MTRH_METBF
ID MTRH_METBF Reviewed; 316 AA.
AC O93716; Q46D24;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=Tetrahydromethanopterin S-methyltransferase subunit H {ECO:0000255|HAMAP-Rule:MF_01501};
DE EC=2.1.1.86 {ECO:0000255|HAMAP-Rule:MF_01501};
DE AltName: Full=N5-methyltetrahydromethanopterin--coenzyme M methyltransferase subunit H {ECO:0000255|HAMAP-Rule:MF_01501};
GN Name=mtrH {ECO:0000255|HAMAP-Rule:MF_01501}; OrderedLocusNames=Mbar_A1255;
OS Methanosarcina barkeri (strain Fusaro / DSM 804).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=269797;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fusaro / DSM 804;
RX PubMed=16980466; DOI=10.1128/jb.00810-06;
RA Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT "The Methanosarcina barkeri genome: comparative analysis with
RT Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT rearrangement within methanosarcinal genomes.";
RL J. Bacteriol. 188:7922-7931(2006).
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:0000255|HAMAP-Rule:MF_01501}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01501};
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. {ECO:0000255|HAMAP-Rule:MF_01501}.
CC -!- SUBUNIT: The complex is composed of 8 subunits; MtrA, MtrB, MtrC, MtrD,
CC MtrE, MtrF, MtrG and MtrH. {ECO:0000255|HAMAP-Rule:MF_01501}.
CC -!- SIMILARITY: Belongs to the MtrH family. {ECO:0000255|HAMAP-
CC Rule:MF_01501}.
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DR EMBL; AJ132817; CAA10790.1; -; Genomic_DNA.
DR EMBL; CP000099; AAZ70218.1; -; Genomic_DNA.
DR RefSeq; WP_011306265.1; NC_007355.1.
DR AlphaFoldDB; O93716; -.
DR SMR; O93716; -.
DR STRING; 269797.Mbar_A1255; -.
DR EnsemblBacteria; AAZ70218; AAZ70218; Mbar_A1255.
DR GeneID; 3627855; -.
DR KEGG; mba:Mbar_A1255; -.
DR eggNOG; arCOG04336; Archaea.
DR HOGENOM; CLU_048697_0_0_2; -.
DR OMA; YARHKIV; -.
DR OrthoDB; 86442at2157; -.
DR UniPathway; UPA00640; UER00698.
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 3: Inferred from homology;
KW Methanogenesis; Methyltransferase; One-carbon metabolism; Transferase.
FT CHAIN 1..316
FT /note="Tetrahydromethanopterin S-methyltransferase subunit
FT H"
FT /id="PRO_0000147562"
SQ SEQUENCE 316 AA; 34256 MW; E57FCD869D32CBB4 CRC64;
MFKFDKKQEV FEIGGVKFGG QPGEFPTVLV STMFYARHKI VTDEDKGIFD RAAAETLWNT
QVSLSDATGN PYVNQIVGET PESIKRYIDW FVEIDDRTPF LIDSSAGNVR AAAAQYCTEI
GVADRAIHNS INASIEQEEI DVLTESDVEA AIVLAFNATD PTVKGKMDIL EVGGSGLTKG
MLQISEECGI KYPLIDVAAM PLGAGSGPTI RSIPTMKAKF GLPIGGGYHN MASAWDWLRK
FKKTQPDAKA IYMPADIGTN LVAQIAGSDY LLYGPIENVN QIFPAVAMVD IMLGETAKDL
GVEIADLENH PVTKLT
