ID HMD_METTM Reviewed; 344 AA. AC P32440; D9PY07; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 30-NOV-2010, sequence version 3. DT 04-NOV-2026, entry version 137. DE RecName: Full=5,10-methenyltetrahydromethanopterin hydrogenase; DE EC=1.12.98.2 {ECO:0000269|PubMed:1765081}; 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; GN Name=hmd {ECO:0000303|PubMed:1765081}; OrderedLocusNames=MTBMA_c15260; OS Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM OS 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium OS thermoautotrophicum). OC Archaea; Methanobacteriati; Methanobacteriota; Methanomada group; OC Methanobacteria; Methanobacteriales; Methanobacteriaceae; OC Methanothermobacter. OX NCBI_TaxID=79929; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY. RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / RC Marburg; RX PubMed=1765081; DOI=10.1111/j.1432-1033.1991.tb16491.x; RA Von Buenau R., Zirngibl C., Thauer R.K., Klein A.; RT "Hydrogen-forming and coenzyme-F420-reducing methylene RT tetrahydromethanopterin dehydrogenase are genetically distinct enzymes in RT Methanobacterium thermoautotrophicum (Marburg)."; RL Eur. J. Biochem. 202:1205-1208(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / RC Marburg; RX PubMed=20802048; DOI=10.1128/jb.00844-10; RA Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H., RA Gottschalk G., Thauer R.K.; RT "Complete genome sequence of Methanothermobacter marburgensis, a RT methanoarchaeon model organism."; RL J. Bacteriol. 192:5850-5851(2010). RN [3] RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL RP PROPERTIES. RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / RC Marburg; 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:1765081}. 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, ECO:0000269|PubMed:1765081}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20018; CC Evidence={ECO:0000269|PubMed:1521540}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:20019; CC Evidence={ECO:0000269|PubMed:1521540}; CC -!- ACTIVITY REGULATION: Activity requires salt; 100 mM sodium or potassium CC salts of chloride, phosphate or sulfate are equally effective. CC Inactivated by O(2). {ECO:0000269|PubMed:1521540, CC ECO:0000269|PubMed:1765081}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=20 uM for 5,10-methylenetetrahydromethanopterin CC {ECO:0000269|PubMed:1765081}; CC KM=40 uM for 5,10-methylenetetrahydromethanopterin CC {ECO:0000269|PubMed:1521540}; CC KM=50 uM for 5,10-methenyl-5,6,7,8-tetrahydromethanopterin CC {ECO:0000269|PubMed:1521540}; CC pH dependence: CC Optimum pH is 6.0-6.5 when making H(2) and 7.5 in the other CC direction. {ECO:0000269|PubMed:1521540, ECO:0000269|PubMed:1765081}; CC Temperature dependence: CC Optimum temperature is 60 degrees Celsius. CC {ECO:0000269|PubMed:1521540, ECO:0000269|PubMed:1765081}; 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, ECO:0000269|PubMed:1765081}. 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 EMBL; X59547; CAA42121.1; -; Genomic_DNA. DR EMBL; CP001710; ADL59105.1; -; Genomic_DNA. DR PIR; S19705; S19705. DR RefSeq; WP_013296316.1; NC_014408.1. DR PDB; 4JJF; X-ray; 2.20 A; A/B=1-344. DR PDB; 4JJG; X-ray; 2.50 A; A/B=1-344. DR PDB; 5OK4; X-ray; 1.29 A; A=1-344. DR PDB; 6GGU; X-ray; 2.60 A; A=1-344. DR AlphaFoldDB; P32440; -. DR SMR; P32440; -. DR STRING; 79929.MTBMA_c15260; -. DR PaxDb; 79929-MTBMA_c15260; -. DR GeneID; 77400297; -. DR GeneID; 9705235; -. DR KEGG; mmg:MTBMA_c15260; -. DR PATRIC; fig|79929.8.peg.1479; -. DR HOGENOM; CLU_772960_0_0_2; -. DR OMA; ACIHFVH; -. DR OrthoDB; 113982at2157; -. DR BRENDA; 1.12.98.2; 7427. DR UniPathway; UPA00640; UER00696. DR EvolutionaryTrace; P32440; -. DR Proteomes; UP000000345; Chromosome. DR GO; GO:0047068; F:N5,N10-methenyltetrahydromethanopterin hydrogenase activity; IDA:MENGO. DR GO; GO:0019386; P:methanogenesis, from carbon dioxide; IEA:UniProtKB-UniRule. DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-UniRule. DR FunFam; 1.20.120.1300:FF:000001; 5,10-methenyltetrahydromethanopterin hydrogenase; 1. DR FunFam; 3.40.50.720:FF:001042; 5,10-methenyltetrahydromethanopterin hydrogenase; 1. DR Gene3D; 1.20.120.1300; Hmd, C-terminal helical subdomain; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR HAMAP; MF_01090; HMD; 1. DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf. DR InterPro; IPR010062; HMD. DR InterPro; IPR004889; HMD_C. DR InterPro; IPR038182; HMD_C_sf. DR InterPro; IPR055205; HMD_N. DR InterPro; IPR024190; METHMP_Hmd. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR NCBIfam; TIGR01723; hmd_TIGR; 1. DR PANTHER; PTHR11645; PYRROLINE-5-CARBOXYLATE REDUCTASE; 1. DR PANTHER; PTHR11645:SF0; PYRROLINE-5-CARBOXYLATE REDUCTASE 3; 1. DR Pfam; PF03201; HMD; 1. DR Pfam; PF22616; HMD_N; 1. DR PIRSF; PIRSF016158; HMD; 1. DR PIRSF; PIRSF500165; HMDI; 1. DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. PE 1: Evidence at protein level; KW 3D-structure; Methanogenesis; One-carbon metabolism; Oxidoreductase; KW Reference proteome. FT CHAIN 1..344 FT /note="5,10-methenyltetrahydromethanopterin hydrogenase" FT /id="PRO_0000218512" FT CONFLICT 74..75 FT /note="DD -> EH (in Ref. 1; CAA42121)" FT /evidence="ECO:0000305" FT CONFLICT 91 FT /note="K -> N (in Ref. 1; CAA42121)" FT /evidence="ECO:0000305" FT CONFLICT 261 FT /note="I -> M (in Ref. 1; CAA42121)" FT /evidence="ECO:0000305" FT CONFLICT 265 FT /note="G -> C (in Ref. 1; CAA42121)" FT /evidence="ECO:0000305" FT CONFLICT 304..305 FT /note="ID -> RY (in Ref. 1; CAA42121)" FT /evidence="ECO:0000305" FT STRAND 2..6 FT /evidence="ECO:0007829|PDB:5OK4" FT HELIX 12..17 FT /evidence="ECO:0007829|PDB:5OK4" FT HELIX 23..32 FT /evidence="ECO:0007829|PDB:5OK4" FT HELIX 35..39 FT /evidence="ECO:0007829|PDB:5OK4" FT HELIX 42..53 FT /evidence="ECO:0007829|PDB:5OK4" FT STRAND 58..62 FT /evidence="ECO:0007829|PDB:5OK4" FT HELIX 64..67 FT /evidence="ECO:0007829|PDB:5OK4" FT STRAND 69..72 FT /evidence="ECO:0007829|PDB:5OK4" FT HELIX 78..87 FT /evidence="ECO:0007829|PDB:5OK4" FT HELIX 89..91 FT /evidence="ECO:0007829|PDB:5OK4" FT HELIX 93..106 FT /evidence="ECO:0007829|PDB:5OK4" FT TURN 110..112 FT /evidence="ECO:0007829|PDB:5OK4" FT STRAND 113..118 FT /evidence="ECO:0007829|PDB:5OK4" FT HELIX 120..123 FT /evidence="ECO:0007829|PDB:5OK4" FT STRAND 126..129 FT /evidence="ECO:0007829|PDB:5OK4" FT HELIX 131..135 FT /evidence="ECO:0007829|PDB:5OK4" FT STRAND 139..143 FT /evidence="ECO:0007829|PDB:5OK4" FT HELIX 148..150 FT /evidence="ECO:0007829|PDB:5OK4" FT HELIX 151..155 FT /evidence="ECO:0007829|PDB:5OK4" FT TURN 156..158 FT /evidence="ECO:0007829|PDB:5OK4" FT HELIX 159..161 FT /evidence="ECO:0007829|PDB:5OK4" FT STRAND 167..169 FT /evidence="ECO:0007829|PDB:5OK4" FT HELIX 176..183 FT /evidence="ECO:0007829|PDB:5OK4" FT TURN 186..188 FT /evidence="ECO:0007829|PDB:4JJF" FT TURN 190..192 FT /evidence="ECO:0007829|PDB:4JJF" FT HELIX 194..196 FT /evidence="ECO:0007829|PDB:4JJF" FT STRAND 198..200 FT /evidence="ECO:0007829|PDB:5OK4" FT TURN 208..210 FT /evidence="ECO:0007829|PDB:5OK4" FT STRAND 214..221 FT /evidence="ECO:0007829|PDB:5OK4" FT HELIX 223..237 FT /evidence="ECO:0007829|PDB:5OK4" FT STRAND 240..244 FT /evidence="ECO:0007829|PDB:5OK4" FT HELIX 245..247 FT /evidence="ECO:0007829|PDB:5OK4" FT HELIX 249..251 FT /evidence="ECO:0007829|PDB:5OK4" FT TURN 253..255 FT /evidence="ECO:0007829|PDB:5OK4" FT HELIX 256..271 FT /evidence="ECO:0007829|PDB:5OK4" FT HELIX 272..277 FT /evidence="ECO:0007829|PDB:5OK4" FT HELIX 281..302 FT /evidence="ECO:0007829|PDB:5OK4" FT HELIX 304..309 FT /evidence="ECO:0007829|PDB:5OK4" FT HELIX 313..316 FT /evidence="ECO:0007829|PDB:5OK4" FT HELIX 317..320 FT /evidence="ECO:0007829|PDB:5OK4" FT HELIX 321..323 FT /evidence="ECO:0007829|PDB:5OK4" FT HELIX 328..342 FT /evidence="ECO:0007829|PDB:5OK4" SQ SEQUENCE 344 AA; 37654 MW; A34EFC260D324025 CRC64; MKLAILGAGC YRTHAASGIT NFSRACEVAE MVGKPEIAMT HSTITMGAEL KELAGVDEVV VADPVFDNQF TVIDDFAYED VIEAHKEDPE KIMPQIREKV NEVAKELPKP PEGAIHFTHP EDLGFEITTD DREAVADADF IMTWFPKGDM QPDIINKFID DIKPGAIVTH ACTIPTTKFY KIFEQKHGDL VTKPETLNVT SYHPGAVPEM KGQVYIAEGY ASEDAIETLF ELGQKARGNA YRLPAELLGP VCDMCSALTA ITYAGILSYR DSVTQVLGAP ASFAQMMAKE SLEQITALME KVGIDKMEEN LDPGALLGTA DSMNFGASAE ILPTVFEILE KRKK //