ID FDHB_METTF Reviewed; 394 AA. AC Q50570; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 24-JAN-2024, entry version 96. DE RecName: Full=Formate dehydrogenase subunit beta; DE EC=1.17.1.9; GN Name=fdhB; OS Methanothermobacter thermautotrophicus (Methanobacterium thermoformicicum). OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria; OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter. OX NCBI_TaxID=145262; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=DSM 3720 / Z-245; RX PubMed=9006048; DOI=10.1128/jb.179.3.899-908.1997; RA Noelling J., Reeve J.N.; RT "Growth- and substrate-dependent transcription of the formate dehydrogenase RT (fdhCAB) operon in Methanobacterium thermoformicicum Z-245."; RL J. Bacteriol. 179:899-908(1997). 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}. 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; U52681; AAC44821.1; -; Genomic_DNA. DR RefSeq; WP_048176090.1; NZ_CP064337.1. DR AlphaFoldDB; Q50570; -. DR SMR; Q50570; -. DR GeneID; 77403974; -. 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 Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 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; 7-HYDROXYMETHYL CHLOROPHYLL A REDUCTASE, CHLOROPLASTIC; 1. DR PANTHER; PTHR31332:SF6; FORMATE DEHYDROGENASE SUBUNIT BETA; 1. DR Pfam; PF13183; Fer4_8; 1. DR Pfam; PF04432; FrhB_FdhB_C; 1. DR Pfam; PF04422; FrhB_FdhB_N; 1. DR SUPFAM; SSF46548; alpha-helical ferredoxin; 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; Repeat; Transport. FT CHAIN 1..394 FT /note="Formate dehydrogenase subunit beta" FT /id="PRO_0000159223" FT DOMAIN 285..315 FT /note="4Fe-4S ferredoxin-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711" FT DOMAIN 337..367 FT /note="4Fe-4S ferredoxin-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711" FT BINDING 295 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000250" FT BINDING 298 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000250" FT BINDING 301 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000250" FT BINDING 305 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000250" FT BINDING 346 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000250" FT BINDING 349 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000250" FT BINDING 352 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000250" FT BINDING 356 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000250" SQ SEQUENCE 394 AA; 43683 MW; F95B3E85B4C44316 CRC64; MVEVNDMYYA FSKNEEIAEK GEYGGAVTSL LKFLLEEGMV DAVLAVKKGS DLYDAVPTLI TEPEKVIESA GSLHCGTLNI AKVITRYLNG AKDIKIAVTT KPCDAMTIVE VAKRGKIDLD NVIMVGVNCG GTLPPVKTRA MIEEVYEMDP DDVVKEEIAK GKLIIETSDA EKGISVDEVE EMGYGRRTNC RRCEKNIPRM ADLALGNWGV IGPLAGKATF VEVTSEKGAD LLEKAVSAGV IEIEDPIPKG IEIREKIDQA MVNLAKKWQK NDFNEETGAE ILMNLDRYMD ELNKCIKCYS CREACPICYC EECSLETKTP EWIEKGKIPP SPLFHLERML HMVDSCTNCG QCEELCPAEI PLAKIWHEIN CRVQETFGYK TGFETGQEPP LTHP //