MTRE_METTM
ID MTRE_METTM Reviewed; 295 AA.
AC P80186; D9PY28;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=Tetrahydromethanopterin S-methyltransferase subunit E;
DE EC=2.1.1.86 {ECO:0000269|PubMed:8477726};
DE AltName: Full=N5-methyltetrahydromethanopterin--coenzyme M methyltransferase subunit E;
GN Name=mtrE {ECO:0000303|PubMed:7737157}; OrderedLocusNames=MTBMA_c15470;
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], 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 [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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 81-295.
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 [4]
RP PROTEIN SEQUENCE OF 1-30, FUNCTION, CATALYTIC ACTIVITY, 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).
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: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;
CC Evidence={ECO:0000269|PubMed:8477726};
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.
CC -!- SUBUNIT: The complex is composed of 8 subunits; MtrA, MtrB, MtrC, MtrD,
CC MtrE, MtrF, MtrG and MtrH. {ECO:0000269|PubMed:7737157}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: The first gene of the probable mtrEDCBAFGH operon.
CC {ECO:0000305|PubMed:7737157}.
CC -!- SIMILARITY: Belongs to the MtrE family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X84218; CAA59000.1; -; Genomic_DNA.
DR EMBL; CP001710; ADL59126.1; -; Genomic_DNA.
DR EMBL; X73123; CAA51552.1; -; Genomic_DNA.
DR RefSeq; WP_013296336.1; NC_014408.1.
DR AlphaFoldDB; P80186; -.
DR STRING; 79929.MTBMA_c15470; -.
DR TCDB; 3.C.1.1.1; the na(+) transporting methyltetrahydromethanopterin:coenzyme m methyltransferase (nat-mmm) family.
DR EnsemblBacteria; ADL59126; ADL59126; MTBMA_c15470.
DR GeneID; 41345243; -.
DR KEGG; mmg:MTBMA_c15470; -.
DR PATRIC; fig|79929.8.peg.1500; -.
DR HOGENOM; CLU_958513_0_0_2; -.
DR OMA; QMGNIHR; -.
DR UniPathway; UPA00640; UER00698.
DR Proteomes; UP000000345; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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:0012506; C:vesicle membrane; IEA:InterPro.
DR GO; GO:0030269; F:tetrahydromethanopterin S-methyltransferase activity; IDA:MENGO.
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_01098; MtrE; 1.
DR InterPro; IPR005780; MeTrfase_E.
DR Pfam; PF04206; MtrE; 1.
DR PIRSF; PIRSF016509; MtrE; 1.
DR TIGRFAMs; TIGR01113; mtrE; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Membrane; Methanogenesis;
KW Methyltransferase; One-carbon metabolism; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..295
FT /note="Tetrahydromethanopterin S-methyltransferase subunit
FT E"
FT /id="PRO_0000147544"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 295 AA; 31232 MW; B801FF65AE3E6C09 CRC64;
MDPMITGLGV VALMGAAATI AGAAEDLESD VGSQSNPNSQ VQLAPQMGHL HRIINKAVSG
EPVAYGTWCG IAGSVAFVLM NSMQLPVIMA IAIGAVIAAM VHTTYAVTSH MGRIVSQSQF
NQPLFMDMLV QHLGPIAGHG FIVTFCTVGL SYLMTLPIPG FAHPFPLPLL AVLWGITIGA
IGSSTGDVHY GAEREYQQYP FGGGIPVAIH GDITTKAELG ARNSMDVVHF CAKYGGPLTG
FAFGAIVFLS FWNTIVFGIT GGIISGLIIV LLLIILNNRL EVFARNRYGP YKEEE
