ID HMD_METWO Reviewed; 19 AA. AC P32441; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1993, sequence version 1. DT 02-SEP-2026, entry version 69. DE RecName: Full=5,10-methenyltetrahydromethanopterin hydrogenase; DE EC=1.12.98.2 {ECO:0000269|PubMed:1521540}; DE AltName: Full=H(2)-dependent methylene-H(4)MPT dehydrogenase; DE AltName: Full=H(2)-forming N(5),N(10)-methylenetetrahydromethanopterin dehydrogenase {ECO:0000303|PubMed:1521540}; DE AltName: Full=N(5),N(10)-methenyltetrahydromethanopterin hydrogenase; DE AltName: Full=[Fe]-hydrogenase; DE Flags: Fragment; GN Name=hmd {ECO:0000250|UniProtKB:P32440}; OS Methanothermobacter wolfeii (Methanobacterium wolfei). OC Archaea; Methanobacteriati; Methanobacteriota; Methanomada group; OC Methanobacteria; Methanobacteriales; Methanobacteriaceae; OC Methanothermobacter. OX NCBI_TaxID=145261; RN [1] RP PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND RP PATHWAY. RC STRAIN=ATCC 43096 / DSM 2970 / JCM 14652 / NBRC 100332 / VKM B-1829; RX PubMed=1521540; DOI=10.1111/j.1432-1033.1992.tb17215.x; RA Zirngibl C., van Dongen W., Schwoerer B., von Buenau R., Richter M., RA Klein A., Thauer R.K.; RT "H2-forming methylenetetrahydromethanopterin dehydrogenase, a novel type of RT hydrogenase without iron-sulfur clusters in methanogenic archaea."; RL Eur. J. Biochem. 208:511-520(1992). CC -!- FUNCTION: Catalyzes the reversible reduction of methenyl-H(4)MPT(+) to CC methylene-H(4)MPT. {ECO:0000269|PubMed:1521540}. CC -!- CATALYTIC ACTIVITY: CC Reaction=5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2 = 5,10- CC methylenetetrahydromethanopterin + H(+); Xref=Rhea:RHEA:20017, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:18276, ChEBI:CHEBI:57818, CC ChEBI:CHEBI:58337; EC=1.12.98.2; CC Evidence={ECO:0000269|PubMed:1521540}; CC -!- ACTIVITY REGULATION: Very sensitive to O(2). CC {ECO:0000269|PubMed:1521540}. CC -!- PATHWAY: One-carbon metabolism; methanogenesis from CO(2); 5,10- CC methylene-5,6,7,8-tetrahydromethanopterin from 5,10-methenyl-5,6,7,8- CC tetrahydromethanopterin (hydrogen route): step 1/1. CC {ECO:0000269|PubMed:1521540}. CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q02394}. CC -!- SIMILARITY: Belongs to the HMD 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 AlphaFoldDB; P32441; -. DR STRING; 145261.MWSIV6_1534; -. DR BRENDA; 1.12.98.2; 3258. DR UniPathway; UPA00640; UER00696. DR GO; GO:0047068; F:N5,N10-methenyltetrahydromethanopterin hydrogenase activity; EXP:UniProtKB. DR GO; GO:0019386; P:methanogenesis, from carbon dioxide; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR055205; HMD_N. DR Pfam; PF22616; HMD_N; 1. PE 1: Evidence at protein level; KW Direct protein sequencing; Methanogenesis; One-carbon metabolism; KW Oxidoreductase. FT CHAIN <1..19 FT /note="5,10-methenyltetrahydromethanopterin hydrogenase" FT /id="PRO_0000218516" FT NON_TER 1 SQ SEQUENCE 19 AA; 1911 MW; 0C17E9D7BF1F97C9 CRC64; MKLAILGAGC YRTDAASGI //