ID MTRH_METTM Reviewed; 310 AA. AC P80187; D9PY21; Q50775; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 02-SEP-2026, entry version 129. DE RecName: Full=Tetrahydromethanopterin S-methyltransferase subunit H; DE EC=7.2.1.4 {ECO:0000269|PubMed:8477726}; DE AltName: Full=N5-methyltetrahydromethanopterin--coenzyme M methyltransferase subunit H; GN Name=mtrH; OrderedLocusNames=MTBMA_c15400; 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], PARTIAL PROTEIN SEQUENCE, SUBUNIT, AND RP OPERON STRUCTURE. RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / RC Marburg; RX PubMed=7737157; DOI=10.1111/j.1432-1033.1995.0640m.x; RA Harms U., Weiss D.S., Gaertner P., Linder D., Thauer R.K.; RT "The energy conserving N5-methyltetrahydromethanopterin:coenzyme M RT methyltransferase complex from Methanobacterium thermoautotrophicum is RT composed of eight different subunits."; RL Eur. J. Biochem. 228:640-648(1995). 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 PROTEIN SEQUENCE OF 1-30, FUNCTION, CATALYTIC ACTIVITY, AND RP BIOPHYSICOCHEMICAL PROPERTIES. RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / RC Marburg; RX PubMed=8477726; DOI=10.1111/j.1432-1033.1993.tb17792.x; RA Gaertner P., Ecker A., Fischer R., Linder D., Fuchs G., Thauer R.K.; RT "Purification and properties of N5-methyltetrahydromethanopterin:coenzyme M RT methyltransferase from Methanobacterium thermoautotrophicum."; RL Eur. J. Biochem. 213:537-545(1993). RN [4] RP FUNCTION. RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / RC Marburg; RX PubMed=10338124; DOI=10.1016/s0014-5793(99)00429-9; RA Hippler B., Thauer R.K.; RT "The energy conserving methyltetrahydromethanopterin:coenzyme M RT methyltransferase complex from methanogenic archaea: function of the RT subunit MtrH."; RL FEBS Lett. 449:165-168(1999). CC -!- FUNCTION: Part of a complex that catalyzes the formation of methyl- CC coenzyme M and tetrahydromethanopterin from coenzyme M and methyl- CC tetrahydromethanopterin. This is an energy-conserving, sodium-ion CC translocating step. MtrH catalyzes the transfer of the methyl group CC from methyl-tetrahydromethanopterin to the corrinoid prosthetic group CC of MtrA. {ECO:0000269|PubMed:10338124, ECO:0000269|PubMed:8477726}. CC -!- CATALYTIC ACTIVITY: CC Reaction=5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme M + 2 CC Na(+)(in) = 5,6,7,8-tetrahydromethanopterin + methyl-coenzyme M + 2 CC Na(+)(out); Xref=Rhea:RHEA:53492, ChEBI:CHEBI:29101, CC ChEBI:CHEBI:58103, ChEBI:CHEBI:58116, ChEBI:CHEBI:58286, CC ChEBI:CHEBI:58319; EC=7.2.1.4; Evidence={ECO:0000269|PubMed:8477726}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=260 uM for 5-methyl-5,6,7,8-tetrahydromethanopterin CC {ECO:0000269|PubMed:8477726}; CC KM=60 uM for coenzyme M {ECO:0000269|PubMed:8477726}; CC Vmax=11.6 umol/min/mg enzyme {ECO:0000269|PubMed:8477726}; CC Note=From other experiments a much lower Km for CC 5-methyl-5,6,7,8-tetrahydromethanopterin is estimated. CC {ECO:0000269|PubMed:8477726}; CC -!- PATHWAY: One-carbon metabolism; methanogenesis from CO(2); methyl- CC coenzyme M from 5,10-methylene-5,6,7,8-tetrahydromethanopterin: step CC 2/2. CC -!- SUBUNIT: The complex is composed of 8 subunits; MtrA, MtrB, MtrC, MtrD, CC MtrE, MtrF, MtrG and MtrH. {ECO:0000269|PubMed:7737157}. CC -!- INDUCTION: The last gene of the probable mtrEDCBAFGH operon. CC {ECO:0000305|PubMed:7737157}. CC -!- SIMILARITY: Belongs to the MtrH 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; X84219; CAA59003.1; -; Genomic_DNA. DR EMBL; CP001710; ADL59119.1; -; Genomic_DNA. DR RefSeq; WP_013296329.1; NC_014408.1. DR AlphaFoldDB; P80187; -. DR SMR; P80187; -. DR STRING; 79929.MTBMA_c15400; -. DR TCDB; 3.C.1.1.1; the na(+) transporting methyltetrahydromethanopterin:coenzyme m methyltransferase (nat-mmm) family. DR PaxDb; 79929-MTBMA_c15400; -. DR GeneID; 77400311; -. DR GeneID; 9705249; -. DR KEGG; mmg:MTBMA_c15400; -. DR PATRIC; fig|79929.8.peg.1493; -. DR HOGENOM; CLU_048697_0_0_2; -. DR OrthoDB; 18811at2157; -. DR BRENDA; 7.2.1.4; 7427. DR UniPathway; UPA00640; UER00698. DR Proteomes; UP000000345; Chromosome. DR GO; GO:0034708; C:methyltransferase complex; IDA:UniProtKB. DR GO; GO:0030269; F:tetrahydromethanopterin S-methyltransferase activity; IEA:UniProtKB-UniRule. 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 Gene3D; 3.20.20.20; Dihydropteroate synthase-like; 1. DR HAMAP; MF_01501; MtrH; 1. DR InterPro; IPR011005; Dihydropteroate_synth-like_sf. DR InterPro; IPR023467; MeTrfase_MtrH/MtxH. DR InterPro; IPR028342; MtrH. DR NCBIfam; TIGR01114; mtrH; 1. DR NCBIfam; NF002142; PRK00979.1-1; 1. DR Pfam; PF02007; MtrH; 1. DR PIRSF; PIRSF500206; MtrH; 1. DR PIRSF; PIRSF004960; MtrH_MtxH; 1. DR SUPFAM; SSF51717; Dihydropteroate synthetase-like; 1. PE 1: Evidence at protein level; KW Direct protein sequencing; Methanogenesis; Methyltransferase; KW One-carbon metabolism; Reference proteome; Transferase; Translocase. FT CHAIN 1..310 FT /note="Tetrahydromethanopterin S-methyltransferase subunit FT H" FT /id="PRO_0000147568" SQ SEQUENCE 310 AA; 33474 MW; EB3B44FDD73F2A66 CRC64; MFRFDKEQIV LDIAGTKIGG QPGEYPTVLA GTIFYGGHSI IEDEKAGVFD KDKAEALIKT QEEMSDVTGN PHIVQTFGQT PEAIVKYLEF VGDITDAPFF IDSTSGEARI AGAEYASEVG LEDRAIYNSV NMAADESELE ALKNTKLSAS IVLGFNPMDP TVEGKIGIWE DGAGTIDKGL LEMAADCGID KYLMDVAVTP LGQGAGVAVR TSFAVKSKWG YPVGSGIHNV PSAWDWLREY KKEHKEAWPV CDVGSNLIQQ MAGGDFVLYG PIENARMAFP ACAMADIFIS EAAKDIGTEA VEDHPFFKLL //