MTRH_METMA
ID MTRH_METMA Reviewed; 316 AA.
AC P80650; O59643;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 26-JUL-2002, sequence version 3.
DT 25-MAY-2022, entry version 146.
DE RecName: Full=Tetrahydromethanopterin S-methyltransferase subunit H;
DE EC=2.1.1.86;
DE AltName: Full=N5-methyltetrahydromethanopterin--coenzyme M methyltransferase subunit H;
GN Name=mtrH; OrderedLocusNames=MM_1540;
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=9559648; DOI=10.1016/s0014-5793(98)00229-4;
RA Lienard T., Gottschalk G.;
RT "Cloning, sequencing and expression of the genes encoding the sodium
RT translocating N5-methyltetrahydromethanopterin:coenzyme M methyltransferase
RT of the methylotrophic archaeon Methanosarcina mazei Go1.";
RL FEBS Lett. 425:204-208(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA Fritz H.-J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
RN [3]
RP PROTEIN SEQUENCE OF 1-14.
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=8774736; DOI=10.1111/j.1432-1033.1996.0857u.x;
RA Lienard T., Becher B., Marschall M., Bowien S., Gottschalk G.;
RT "Sodium ion translocation by N5-methyltetrahydromethanopterin: coenzyme M
RT methyltransferase from Methanosarcina mazei Go1 reconstituted in ether
RT lipid liposomes.";
RL Eur. J. Biochem. 239:857-864(1996).
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:0000250}.
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 -!- 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:0000250}.
CC -!- SIMILARITY: Belongs to the MtrH family. {ECO:0000305}.
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DR EMBL; AF042381; AAC38337.1; -; Genomic_DNA.
DR EMBL; AE008384; AAM31236.1; -; Genomic_DNA.
DR RefSeq; WP_011033486.1; NC_003901.1.
DR AlphaFoldDB; P80650; -.
DR SMR; P80650; -.
DR STRING; 192952.MM_1540; -.
DR EnsemblBacteria; AAM31236; AAM31236; MM_1540.
DR GeneID; 44088832; -.
DR GeneID; 66136930; -.
DR KEGG; mma:MM_1540; -.
DR PATRIC; fig|192952.21.peg.1781; -.
DR eggNOG; arCOG04336; Archaea.
DR HOGENOM; CLU_048697_0_0_2; -.
DR OMA; YARHKIV; -.
DR BRENDA; 2.1.1.86; 3270.
DR UniPathway; UPA00640; UER00698.
DR Proteomes; UP000000595; Chromosome.
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 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; Reference proteome; Transferase.
FT CHAIN 1..316
FT /note="Tetrahydromethanopterin S-methyltransferase subunit
FT H"
FT /id="PRO_0000147565"
FT CONFLICT 59
FT /note="N -> D (in Ref. 1; AAC38337)"
FT /evidence="ECO:0000305"
FT CONFLICT 65
FT /note="S -> G (in Ref. 1; AAC38337)"
FT /evidence="ECO:0000305"
FT CONFLICT 77..79
FT /note="VGE -> CRG (in Ref. 1; AAC38337)"
FT /evidence="ECO:0000305"
FT CONFLICT 91
FT /note="F -> V (in Ref. 1; AAC38337)"
FT /evidence="ECO:0000305"
FT CONFLICT 98..109
FT /note="TPFLIDSSAGNV -> HLSDRLSAER (in Ref. 1; AAC38337)"
FT /evidence="ECO:0000305"
FT CONFLICT 131
FT /note="I -> L (in Ref. 1; AAC38337)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="K -> E (in Ref. 1; AAC38337)"
FT /evidence="ECO:0000305"
FT CONFLICT 290
FT /note="D -> A (in Ref. 1; AAC38337)"
FT /evidence="ECO:0000305"
FT CONFLICT 295
FT /note="E -> G (in Ref. 1; AAC38337)"
FT /evidence="ECO:0000305"
FT CONFLICT 307
FT /note="L -> W (in Ref. 1; AAC38337)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 316 AA; 34044 MW; 33726B6EC1109FDD CRC64;
MFKFDKKQEV FELGGVKFGG QPGENPTVLV STMFYARHKI VTDEDKGIFD RAAAETLWNT
QVSLSDATGL PYVNQIVGET PESIKRYIEW FVGIDDRTPF LIDSSAGNVR AAAAQYCTEI
GVADRAIHNS INASIEQSEI DVLTESDVSA AIVLAFNATD PTVKGKIDIL EVGGSGQTKG
MLQVAKECGI KYPIIDVAAM PLGAGSGATI RSVPTLKGKF GLPIGGGYHN MASAWDWLRK
FKKTQPDPKA IYMPTDIGTN LVAQIAGSDY LLYGPIENVN QIFPAVAMVD IMLGETAKEL
GVEIADLENH PVTKLT
