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MTRC_METBF
ID   MTRC_METBF              Reviewed;         267 AA.
AC   Q9Y8K2; Q46D19;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 2.
DT   25-MAY-2022, entry version 115.
DE   RecName: Full=Tetrahydromethanopterin S-methyltransferase subunit C {ECO:0000255|HAMAP-Rule:MF_01096};
DE            EC=2.1.1.86 {ECO:0000255|HAMAP-Rule:MF_01096};
DE   AltName: Full=N5-methyltetrahydromethanopterin--coenzyme M methyltransferase subunit C {ECO:0000255|HAMAP-Rule:MF_01096};
GN   Name=mtrC {ECO:0000255|HAMAP-Rule:MF_01096}; OrderedLocusNames=Mbar_A1260;
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_01096}.
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_01096};
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_01096}.
CC   -!- SUBUNIT: The complex is composed of 8 subunits; MtrA, MtrB, MtrC, MtrD,
CC       MtrE, MtrF, MtrG and MtrH. {ECO:0000255|HAMAP-Rule:MF_01096}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01096};
CC       Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01096}.
CC   -!- SIMILARITY: Belongs to the MtrC family. {ECO:0000255|HAMAP-
CC       Rule:MF_01096}.
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DR   EMBL; AJ132817; CAB41640.1; -; Genomic_DNA.
DR   EMBL; CP000099; AAZ70223.1; -; Genomic_DNA.
DR   RefSeq; WP_011306270.1; NC_007355.1.
DR   AlphaFoldDB; Q9Y8K2; -.
DR   STRING; 269797.Mbar_A1260; -.
DR   EnsemblBacteria; AAZ70223; AAZ70223; Mbar_A1260.
DR   GeneID; 3627860; -.
DR   KEGG; mba:Mbar_A1260; -.
DR   eggNOG; arCOG04868; Archaea.
DR   HOGENOM; CLU_092286_0_0_2; -.
DR   OMA; HPFNACL; -.
DR   OrthoDB; 61293at2157; -.
DR   UniPathway; UPA00640; UER00698.
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; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..267
FT                   /note="Tetrahydromethanopterin S-methyltransferase subunit
FT                   C"
FT                   /id="PRO_0000147521"
FT   TRANSMEM        19..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01096"
FT   TRANSMEM        75..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01096"
FT   TRANSMEM        97..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01096"
FT   TRANSMEM        140..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01096"
FT   TRANSMEM        162..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01096"
FT   TRANSMEM        198..218
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01096"
FT   TRANSMEM        221..241
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01096"
FT   CONFLICT        54
FT                   /note="V -> D (in Ref. 1; CAB41640)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   267 AA;  26805 MW;  DF4FE90AB7EEC089 CRC64;
     MSAGGAGGEA KGGYPPQTIM ALGIVGGLVG IYLGNFAPPA YSFFGGLGAI CATVWGADAV
     RRVASYGLGT GVPSIGMLAL GMGILAALFG LSVGGTAGPI VAIVVAAIIG GVIGALANKV
     IGMGIPIMEK AMVEISCAGT LVILGLSVVI AGSFDFASVV QYVVANGYIA LIFIIGGMGI
     LHPFNASLGP DEKQDRTLML AVEKGAIALI IAGFASSLHE GLMAAGLNML IGIIIWYVAF
     SKHYALIKRD AYAVVGSGML PSSEELQ
 
 
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