ID Q50743_METTF Unreviewed; 887 AA.
AC Q50743;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE RecName: Full=formate dehydrogenase {ECO:0000256|ARBA:ARBA00013128};
DE EC=1.17.1.9 {ECO:0000256|ARBA:ARBA00013128};
GN Name=flpF {ECO:0000313|EMBL:CAA61208.1};
OS Methanothermobacter thermautotrophicus (Methanobacterium thermoformicicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=145262 {ECO:0000313|EMBL:CAA61208.1};
RN [1] {ECO:0000313|EMBL:CAA61208.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Marburg/DSM 2133 {ECO:0000313|EMBL:CAA61208.1};
RX PubMed=8575452; DOI=10.1111/j.1432-1033.1995.910_a.x;
RA Hochheimer A., Schmitz R.A., Thauer R.K., Hedderich R.;
RT "The tungsten formylmethanofuran dehydrogenase from Methanobacterium
RT thermoautotrophicum contains sequence motifs characteristic for enzymes
RT containing molybdopterin dinucleotide.";
RL Eur. J. Biochem. 234:910-920(1995).
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 Evidence={ECO:0000256|ARBA:ARBA00000455};
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|ARBA:ARBA00034078};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: In the C-terminal section; belongs to the prokaryotic
CC molybdopterin-containing oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00007023}.
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DR EMBL; X87969; CAA61208.1; -; Genomic_DNA.
DR PIR; S63554; S57430.
DR AlphaFoldDB; Q50743; -.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
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; cd00207; fer2; 1.
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; 3.10.20.740; -; 1.
DR Gene3D; 3.30.70.20; -; 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; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
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; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
DR NCBIfam; TIGR01591; Fdh-alpha; 1.
DR PANTHER; PTHR43105:SF15; FORMATE DEHYDROGENASE H; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF13510; Fer2_4; 1.
DR Pfam; PF12838; Fer4_7; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR Pfam; PF10588; NADH-G_4Fe-4S_3; 1.
DR PIRSF; PIRSF036643; FDH_alpha; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SMART; SM00929; NADH-G_4Fe-4S_3; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
DR PROSITE; PS51839; 4FE4S_HC3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
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}.
FT DOMAIN 3..81
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 80..119
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 142..172
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 185..213
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 216..272
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 887 AA; 97153 MW; CB31C5D0282C787F CRC64;
MKGTVKFRID GREVEAARGM TVLEAALANG IYIPNLCFRE GIEPFGGCRL CLVENNEGRL
VTACETPAED GSEFISESER INRIRRTTLS LIIADHSRDC LACPASGDCR LQELSSYLNV
SDGDLERLRP ELSGIDVDES NPFFLRNHDK CILCGICVRV CRGLGAEAVD FAYRGHDTRI
ATFMDRDILD SSCVSCGECV EACPVGALLP RTERPSTEVR TVCPYCGAGC EIYLGVRGNR
VVSSRGVPDS PVNQGRLCVK GRFALKFVNS PERLKKPLIK VDGEFVEVEW DEAISVVAER
LSEYTGEEFA AVASAKCTNE ENYLLQKFTR AVMGSGNIDH CARLCHAPSL TGLRMSLGSG
AMTNSISELG AAGCILAVGT NPTETHPVTS YRVIRALRSR ARLVVVDPRK TRLSELADIH
LQNRPGSDIP LLMAMCRFIL EEGLHDSEFI DSRTEKFEDF RDAVMALDLD EVERITGVNV
KDIRRAAIMY ASNSPASIIY SMGITQHVNG TGNVLALSNL ALLTGNIGIK SAGINPLRGQ
NNVQGACDMG ALPDLLPGYQ GIGEAAGKFS EKWGSPIPPA GLTLPEMFDA ARDGKIRCMY
IMGENPLLSE PDIERTREAL EGLEFLVVQD ICLTETAELA DVVLPAASFA EKDGTFTNTE
RRVQLLRKAL DAPGDALPDW QIISMIAGRM GREDFDYESA SRIFDEIREL VPSYAGISHE
RLKSGGIQWP CTSEEDAGTG YLHSEEFPTP TGRASFLLPD YQFRGVPEEY PLVLVTGRNL
YQYHTRSMTA RVEELESFSD HEELLMNPAD ASSMGIREGD TVEVTSERGS LRVRAGVTDE
VMEGVVFMTF HFADAPANVL TGGDRDPFSG MPGLKFTPVR VCRVQLR
//
