MTRA_META3
ID MTRA_META3 Reviewed; 240 AA.
AC A6UWH7;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 67.
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=Maeo_1273;
OS Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 /
OS Nankai-3).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=419665;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3;
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., Lykidis A.,
RA Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT "Complete sequence of Methanococcus aeolicus Nankai-3.";
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. {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; CP000743; ABR56849.1; -; Genomic_DNA.
DR RefSeq; WP_011973981.1; NC_009635.1.
DR AlphaFoldDB; A6UWH7; -.
DR SMR; A6UWH7; -.
DR STRING; 419665.Maeo_1273; -.
DR EnsemblBacteria; ABR56849; ABR56849; Maeo_1273.
DR GeneID; 5327467; -.
DR KEGG; mae:Maeo_1273; -.
DR eggNOG; arCOG03221; Archaea.
DR HOGENOM; CLU_100863_0_0_2; -.
DR OMA; ARMKIVS; -.
DR OrthoDB; 89197at2157; -.
DR UniPathway; UPA00640; UER00698.
DR Proteomes; UP000001106; 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_0000403062"
FT TOPO_DOM 1..216
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01093"
FT TRANSMEM 217..234
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01093"
FT TOPO_DOM 235..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; 25070 MW; C40DC2CE23D686C5 CRC64;
MADKKAPASG WPIVSGEYVV GNPESCVAVV TLGSHGLDEA AIEAGAAISG PCHTENLGIE
KVVANYISNP NIRFMLVTGS EVQGHITGQC FKALYENGIG DDGGIIGAKG AIPFLENAGQ
DAISRFQNQL VEIVDLIDVE DTGKISSAIK DCISKDPGAF EEDPMILDLE GGGGEAGADE
STSIKPAAPE TVLLEARMRM ISEKINDAAL IAKFNSGYYN GKIQGIAIGL FLSLLIFSLL
