ID L0L1I6_METHD Unreviewed; 241 AA.
AC L0L1I6;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
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 OrderedLocusNames=Metho_2092 {ECO:0000313|EMBL:AGB50258.1};
OS Methanomethylovorans hollandica (strain DSM 15978 / NBRC 107637 / DMS1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanomethylovorans.
OX NCBI_TaxID=867904 {ECO:0000313|EMBL:AGB50258.1, ECO:0000313|Proteomes:UP000010866};
RN [1] {ECO:0000313|Proteomes:UP000010866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15978 / NBRC 107637 / DMS1
RC {ECO:0000313|Proteomes:UP000010866};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Held B.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Spring S., Schroeder M., Brambilla E., Klenk H.-P.,
RA Eisen J.A.;
RT "Complete sequence of chromosome of Methanomethylovorans hollandica DSM
RT 15978.";
RL Submitted (FEB-2012) 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; CP003362; AGB50258.1; -; Genomic_DNA.
DR RefSeq; WP_015325423.1; NC_019977.1.
DR AlphaFoldDB; L0L1I6; -.
DR STRING; 867904.Metho_2092; -.
DR GeneID; 14406605; -.
DR KEGG; mhz:Metho_2092; -.
DR HOGENOM; CLU_100863_0_0_2; -.
DR OrthoDB; 130682at2157; -.
DR UniPathway; UPA00640; UER00698.
DR Proteomes; UP000010866; 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 Reference proteome {ECO:0000313|Proteomes:UP000010866};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01093, ECO:0000313|EMBL:AGB50258.1};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_01093};
KW Transmembrane helix {ECO:0000256|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:0000256|HAMAP-Rule:MF_01093"
SQ SEQUENCE 241 AA; 25562 MW; 7BCEBD6770D628E5 CRC64;
MVDKREPAPQ WPVLKGEYEV GDVKNCVAVI TLGSHLTGGP QLDAGACITG PCKTENLGIE
KVVVHIISNP NIRFLIVTGS EVKGHVTGDA ILKMHQNGVK DNRIVGAVGA IPYIENLTAE
AIERFQQQVE CVNFIGTEDT NAIVAKIKEY AAKDPGAYDA EPMLLKIGEG GEEEKEEAGG
LKPMAAEMAT VRSRILSVNK EMMGIGNLNK FHAGVHAGKV EGIMIGLGIT LTILGLLLGG
N
//
