ID MTRA_METBF Reviewed; 240 AA.
AC Q9Y8K4; Q46D21;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 27-MAR-2024, entry version 128.
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=Mbar_A1258;
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. {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; AJ132817; CAB41642.1; -; Genomic_DNA.
DR EMBL; CP000099; AAZ70221.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9Y8K4; -.
DR SMR; Q9Y8K4; -.
DR STRING; 269797.Mbar_A1258; -.
DR PaxDb; 269797-Mbar_A1258; -.
DR GeneID; 24825090; -.
DR KEGG; mba:Mbar_A1258; -.
DR eggNOG; arCOG03221; Archaea.
DR HOGENOM; CLU_100863_0_0_2; -.
DR OrthoDB; 130682at2157; -.
DR UniPathway; UPA00640; UER00698.
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 NCBIfam; TIGR01111; mtrA; 1.
DR Pfam; PF04208; MtrA; 1.
DR PIRSF; PIRSF500207; MtrA; 1.
DR PIRSF; PIRSF009452; MtrA_MtxA; 1.
PE 3: Inferred from homology;
KW Cell membrane; Cobalt; Membrane; Methanogenesis; Methyltransferase;
KW One-carbon metabolism; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..240
FT /note="Tetrahydromethanopterin S-methyltransferase subunit
FT A"
FT /id="PRO_0000147502"
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; 25413 MW; A3D04EB09F6AD3A4 CRC64;
MADKKEPAPG WPILKGEYEV GDVKNCVLVI TCGSHLPGQP ILDAGAAVTG SCKTENLGIE
KVVAHIISNP NIRYLLVTGS EVKGHITGQS VMSLHANGVK DNRISGALGA IPYVENLNED
AIARFQEQVD VVNLLDTEDM GAITSKVKEL ASKDPGAFDA EPMIVEISEE GEEEEEGGAV
RPVSGEIAVI RSRLKAIEAR MMDIGNLNKF HSGVHAGKIE GAMIGLTVTI SLLGLLLLGR
//
