ID A0A109UVP0_9EURY Unreviewed; 238 AA.
AC A0A109UVP0;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Tetrahydromethanopterin S-methyltransferase subunit A {ECO:0000256|HAMAP-Rule:MF_01093};
DE EC=2.1.1.86 {ECO:0000256|HAMAP-Rule:MF_01093};
DE AltName: Full=N5-methyltetrahydromethanopterin--coenzyme M methyltransferase subunit A {ECO:0000256|HAMAP-Rule:MF_01093};
GN Name=mtrA {ECO:0000256|HAMAP-Rule:MF_01093};
GN ORFNames=TL18_09295 {ECO:0000313|EMBL:AMD18192.1};
OS Methanobrevibacter sp. YE315.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=1609968 {ECO:0000313|EMBL:AMD18192.1, ECO:0000313|Proteomes:UP000057992};
RN [1] {ECO:0000313|EMBL:AMD18192.1, ECO:0000313|Proteomes:UP000057992}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YE315 {ECO:0000313|EMBL:AMD18192.1,
RC ECO:0000313|Proteomes:UP000057992};
RA Ouwerkerk D., Gilbert R.A., Klieve A.V., Martinez E.;
RT "Genome sequence of Methanobrevibacter sp. YE315.";
RL Submitted (JAN-2015) 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. {ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_01093};
CC -!- COFACTOR:
CC Name=5-hydroxybenzimidazolylcob(I)amide; Xref=ChEBI:CHEBI:60494;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01093};
CC Note=Binds 1 5-hydroxybenzimidazolylcobamide group. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01093}.
CC -!- SUBUNIT: The complex is composed of 8 subunits; MtrA, MtrB, MtrC, MtrD,
CC MtrE, MtrF, MtrG and MtrH. {ECO:0000256|HAMAP-Rule:MF_01093}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01093};
CC Single-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01093}.
CC -!- SIMILARITY: Belongs to the MtrA family. {ECO:0000256|HAMAP-
CC Rule:MF_01093}.
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DR EMBL; CP010834; AMD18192.1; -; Genomic_DNA.
DR RefSeq; WP_067044647.1; NZ_CP010834.1.
DR AlphaFoldDB; A0A109UVP0; -.
DR STRING; 1609968.TL18_09295; -.
DR GeneID; 28488053; -.
DR KEGG; meye:TL18_09295; -.
DR PATRIC; fig|1609968.3.peg.1894; -.
DR OrthoDB; 130682at2157; -.
DR UniPathway; UPA00640; UER00698.
DR Proteomes; UP000057992; Chromosome.
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 {ECO:0000256|HAMAP-Rule:MF_01093};
KW Cobalt {ECO:0000256|HAMAP-Rule:MF_01093};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_01093};
KW Methanogenesis {ECO:0000256|HAMAP-Rule:MF_01093};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_01093}; One-carbon metabolism {ECO:0000256|HAMAP-Rule:MF_01093};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01093, ECO:0000313|EMBL:AMD18192.1};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_01093};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01093}.
FT TRANSMEM 218..237
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01093"
FT BINDING 82
FT /ligand="5-hydroxybenzimidazolylcob(I)amide"
FT /ligand_id="ChEBI:CHEBI:60494"
FT /ligand_note="cofactor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01093"
SQ SEQUENCE 238 AA; 25260 MW; 69BBB5A81247C510 CRC64;
MADKKAPADG WPVISGDYIV GDPESPVAVT TLASHIEAEL SGAAIAGPCK TENLGIEKVV
ANIISNPNIR FLILAGAEVQ GHITGQSIQA LYDNGADPDK KKIIGATGAI PFVENVPLEG
IERFQQQLEI VDLIDTEDIG AIQSKINECV EKDPGAFEEE AMVISVDDDG GDEEEGEAIR
VISAETGLIE ARIRDINTKI DMVGAIQRNM AGNYAGKVQG IMIGLAFTLI IGVLFLMF
//