ID Q64EC9_9ARCH Unreviewed; 102 AA.
AC Q64EC9;
DT 25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Tetrahydromethanopterin S-methyltransferase subunit B {ECO:0000256|ARBA:ARBA00015127};
DE EC=2.1.1.86 {ECO:0000256|ARBA:ARBA00012514};
DE AltName: Full=N5-methyltetrahydromethanopterin--coenzyme M methyltransferase subunit B {ECO:0000256|ARBA:ARBA00029818};
GN Name=mtrB {ECO:0000313|EMBL:AAU82248.1};
GN ORFNames=GZ12E2_15 {ECO:0000313|EMBL:AAU82248.1};
OS uncultured archaeon GZfos12E2.
OC Archaea; environmental samples.
OX NCBI_TaxID=285364 {ECO:0000313|EMBL:AAU82248.1};
RN [1] {ECO:0000313|EMBL:AAU82248.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15353801; DOI=10.1126/science.1100025;
RA Hallam S.J., Putnam N., Preston C.M., Detter J.C., Rokhsar D.,
RA Richardson P.M., DeLong E.F.;
RT "Reverse methanogenesis: testing the hypothesis with environmental
RT genomics.";
RL Science 305:1457-1462(2004).
RN [2] {ECO:0000313|EMBL:AAU82248.1}
RP NUCLEOTIDE SEQUENCE.
RA Putnam N., Detter J.C., Richardson P.M., Rokhsar D.;
RL Submitted (AUG-2004) 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|ARBA:ARBA00002533}.
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:0000256|ARBA:ARBA00001816};
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|ARBA:ARBA00004839}.
CC -!- SUBUNIT: The complex is composed of 8 subunits; MtrA, MtrB, MtrC, MtrD,
CC MtrE, MtrF, MtrG and MtrH. {ECO:0000256|ARBA:ARBA00011616}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the MtrB family.
CC {ECO:0000256|ARBA:ARBA00010027}.
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DR EMBL; AY714818; AAU82248.1; -; Genomic_DNA.
DR AlphaFoldDB; Q64EC9; -.
DR UniPathway; UPA00640; UER00698.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030269; F:tetrahydromethanopterin S-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0019386; P:methanogenesis, from carbon dioxide; IEA:UniProtKB-UniPathway.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR InterPro; IPR008690; MtrB_MeTrfase.
DR NCBIfam; TIGR04166; methano_MtrB; 1.
DR Pfam; PF05440; MtrB; 1.
DR PIRSF; PIRSF005518; MtrB; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Methyltransferase {ECO:0000313|EMBL:AAU82248.1};
KW Transferase {ECO:0000313|EMBL:AAU82248.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 72..97
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 102 AA; 10957 MW; 81FA510506681A01 CRC64;
MVIVINEKYK VVLEESTLTV GEARAGFYKV SLAPIDEQLN ILEDAVDDLF NVLDPTTTYA
MAQPNREGIT NIAGFITMLM VGLTFGILAV ALVLYGIGFG GA
//
