FDHA_METJA
ID FDHA_METJA Reviewed; 673 AA.
AC P61159;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Formate dehydrogenase subunit alpha;
DE EC=1.17.1.9;
GN Name=fdhA; OrderedLocusNames=MJ1353;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP PROBABLE SELENOCYSTEINE AT SEC-131.
RX PubMed=9102456; DOI=10.1006/jmbi.1996.0812;
RA Wilting R., Schorling S., Persson B.C., Boeck A.;
RT "Selenoprotein synthesis in archaea: identification of an mRNA element of
RT Methanococcus jannaschii probably directing selenocysteine insertion.";
RL J. Mol. Biol. 266:637-641(1997).
CC -!- FUNCTION: Catalyzes the oxidation of formate. {ECO:0000250}.
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; Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
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. {ECO:0000250}.
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; L77117; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR InParanoid; P61159; -.
DR OMA; DGPPCCY; -.
DR PhylomeDB; P61159; -.
DR Proteomes; UP000000805; Chromosome.
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: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.
PE 3: Inferred from homology;
KW 4Fe-4S; FAD; Flavoprotein; Iron; Iron-sulfur; Metal-binding; Molybdenum;
KW NAD; Oxidoreductase; Reference proteome; Selenocysteine; Zinc.
FT CHAIN 1..673
FT /note="Formate dehydrogenase subunit alpha"
FT /id="PRO_0000063226"
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"
FT NON_STD 131
FT /note="Selenocysteine"
FT /evidence="ECO:0000305"
SQ SEQUENCE 673 AA; 75770 MW; B87A668BDF6B98D5 CRC64;
MEFKIVNTIC PYCGVGCGLG LVVKDGRVIG IHPNKRHPIN EGKLCAKGNY CYQFIHSKDR
LTKPLIKKES GFVETTWNKA LEVIAENLKT YKDEIGFFSS ARCTNEDNYI LQKFARVALK
TNNIDHCARL UHSATVTGMS ACFGSGAMTN SIEDIELADC ILIIGSNTFE QHPLIARRIM
RAKDKGAKII VIDPRRTITA KNSDIYLQII PGTNVALINA MINVIIKENL IDKEFIKNRT
EGFEKLKEII KKYTPEYASK ICGVDKELII ESAKIYGNAE RASIIYCMGV TQFTHGVDAV
KALCNLAMIT GNIGKEGTGV NPLRGQNNVQ GACDMGALPN VFPGYQKVED GYKLFEEYWK
TDLNPNSGLT IPEMIDESGK NIKFLYIMGE NPIVSDPDVK HVEKALKSLD FLVVQDIFLT
ETAKLADVVL PAACWAEKDG TFTNTERRVQ LIRKAVNPPG EALEDWIIIK KLAEKLGYGD
KFNYNKVEDI FNEIRKVTPQ YRGITYKRLK IDGIHWPCLD ENHSGTKILH KDKFLTDNGR
GKIFPVEYRE VAELPDKDYP FILTTGRIIF HYHTGTMTRR CKNLVEEINE PFIEINPDDA
KSLKIENGDL VKVISRRGEI TAKARITEDI KKGVVFMPFH FVEANPNVLT NTALDELCKI
PELKVCAVKI ERI
