MTRH_METTM
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 25-MAY-2022, entry version 115.
DE RecName: Full=Tetrahydromethanopterin S-methyltransferase subunit H;
DE EC=2.1.1.86 {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; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; 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=2.1.1.86;
CC 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 5-methyl-5,6,7,8-
CC tetrahydromethanopterin is estimated. {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}.
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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 EnsemblBacteria; ADL59119; ADL59119; MTBMA_c15400.
DR GeneID; 9705249; -.
DR KEGG; mmg:MTBMA_c15400; -.
DR PATRIC; fig|79929.8.peg.1493; -.
DR HOGENOM; CLU_048697_0_0_2; -.
DR OMA; YARHKIV; -.
DR OrthoDB; 86442at2157; -.
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-UniPathway.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.20.20.20; -; 1.
DR HAMAP; MF_01501; MtrH; 1.
DR InterPro; IPR011005; Dihydropteroate_synth-like.
DR InterPro; IPR023467; MeTrfase_MtrH/MtxH.
DR InterPro; IPR028342; MtrH.
DR Pfam; PF02007; MtrH; 1.
DR PIRSF; PIRSF500206; MtrH; 1.
DR PIRSF; PIRSF004960; MtrH_MtxH; 1.
DR SUPFAM; SSF51717; SSF51717; 1.
DR TIGRFAMs; TIGR01114; mtrH; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Methanogenesis; Methyltransferase;
KW One-carbon metabolism; Transferase.
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
