FDHA_METFO
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 03-AUG-2022, entry version 102.
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}.
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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; 1029at2157; -.
DR SABIO-RK; P06131; -.
DR GO; GO:0009326; C:formate dehydrogenase complex; IEA:UniProtKB-EC.
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 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 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; SSF50692; 1.
DR TIGRFAMs; TIGR01591; Fdh-alpha; 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
