FDHB_METFO
ID FDHB_METFO Reviewed; 399 AA.
AC P06130;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Formate dehydrogenase subunit beta;
DE EC=1.17.1.9;
GN Name=fdhB;
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 1-22.
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).
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=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305};
CC Note=Binds 2 [4Fe-4S] clusters. {ECO:0000305};
CC -!- SUBUNIT: Dimer of an alpha and a beta subunit.
CC -!- SIMILARITY: Belongs to the FrhB family. {ECO:0000305}.
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DR EMBL; J02581; AAA72183.1; -; Genomic_DNA.
DR PIR; B24698; B24698.
DR RefSeq; WP_023991259.1; NZ_LN734822.1.
DR AlphaFoldDB; P06130; -.
DR SMR; P06130; -.
DR STRING; 2162.BRM9_0167; -.
DR PRIDE; P06130; -.
DR GeneID; 26738400; -.
DR OrthoDB; 34322at2157; -.
DR SABIO-RK; P06130; -.
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 Gene3D; 1.10.1060.10; -; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR007516; Co_F420_Hydgase/DH_bsu_N.
DR InterPro; IPR045220; FRHB/FDHB/HCAR-like.
DR InterPro; IPR007525; FrhB_FdhB_C.
DR InterPro; IPR009051; Helical_ferredxn.
DR PANTHER; PTHR31332; PTHR31332; 1.
DR Pfam; PF04432; FrhB_FdhB_C; 1.
DR Pfam; PF04422; FrhB_FdhB_N; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 1: Evidence at protein level;
KW 4Fe-4S; Direct protein sequencing; Electron transport; Iron; Iron-sulfur;
KW Metal-binding; NAD; Oxidoreductase; Repeat; Transport.
FT CHAIN 1..399
FT /note="Formate dehydrogenase subunit beta"
FT /id="PRO_0000159222"
FT DOMAIN 287..316
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 339..367
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 296
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 299
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 302
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 306
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 348
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 351
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 354
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 358
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
SQ SEQUENCE 399 AA; 43922 MW; D57F778C6C8F67BB CRC64;
MINTNDMFYA KSSDAEIAEA GEYGGAVTTL LKFLLKEGIV DAVLAVDSSA DLYDVVPILI
EDPEDVVKAA GSLHFGTLNL AKVVTRYLDG AQDMKIAVTV KPCDAMTMVE LMKREKVNAD
NVIMVGLNCG GTMPPVKGRQ MMEEFYEVDP DSVVKEEIAK GKLIVETEDG TEKEIPIDEL
EDEGFGRRTN CRRCEVNIPR MADLACGNWG VIGPLAGKAT FIEVCSPKGA EVLEKAKEAG
VIDLEDPIPK GIEIREKIDG AMVKLADKWQ GNDWEDKAGR EIFSVLTEYM DDFSRCLKCY
GCREACPICY CEDCCLEANN GPDWLSKGEI PPSPMFHLER MLHMVESCTN CGQCEEVCPG
EIPLAKIWHE VNAKMKDTFG YVKGTGDEKP PIAYFPVGK