MTRA_METMA
ID MTRA_METMA Reviewed; 240 AA.
AC O59640;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 26-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 145.
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=MM_1543;
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).
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.
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 Note=Binds 1 5-hydroxybenzimidazolylcobamide group.;
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; AF042381; AAC38334.1; -; Genomic_DNA.
DR EMBL; AE008384; AAM31239.1; -; Genomic_DNA.
DR RefSeq; WP_011033489.1; NC_003901.1.
DR AlphaFoldDB; O59640; -.
DR SMR; O59640; -.
DR STRING; 192952.MM_1543; -.
DR DNASU; 1479885; -.
DR EnsemblBacteria; AAM31239; AAM31239; MM_1543.
DR GeneID; 24879462; -.
DR KEGG; mma:MM_1543; -.
DR PATRIC; fig|192952.21.peg.1784; -.
DR eggNOG; arCOG03221; Archaea.
DR HOGENOM; CLU_100863_0_0_2; -.
DR OMA; EVKGHIT; -.
DR BRENDA; 2.1.1.86; 3270.
DR UniPathway; UPA00640; UER00698.
DR Proteomes; UP000000595; 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_0000147505"
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"
FT CONFLICT 16
FT /note="G -> R (in Ref. 1; AAC38334)"
FT /evidence="ECO:0000305"
FT CONFLICT 71
FT /note="N -> D (in Ref. 1; AAC38334)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="E -> G (in Ref. 1; AAC38334)"
FT /evidence="ECO:0000305"
FT CONFLICT 161
FT /note="D -> E (in Ref. 1; AAC38334)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 240 AA; 25366 MW; 44C086DD3561E526 CRC64;
MADKREPAPG WPILKGEYEV GDVKNSVLVI TCGSHLPGKP ILDAGAACTG SCKTENLGIE
KVVAHIISNP NIRYLLVTGS EVKGHITGQS MMSLHANGVK ENRIAGALGA IPYVENLNAA
AVARFQEQVQ VVNLLDTEDM GAITSKVREL ASKDPGAFDA DPLVVEISEE GEEEEEGGVV
RPVSGEIAVL RSRLKAIEAR MMDIGNLNKF HSGVHAGKVE GAMIGLTITI SLLGLLLLGR
