEMLA ENSGPERTTM FVYAMGWTQH TYGVQNIGAA ALLQLLLGNV GRPGGGILAL
     RGHATIQGST DVPTLHHSIH GYMAHPDARR RHDTLRDYIL TETRPTGYWA NLPKFMVSYL
     KSMYGDAAKP ENDFGYDWHP KIAGDYSFMA SFHAMAKGEI KGAFFFGQNP ATSINGGLIR
     RALANLDWMV VKDNFEIETA AFWYKSPEVE SGELKPEQIK TEVFLFPSAQ VGEIEGTFTN
     TQRWIQFHEK AADPPGDCRS DAWFTHQLAL RLKKLYADST LPRDQGFKNL TWDFDYEPGK
     YPTNTRIQGE PDVMKIWREI NGFKTDTGEL LKGFGELKDD GSTTCASWIY CGAYPEEGKF
     LPANRNPDPD DKPGTHLGWA YAWPANRRIL YNRASADPNG NPWSERKKLI WWDAGQKKWV
     GYDVPDFPAT KAPDTPAKPG AAGMDAHDGK SPFILLPDGK GWLFVPTGLQ DGPLPTHYEP
     MESPVPNLLY PKWQTNPIAK IYEHERNQLA QVGDPQFPIV LTTYRLTEHH LSGAMSRWLP
     WLAELQPELF VEISPELAQE KGIQNLDWVR ITSKRGSIVA KALVTPRLRP LTVNGKTVHQ
     IGMPWHWGFM GLSTGDVVND LTSWVADPNV MIHEAKALLV NVEKAK
//