MTRE_METBF
ID MTRE_METBF Reviewed; 302 AA.
AC Q9Y8K0; Q46D17;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Tetrahydromethanopterin S-methyltransferase subunit E {ECO:0000255|HAMAP-Rule:MF_01098};
DE EC=2.1.1.86 {ECO:0000255|HAMAP-Rule:MF_01098};
DE AltName: Full=N5-methyltetrahydromethanopterin--coenzyme M methyltransferase subunit E {ECO:0000255|HAMAP-Rule:MF_01098};
GN Name=mtrE {ECO:0000255|HAMAP-Rule:MF_01098}; OrderedLocusNames=Mbar_A1262;
OS Methanosarcina barkeri (strain Fusaro / DSM 804).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=269797;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10338124; DOI=10.1016/s0014-5793(99)00429-9;
RA Hippler B., Thauer R.K.;
RT "The energy conserving methyltetrahydromethanopterin:coenzyme M
RT methyltransferase complex from methanogenic archaea: function of the
RT subunit MtrH.";
RL FEBS Lett. 449:165-168(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fusaro / DSM 804;
RX PubMed=16980466; DOI=10.1128/jb.00810-06;
RA Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT "The Methanosarcina barkeri genome: comparative analysis with
RT Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT rearrangement within methanosarcinal genomes.";
RL J. Bacteriol. 188:7922-7931(2006).
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_01098}.
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_01098};
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_01098}.
CC -!- SUBUNIT: The complex is composed of 8 subunits; MtrA, MtrB, MtrC, MtrD,
CC MtrE, MtrF, MtrG and MtrH. {ECO:0000255|HAMAP-Rule:MF_01098}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01098};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01098}.
CC -!- SIMILARITY: Belongs to the MtrE family. {ECO:0000255|HAMAP-
CC Rule:MF_01098}.
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DR EMBL; AJ132817; CAB41638.1; -; Genomic_DNA.
DR EMBL; CP000099; AAZ70225.1; -; Genomic_DNA.
DR RefSeq; WP_011306272.1; NC_007355.1.
DR AlphaFoldDB; Q9Y8K0; -.
DR STRING; 269797.Mbar_A1262; -.
DR EnsemblBacteria; AAZ70225; AAZ70225; Mbar_A1262.
DR GeneID; 3627862; -.
DR KEGG; mba:Mbar_A1262; -.
DR eggNOG; arCOG04870; Archaea.
DR HOGENOM; CLU_958513_0_0_2; -.
DR OMA; QMGNIHR; -.
DR OrthoDB; 50292at2157; -.
DR UniPathway; UPA00640; UER00698.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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:0012506; C:vesicle membrane; 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_01098; MtrE; 1.
DR InterPro; IPR005780; MeTrfase_E.
DR Pfam; PF04206; MtrE; 1.
DR PIRSF; PIRSF016509; MtrE; 1.
DR TIGRFAMs; TIGR01113; mtrE; 1.
PE 3: Inferred from homology;
KW Cell membrane; Membrane; Methanogenesis; Methyltransferase;
KW One-carbon metabolism; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..302
FT /note="Tetrahydromethanopterin S-methyltransferase subunit
FT E"
FT /id="PRO_0000147537"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01098"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01098"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01098"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01098"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01098"
FT TRANSMEM 259..279
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01098"
SQ SEQUENCE 302 AA; 32507 MW; 78BE4AE4E0A9A182 CRC64;
MEPLISMGVL ALIGVAATIA GASEDLESDI GSQSNPNSQV QLAPQMMFPH RIFNKAISGE
PPSNALMCSI GAAVATVLIS EFTMSPLFAL VFGSLIAACV HATFAVTSTM GRCASQSRFK
QPIYLDMIRS HITPIMGYAF ITTFCILVVS YLMTVVLGHP FPLTMLAFIW GITIGAIGSS
TGDVHYGAER EFQQFEFGSG LNASNSGNIV RYAESGLRDG FDNSWFCAKF GGPVTGLAFG
MTVFLGSWIT TIFDPAKGLG WLSVIAGIVI VFILIIWNWK MEVYARKAYG PYKEDKTEEA
SA
