ID FDHA_METFO Reviewed; 684 AA. AC P06131; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1988, sequence version 1. DT 27-MAR-2024, entry version 107. DE RecName: Full=Formate dehydrogenase subunit alpha; DE EC=1.17.1.9; GN Name=fdhA; OS Methanobacterium formicicum. OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria; OC Methanobacteriales; Methanobacteriaceae; Methanobacterium. OX NCBI_TaxID=2162; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-26. RC STRAIN=JF-1; RX PubMed=3531194; DOI=10.1016/s0021-9258(18)69253-1; RA Shuber A.P., Orr E.C., Recny M.A., Schendel P.F., May H.D., Schauer N.L., RA Ferry J.G.; RT "Cloning, expression, and nucleotide sequence of the formate dehydrogenase RT genes from Methanobacterium formicicum."; RL J. Biol. Chem. 261:12942-12947(1986). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20. RC STRAIN=JF-1; RX PubMed=1378430; DOI=10.1128/jb.174.15.4997-5004.1992; RA White W.B., Ferry J.G.; RT "Identification of formate dehydrogenase-specific mRNA species and RT nucleotide sequence of the fdhC gene of Methanobacterium formicicum."; RL J. Bacteriol. 174:4997-5004(1992). CC -!- FUNCTION: Catalyzes the oxidation of formate. CC -!- CATALYTIC ACTIVITY: CC Reaction=formate + NAD(+) = CO2 + NADH; Xref=Rhea:RHEA:15985, CC ChEBI:CHEBI:15740, ChEBI:CHEBI:16526, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945; EC=1.17.1.9; CC -!- COFACTOR: CC Name=Mo-bis(molybdopterin guanine dinucleotide); CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000250}; CC Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo- CC bis-MGD) cofactor per subunit. {ECO:0000250}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305}; CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305}; CC -!- SUBUNIT: Dimer of an alpha and a beta subunit. CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing CC oxidoreductase family. {ECO:0000305}. 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; J02581; AAA72182.1; -; Genomic_DNA. DR PIR; A24698; A24698. DR RefSeq; WP_048072979.1; NZ_LN734822.1. DR AlphaFoldDB; P06131; -. DR SMR; P06131; -. DR STRING; 2162.BRM9_0168; -. DR GeneID; 26738401; -. DR OrthoDB; 23466at2157; -. DR SABIO-RK; P06131; -. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0043794; F:formate dehydrogenase (coenzyme F420) activity; IDA:MENGO. DR GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:UniProtKB-EC. 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; cd02790; MopB_CT_Formate-Dh_H; 1. DR CDD; cd02753; MopB_Formate-Dh-H; 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; IPR041925; CT_Formate-Dh_H. DR InterPro; IPR041924; Formate_Dh-H_N. 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 InterPro; IPR027467; MopterinOxRdtase_cofactor_BS. 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; PS00551; MOLYBDOPTERIN_PROK_1; 1. DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1. DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1. PE 1: Evidence at protein level; KW 4Fe-4S; Direct protein sequencing; FAD; Flavoprotein; Iron; Iron-sulfur; KW Metal-binding; Molybdenum; NAD; Oxidoreductase; Zinc. FT CHAIN 1..684 FT /note="Formate dehydrogenase subunit alpha" FT /id="PRO_0000063225" FT DOMAIN 3..59 FT /note="4Fe-4S Mo/W bis-MGD-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004" FT BINDING 10 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004" FT BINDING 13 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004" FT BINDING 17 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004" FT BINDING 45 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004" SQ SEQUENCE 684 AA; 75717 MW; 38D37CF86BFF06E2 CRC64; MDIKYVPTIC PYCGVGCGMN LVVKDEKVVG VEPWKRHPVN EGKLCPKGNF CYEIIHREDR LTTPLIKENG EFREATWDEA YDLIASKLGA YDPNEIGFFC CARSPNENIY VNQKFARIVV GTHNIDHCAR LCHGPTVAGL AASFGSGAMT NSYASFEDAD LIFSIGANSL EAHPLVGRKL MRAKMNGAYF IVADPRYTPT AKQADQYIPF KTGTDVALMN AMMNVIISEG LEDKEFIEKR TKNYEELKEV VSKYTPEMAE EITQVPADVI RDIAIKYAKA DKAAIVYSLG ITEHSHGVDN VMQTANLAML TGNIGRLGTG VNPLRGQNNV QGACDMGALP TDYPGYRKVA DQEVMEDVTC TWGCSDLGCE PGLKIPEMID AAAKGDLKVL YITGEDPVIS DPDTHHVEEA LNNLDFFVVQ DIFMTDTAEF ADVVLPAACW AEQEGTFTNG ERRVQLIRKA VDAPGESKYD WEIFCDLAKK MGADPEMFTY ESAQDIFEEV RTVTPQYAGM NRERLDRPEA LHWPCPSEDH PGTAMMHIEK FAHPDGLGIF MPLEEQGPME TPDDEYPLIL TTTRLLFHYH AAMTRRAATL DREVPTGYVE INTEDAAELG IANKEKVKVK SRRGEIEIAA RVTDDIVKGI VNIPMHFREC SANILTNAAA IDPKSGMPEY KACAVAISKM EGSK //