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MTRC_METJA
ID   MTRC_METJA              Reviewed;         265 AA.
AC   Q58259;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 112.
DE   RecName: Full=Tetrahydromethanopterin S-methyltransferase subunit C;
DE            EC=2.1.1.86;
DE   AltName: Full=N5-methyltetrahydromethanopterin--coenzyme M methyltransferase subunit C;
GN   Name=mtrC; OrderedLocusNames=MJ0849;
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:0000250}.
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   -!- 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:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the MtrC family. {ECO:0000305}.
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DR   EMBL; L77117; AAB98854.1; -; Genomic_DNA.
DR   PIR; A64406; A64406.
DR   RefSeq; WP_010870363.1; NC_000909.1.
DR   AlphaFoldDB; Q58259; -.
DR   STRING; 243232.MJ_0849; -.
DR   DNASU; 1451737; -.
DR   EnsemblBacteria; AAB98854; AAB98854; MJ_0849.
DR   GeneID; 1451737; -.
DR   KEGG; mja:MJ_0849; -.
DR   eggNOG; arCOG04868; Archaea.
DR   HOGENOM; CLU_092286_0_0_2; -.
DR   InParanoid; Q58259; -.
DR   OMA; HPFNACL; -.
DR   OrthoDB; 61293at2157; -.
DR   PhylomeDB; Q58259; -.
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: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   HAMAP; MF_01096; MtrC; 1.
DR   InterPro; IPR005865; THM_MeTrfase_su_C.
DR   Pfam; PF04211; MtrC; 1.
DR   PIRSF; PIRSF006530; MtrC; 1.
DR   TIGRFAMs; TIGR01148; mtrC; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Membrane; Methanogenesis; Methyltransferase;
KW   One-carbon metabolism; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..265
FT                   /note="Tetrahydromethanopterin S-methyltransferase subunit
FT                   C"
FT                   /id="PRO_0000147522"
FT   TRANSMEM        18..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        41..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        75..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        100..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        141..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        175..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        202..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        224..244
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   265 AA;  27804 MW;  07FB20DA394A7FE0 CRC64;
     MSHGGGGHAA ELYPEEQIFA VGIALSLVGC YLANFLSPYG LGMLIGGLLA SAACVAGANT
     VRKVAAYGLG TGVPSIGMVS LGMGTLAAVA GVLIPDYFNL PYLVAPIITL IVSAVIGYIV
     GRLTVNPVGM KIPIMVRSMT FLSIAGAMAL LGFTVAYVGS LEPQKYIDYA LNNGMMALAF
     IAAGMAILHP FNACLGPNES HKRTLTLAVA CGFITWFVFS VVKLDIVSII VSIILWAIVY
     VKFVKMSFKD ACAVLHVPEI PKKEE
 
 
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