MTRA_METJA
ID MTRA_METJA Reviewed; 241 AA.
AC Q58261;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 123.
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=MJ0851;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB98856.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L77117; AAB98856.1; ALT_INIT; Genomic_DNA.
DR PIR; C64406; C64406.
DR RefSeq; WP_064496640.1; NC_000909.1.
DR PDB; 5L8X; X-ray; 1.85 A; A/B=1-170.
DR PDB; 6ZW0; X-ray; 3.05 A; C/D=140-169.
DR PDBsum; 5L8X; -.
DR PDBsum; 6ZW0; -.
DR AlphaFoldDB; Q58261; -.
DR SMR; Q58261; -.
DR IntAct; Q58261; 2.
DR MINT; Q58261; -.
DR STRING; 243232.MJ_0851; -.
DR DNASU; 1451739; -.
DR EnsemblBacteria; AAB98856; AAB98856; MJ_0851.
DR GeneID; 1451739; -.
DR KEGG; mja:MJ_0851; -.
DR eggNOG; arCOG03221; Archaea.
DR HOGENOM; CLU_100863_0_0_2; -.
DR InParanoid; Q58261; -.
DR OMA; EVKGHIT; -.
DR OrthoDB; 89197at2157; -.
DR PhylomeDB; Q58261; -.
DR UniPathway; UPA00640; UER00698.
DR Proteomes; UP000000805; 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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cobalt; Membrane; Methanogenesis;
KW Methyltransferase; One-carbon metabolism; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..241
FT /note="Tetrahydromethanopterin S-methyltransferase subunit
FT A"
FT /id="PRO_0000147503"
FT TOPO_DOM 1..220
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01093"
FT TRANSMEM 221..241
FT /note="Helical"
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"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:5L8X"
FT HELIX 38..43
FT /evidence="ECO:0007829|PDB:5L8X"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:5L8X"
FT HELIX 57..67
FT /evidence="ECO:0007829|PDB:5L8X"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:5L8X"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:5L8X"
FT HELIX 87..97
FT /evidence="ECO:0007829|PDB:5L8X"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:5L8X"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:5L8X"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:5L8X"
FT HELIX 120..129
FT /evidence="ECO:0007829|PDB:5L8X"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:5L8X"
FT HELIX 142..154
FT /evidence="ECO:0007829|PDB:5L8X"
FT TURN 157..160
FT /evidence="ECO:0007829|PDB:6ZW0"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:6ZW0"
SQ SEQUENCE 241 AA; 25880 MW; 155EAE6418E09B8D CRC64;
MANKREPAPG WPIVSGEYVV GNPESCVGVV TLGSHGLEQA CIDAGAAIAG PCHTENLGIE
KVVANYISNP NIRFMILCGS EVQGHITGQC FKALWENGIG DDGGIIGAKG AIPFLENVNK
EAVERFRRQI VEVVDLIDCE DIGKITQAIK ECLSKDPGAI DEDPFIIELE GGKGGGEEEE
GVIKPITPEM AIIESRMRLI GNEMCYNGLL AKWQAGYYNG KIQGIATGLF LMLLIMGILM
F
