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MTRE_METVS
ID   MTRE_METVS              Reviewed;         299 AA.
AC   A6UQK6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 70.
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=Mevan_0873;
OS   Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148
OS   / SB).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=406327;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Anderson I.,
RA   Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of Methanococcus vannielii SB.";
RL   Submitted (JUN-2007) 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: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; CP000742; ABR54778.1; -; Genomic_DNA.
DR   RefSeq; WP_011972679.1; NC_009634.1.
DR   AlphaFoldDB; A6UQK6; -.
DR   STRING; 406327.Mevan_0873; -.
DR   EnsemblBacteria; ABR54778; ABR54778; Mevan_0873.
DR   GeneID; 5326187; -.
DR   KEGG; mvn:Mevan_0873; -.
DR   eggNOG; arCOG04870; Archaea.
DR   HOGENOM; CLU_958513_0_0_2; -.
DR   OMA; QMGNIHR; -.
DR   OrthoDB; 50292at2157; -.
DR   UniPathway; UPA00640; UER00698.
DR   Proteomes; UP000001107; Chromosome.
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..299
FT                   /note="Tetrahydromethanopterin S-methyltransferase subunit
FT                   E"
FT                   /id="PRO_1000064946"
FT   TRANSMEM        57..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01098"
FT   TRANSMEM        80..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01098"
FT   TRANSMEM        133..153
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01098"
FT   TRANSMEM        158..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01098"
FT   TRANSMEM        237..257
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01098"
FT   TRANSMEM        261..281
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01098"
SQ   SEQUENCE   299 AA;  31018 MW;  F3DB9C1285DAFD3D CRC64;
     MDPTLISLGA LALAGAAATV SGCAEDLESD VGSQSNPNSQ VQLGPQMGNI HRYFNKAISG
     EPVSYGLYVA VAGSVAWALI NAGLNAVLAL IIGSGVAAIV HGAYSVSAFL GRTVGQSQKF
     GQPVYMDVLT SHIGPIVGHG FIAVFTMVLA AYLAVTALGN PFPLPLVALI FGITVGAIGS
     STGDVHYGAE REYQKYAFGG GIPVANQGDI DIYAEYGIRN GLDSSYFCSR LGGPLTGLCF
     GLIIFLDGWR SIVGNIIGGD LVTKTSIALV VGLLVVVAAM ILNRKIEVFA RNKYGPYRN
 
 
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