MTRA2_METTM
ID MTRA2_METTM Reviewed; 185 AA.
AC D9PXT1;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Tetrahydromethanopterin S-methyltransferase subunit A 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_01093};
GN Name=mtrA2 {ECO:0000255|HAMAP-Rule:MF_01093};
GN OrderedLocusNames=MTBMA_c14500;
OS Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM
OS 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium
OS thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=79929;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=20802048; DOI=10.1128/jb.00844-10;
RA Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H.,
RA Gottschalk G., Thauer R.K.;
RT "Complete genome sequence of Methanothermobacter marburgensis, a
RT methanoarchaeon model organism.";
RL J. Bacteriol. 192:5850-5851(2010).
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; CP001710; ADL59029.1; -; Genomic_DNA.
DR RefSeq; WP_013296240.1; NC_014408.1.
DR AlphaFoldDB; D9PXT1; -.
DR SMR; D9PXT1; -.
DR STRING; 79929.MTBMA_c14500; -.
DR EnsemblBacteria; ADL59029; ADL59029; MTBMA_c14500.
DR GeneID; 9705159; -.
DR KEGG; mmg:MTBMA_c14500; -.
DR HOGENOM; CLU_100863_0_0_2; -.
DR OMA; GSHMEDE; -.
DR OrthoDB; 89197at2157; -.
DR UniPathway; UPA00640; UER00698.
DR Proteomes; UP000000345; 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; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..185
FT /note="Tetrahydromethanopterin S-methyltransferase subunit
FT A 2"
FT /id="PRO_0000403069"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01093"
FT TRANSMEM 22..38
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01093"
FT TOPO_DOM 39..185
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01093"
FT BINDING 88
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 185 AA; 20003 MW; 3AC8195A48557619 CRC64;
MVDKKVDKKP VPEDWPHIVG DYVVGDAESP VAVVTLGSHM EDEPVRAGAA ISGPLHTENL
GIEKVVGNVI ANPNLRFLLV CGAEVMGHIT GQTMKALHSN GVDGETGRII GATGAIPYIE
NMPDEAIERF RRQVELVDMV DVEDPAAIRE RIGECVVHDS GAIDEEPLIL RPSEDLNKNK
PDENT
