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MTRA_METAC
ID   MTRA_METAC              Reviewed;         240 AA.
AC   Q8TU03;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Tetrahydromethanopterin S-methyltransferase subunit A {ECO:0000255|HAMAP-Rule:MF_01093};
DE            EC=2.1.1.86 {ECO:0000255|HAMAP-Rule:MF_01093};
DE   AltName: Full=N5-methyltetrahydromethanopterin--coenzyme M methyltransferase subunit A {ECO:0000255|HAMAP-Rule:MF_01093};
GN   Name=mtrA {ECO:0000255|HAMAP-Rule:MF_01093}; OrderedLocusNames=MA_0272;
OS   Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS   C2A).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=188937;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX   PubMed=11932238; DOI=10.1101/gr.223902;
RA   Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA   Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA   Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA   McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA   Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA   Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA   Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA   White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA   Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA   Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT   "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT   physiological diversity.";
RL   Genome Res. 12:532-542(2002).
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. {ECO:0000255|HAMAP-Rule:MF_01093}.
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_01093};
CC   -!- COFACTOR:
CC       Name=5-hydroxybenzimidazolylcob(I)amide; Xref=ChEBI:CHEBI:60494;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01093};
CC       Note=Binds 1 5-hydroxybenzimidazolylcobamide group. {ECO:0000255|HAMAP-
CC       Rule:MF_01093};
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_01093}.
CC   -!- SUBUNIT: The complex is composed of 8 subunits; MtrA, MtrB, MtrC, MtrD,
CC       MtrE, MtrF, MtrG and MtrH. {ECO:0000255|HAMAP-Rule:MF_01093}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01093};
CC       Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01093}.
CC   -!- SIMILARITY: Belongs to the MtrA family. {ECO:0000255|HAMAP-
CC       Rule:MF_01093}.
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DR   EMBL; AE010299; AAM03725.1; -; Genomic_DNA.
DR   RefSeq; WP_011020330.1; NC_003552.1.
DR   AlphaFoldDB; Q8TU03; -.
DR   SMR; Q8TU03; -.
DR   STRING; 188937.MA_0272; -.
DR   PRIDE; Q8TU03; -.
DR   EnsemblBacteria; AAM03725; AAM03725; MA_0272.
DR   GeneID; 1472164; -.
DR   KEGG; mac:MA_0272; -.
DR   HOGENOM; CLU_100863_0_0_2; -.
DR   InParanoid; Q8TU03; -.
DR   OMA; EVKGHIT; -.
DR   OrthoDB; 89197at2157; -.
DR   PhylomeDB; Q8TU03; -.
DR   UniPathway; UPA00640; UER00698.
DR   Proteomes; UP000002487; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0050897; F:cobalt ion binding; IEA:InterPro.
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   GO; GO:0006814; P:sodium ion transport; IEA:InterPro.
DR   HAMAP; MF_01093; MtrA; 1.
DR   InterPro; IPR030688; MeTrfase_MtrA/MtxA.
DR   InterPro; IPR005778; MtrA.
DR   Pfam; PF04208; MtrA; 1.
DR   PIRSF; PIRSF500207; MtrA; 1.
DR   PIRSF; PIRSF009452; MtrA_MtxA; 1.
DR   TIGRFAMs; TIGR01111; mtrA; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Cobalt; Membrane; Methanogenesis; Methyltransferase;
KW   One-carbon metabolism; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..240
FT                   /note="Tetrahydromethanopterin S-methyltransferase subunit
FT                   A"
FT                   /id="PRO_0000147501"
FT   TOPO_DOM        1..218
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01093"
FT   TRANSMEM        219..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01093"
FT   TOPO_DOM        240
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01093"
FT   BINDING         85
FT                   /ligand="5-hydroxybenzimidazolylcob(I)amide"
FT                   /ligand_id="ChEBI:CHEBI:60494"
FT                   /ligand_note="cofactor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01093"
SQ   SEQUENCE   240 AA;  25342 MW;  E6D81A2B358D2079 CRC64;
     MVDKKEPASG WPILKGEYEV GDVKGCVAVI TCASHLPGKP VLDAGAAITG SCKTENLGIE
     KVVAHVISNP NIRYLVVTGA EVKGHVTGQA MLSIHANGVK EHRIVGAVGA IPYVENLNDD
     AVARFQQQIE TVNLLDTEDM GAITAKVREL VAKDPGAFDA EPMVVEISEE GEEEEEGGVV
     RPVSGEIAVI RSRLKAIEAR MLDIGNLNKF HSGVHAGKIE GAMIGLTVTI SLLGLLLLGR
 
 
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