FDHB_METJA
ID FDHB_METJA Reviewed; 379 AA.
AC Q60316;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Formate dehydrogenase subunit beta;
DE EC=1.17.1.9;
GN Name=fdhB; OrderedLocusNames=MJ0005;
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).
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=[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. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FrhB family. {ECO:0000305}.
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DR EMBL; L77117; AAB97986.1; -; Genomic_DNA.
DR PIR; E64300; E64300.
DR AlphaFoldDB; Q60316; -.
DR SMR; Q60316; -.
DR STRING; 243232.MJ_0005; -.
DR EnsemblBacteria; AAB97986; AAB97986; MJ_0005.
DR KEGG; mja:MJ_0005; -.
DR eggNOG; arCOG02653; Archaea.
DR HOGENOM; CLU_063409_0_0_2; -.
DR InParanoid; Q60316; -.
DR OMA; CAPTMFG; -.
DR PhylomeDB; Q60316; -.
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:0052592; F:oxidoreductase activity, acting on CH or CH2 groups, with an iron-sulfur protein as acceptor; IBA:GO_Central.
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 3: Inferred from homology;
KW 4Fe-4S; Electron transport; Iron; Iron-sulfur; Metal-binding; NAD;
KW Oxidoreductase; Reference proteome; Repeat; Transport.
FT CHAIN 1..379
FT /note="Formate dehydrogenase subunit beta"
FT /id="PRO_0000159224"
FT DOMAIN 271..301
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 321..351
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 280
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 283
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 286
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 290
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 330
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 333
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 336
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 340
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
SQ SEQUENCE 379 AA; 43014 MW; 9C257CCAD5547F5A CRC64;
MKYVLIQATD NGILRRAECG GAVTALFKYL LDKKLVDGVL ALKRGEDVYD GIPTFITNSN
ELVETAGSLH CAPTNFGKLI AKYLADKKIA VPAKPCDAMA IRELAKLNQI NLDNVYMIGL
NCGGTISPIT AMKMIELFYE VNPLDVVKEE IDKGKFIIEL KNGEHKAVKI EELEEKGFGR
RKNCQRCEIM IPRMADLACG NWGAEKGWTF VEICSERGRK LVEDAEKDGY IKIKQPSEKA
IQVREKIESI MIKLAKKFQK KHLEEEYPSL EKWKKYWNRC IKCYGCRDNC PLCFCVECSL
EKDYIEEKGK IPPNPLIFQG IRLSHISQSC INCGQCEDAC PMDIPLAYIF HRMQLKIRDT
LGYIPGVDNS LPPLFNIER
