MTRA_METHJ
ID MTRA_METHJ Reviewed; 244 AA.
AC Q2FRN2;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=Mhun_2172;
OS Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 /
OS JF-1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanospirillaceae; Methanospirillum.
OX NCBI_TaxID=323259;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27890 / DSM 864 / NBRC 100397 / JF-1;
RX PubMed=26744606; DOI=10.1186/s40793-015-0124-8;
RA Gunsalus R.P., Cook L.E., Crable B., Rohlin L., McDonald E., Mouttaki H.,
RA Sieber J.R., Poweleit N., Zhou H., Lapidus A.L., Daligault H.E., Land M.,
RA Gilna P., Ivanova N., Kyrpides N., Culley D.E., McInerney M.J.;
RT "Complete genome sequence of Methanospirillum hungatei type strain JF1.";
RL Stand. Genomic Sci. 11:2-2(2016).
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; CP000254; ABD41877.1; -; Genomic_DNA.
DR RefSeq; WP_011449135.1; NC_007796.1.
DR AlphaFoldDB; Q2FRN2; -.
DR SMR; Q2FRN2; -.
DR STRING; 323259.Mhun_2172; -.
DR EnsemblBacteria; ABD41877; ABD41877; Mhun_2172.
DR GeneID; 3922605; -.
DR KEGG; mhu:Mhun_2172; -.
DR eggNOG; arCOG03221; Archaea.
DR HOGENOM; CLU_100863_0_0_2; -.
DR OMA; EVKGHIT; -.
DR OrthoDB; 89197at2157; -.
DR UniPathway; UPA00640; UER00698.
DR Proteomes; UP000001941; 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..244
FT /note="Tetrahydromethanopterin S-methyltransferase subunit
FT A"
FT /id="PRO_0000403068"
FT TOPO_DOM 1..222
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01093"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01093"
FT TOPO_DOM 244
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 244 AA; 25425 MW; 75F5347F587E648F CRC64;
MANKKSPASG WPIVQGDFHT GDPNSPVAVV TMGSHLDEGA ICSAGAAIAG SCKTENLGLE
KVIANVISNP NIRFVITCGT EVKGHLSGQS LIALHQNGVD GGKIVGSKGA IPFIENLSAD
NIKRFQEQVE LVDIMESEDL GAISAKIKEL TARDPGAFDA EAMIVEIKEE GGGAAEEGGE
VRPMSAEVAL IHARMKTIQR TITDIGFYDK YAAGVYGGKV EGLMIGLIVS FVIIGLLLVG
HGVS