MTRA1_METTM
ID MTRA1_METTM Reviewed; 238 AA.
AC P80184; D9PY24;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Tetrahydromethanopterin S-methyltransferase subunit A 1 {ECO:0000255|HAMAP-Rule:MF_01093};
DE EC=2.1.1.86 {ECO:0000255|HAMAP-Rule:MF_01093, ECO:0000269|PubMed:8477726};
DE AltName: Full=N5-methyltetrahydromethanopterin--coenzyme M methyltransferase subunit A 1 {ECO:0000255|HAMAP-Rule:MF_01093};
GN Name=mtrA1 {ECO:0000255|HAMAP-Rule:MF_01093};
GN Synonyms=mtrA {ECO:0000303|PubMed:7737157}; OrderedLocusNames=MTBMA_c15430;
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 [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=8223548; DOI=10.1111/j.1432-1033.1993.tb18225.x;
RA Stupperich E., Juza A., Hoppert M., Mayer F.;
RT "Cloning, sequencing and immunological characterization of the corrinoid-
RT containing subunit of the N5-methyltetrahydromethanopterin: coenzyme-M
RT methyltransferase from Methanobacterium thermoautotrophicum.";
RL Eur. J. Biochem. 217:115-121(1993).
RN [2]
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).
RN [3]
RP PROTEIN SEQUENCE OF 2-24, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=8477726; DOI=10.1111/j.1432-1033.1993.tb17792.x;
RA Gaertner P., Ecker A., Fischer R., Linder D., Fuchs G., Thauer R.K.;
RT "Purification and properties of N5-methyltetrahydromethanopterin:coenzyme M
RT methyltransferase from Methanobacterium thermoautotrophicum.";
RL Eur. J. Biochem. 213:537-545(1993).
RN [4]
RP SUBUNIT, AND OPERON STRUCTURE.
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=7737157; DOI=10.1111/j.1432-1033.1995.0640m.x;
RA Harms U., Weiss D.S., Gaertner P., Linder D., Thauer R.K.;
RT "The energy conserving N5-methyltetrahydromethanopterin:coenzyme M
RT methyltransferase complex from Methanobacterium thermoautotrophicum is
RT composed of eight different subunits.";
RL Eur. J. Biochem. 228:640-648(1995).
RN [5]
RP BINDING SITE HIS-84, AND MUTAGENESIS OF HIS-35; HIS-84 AND HIS-94.
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=9461302; DOI=10.1111/j.1432-1033.1997.00783.x;
RA Harms U., Thauer R.K.;
RT "Identification of the active site histidine in the corrinoid protein MtrA
RT of the energy-conserving methyltransferase complex from Methanobacterium
RT thermoautotrophicum.";
RL Eur. J. Biochem. 250:783-788(1997).
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 ECO:0000269|PubMed:8477726}.
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, ECO:0000269|PubMed:8477726};
CC -!- COFACTOR:
CC Name=5-hydroxybenzimidazolylcob(I)amide; Xref=ChEBI:CHEBI:60494;
CC Evidence={ECO:0000269|PubMed:8477726};
CC Note=Binds 1 5-hydroxybenzimidazolylcobamide group.;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=260 uM for 5-methyl-5,6,7,8-tetrahydromethanopterin
CC {ECO:0000269|PubMed:8477726};
CC KM=60 uM for coenzyme M {ECO:0000269|PubMed:8477726};
CC Vmax=11.6 umol/min/mg enzyme {ECO:0000269|PubMed:8477726};
CC Note=From other experiments a much lower Km for 5-methyl-5,6,7,8-
CC tetrahydromethanopterin is estimated. {ECO:0000269|PubMed:8477726};
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 ECO:0000269|PubMed:7737157}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01093,
CC ECO:0000269|PubMed:8223548}; Single-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01093, ECO:0000269|PubMed:8223548}.
CC -!- INDUCTION: Part of the probable mtrEDCBAFGH operon.
CC {ECO:0000305|PubMed:7737157}.
CC -!- SIMILARITY: Belongs to the MtrA family. {ECO:0000255|HAMAP-
CC Rule:MF_01093}.
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DR EMBL; X73123; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP001710; ADL59122.1; -; Genomic_DNA.
DR RefSeq; WP_013296332.1; NC_014408.1.
DR AlphaFoldDB; P80184; -.
DR SMR; P80184; -.
DR STRING; 79929.MTBMA_c15430; -.
DR TCDB; 3.C.1.1.1; the na(+) transporting methyltetrahydromethanopterin:coenzyme m methyltransferase (nat-mmm) family.
DR EnsemblBacteria; ADL59122; ADL59122; MTBMA_c15430.
DR GeneID; 9705252; -.
DR KEGG; mmg:MTBMA_c15430; -.
DR PATRIC; fig|79929.8.peg.1496; -.
DR HOGENOM; CLU_100863_0_0_2; -.
DR OMA; EVKGHIT; -.
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:0034708; C:methyltransferase complex; IDA:UniProtKB.
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; IPR013347; MeTrfase_F_su.
DR InterPro; IPR030688; MeTrfase_MtrA/MtxA.
DR InterPro; IPR005778; MtrA.
DR Pfam; PF04208; MtrA; 1.
DR Pfam; PF09472; MtrF; 1.
DR PIRSF; PIRSF500207; MtrA; 1.
DR PIRSF; PIRSF009452; MtrA_MtxA; 1.
DR TIGRFAMs; TIGR01111; mtrA; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cobalt; Direct protein sequencing; Membrane; Methanogenesis;
KW Methyltransferase; One-carbon metabolism; Transferase; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8477726"
FT CHAIN 2..238
FT /note="Tetrahydromethanopterin S-methyltransferase subunit
FT A 1"
FT /id="PRO_0000147508"
FT TOPO_DOM 2..218
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01093"
FT TRANSMEM 219..237
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01093"
FT TOPO_DOM 238
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01093"
FT BINDING 84
FT /ligand="5-hydroxybenzimidazolylcob(I)amide"
FT /ligand_id="ChEBI:CHEBI:60494"
FT /ligand_note="cofactor"
FT /evidence="ECO:0000305"
FT MUTAGEN 35
FT /note="H->K: No change in cofactor binding. No change in
FT cofactor binding; when associated with K-94."
FT /evidence="ECO:0000269|PubMed:9461302"
FT MUTAGEN 84
FT /note="H->G,N,S: Abolishes cofactor binding."
FT /evidence="ECO:0000269|PubMed:9461302"
FT MUTAGEN 94
FT /note="H->K: No change in cofactor binding; when associated
FT with K-35."
FT /evidence="ECO:0000269|PubMed:9461302"
SQ SEQUENCE 238 AA; 25617 MW; 7FB17A14112A3463 CRC64;
MVEKKSPAEG WPVVNGDYIV GDPESPVAAT TLASHIEDIP VEAGAAIAGP CKTENLGIEK
MIANLISNPN IRFLILCGSE VQGHITGQSI EALHQNGVDP DKRNIIGATG AIPYIENIPD
EGIERFQKQL EIVNLIDVED ADAIKAKVKE CIEKDPGAFE EEAMIIKVEE GGEEEEGEEV
KPVAPETALI EARMRNIQTQ VKMIGSTNRM FAGMYSGKVQ GIMIGLAFTL TLGILLLV
