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Database: UniProt/SWISS-PROT
Entry: MTRH_METVS
LinkDB: MTRH_METVS
Original site: MTRH_METVS 
ID   MTRH_METVS              Reviewed;         319 AA.
AC   A6UQL3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 77.
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=Mevan_0880;
OS   Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148
OS   / SB).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=406327;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Anderson I.,
RA   Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of Methanococcus vannielii SB.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000742; ABR54785.1; -; Genomic_DNA.
DR   RefSeq; WP_011972686.1; NC_009634.1.
DR   AlphaFoldDB; A6UQL3; -.
DR   SMR; A6UQL3; -.
DR   STRING; 406327.Mevan_0880; -.
DR   GeneID; 5326203; -.
DR   KEGG; mvn:Mevan_0880; -.
DR   eggNOG; arCOG04336; Archaea.
DR   HOGENOM; CLU_048697_0_0_2; -.
DR   OrthoDB; 18811at2157; -.
DR   UniPathway; UPA00640; UER00698.
DR   Proteomes; UP000001107; 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   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   Pfam; PF02007; MtrH; 1.
DR   PIRSF; PIRSF500206; MtrH; 1.
DR   PIRSF; PIRSF004960; MtrH_MtxH; 1.
DR   SUPFAM; SSF51717; Dihydropteroate synthetase-like; 1.
PE   3: Inferred from homology;
KW   Methanogenesis; Methyltransferase; One-carbon metabolism; Transferase.
FT   CHAIN           1..319
FT                   /note="Tetrahydromethanopterin S-methyltransferase subunit
FT                   H"
FT                   /id="PRO_1000024473"
SQ   SEQUENCE   319 AA;  34222 MW;  02CB3953DCCCF298 CRC64;
     MFRFDKEQMV IDFAGAKFGG QPGEYPTALS GTIFYARHKI VEDAKKGIFD KKAAEALINK
     QAEMQDITGN SALVQVFGGT EEALVNYIDF VSEVWEGPML LDSTSGKARM AAAKRATEAG
     YAKQCIYNSI NVSIDEEEFQ SLAESDVEAS IVLCFDPMDP SVEGKLNVLN NGGKTKDVGM
     LDLAEKAGIK YPLIDVAVTP MGAGAGNAVR ASFAVKAKLG LAVGSGIHNV PSAWDWLREF
     RKGLREEGKE QIAKDVHHVC DIGANIVQTM ASGDFVLYGP IDNAELAFPA VAMTDMIIAE
     TAKELGTTPA AVHPLNKLI
//
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