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MTRD_METKA
ID   MTRD_METKA              Reviewed;         225 AA.
AC   O32864;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 111.
DE   RecName: Full=Tetrahydromethanopterin S-methyltransferase subunit D;
DE            EC=2.1.1.86;
DE   AltName: Full=N5-methyltetrahydromethanopterin--coenzyme M methyltransferase subunit D;
GN   Name=mtrD; OrderedLocusNames=MK0657;
OS   Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC   Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC   Methanopyrus.
OX   NCBI_TaxID=190192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9461302; DOI=10.1111/j.1432-1033.1997.00783.x;
RA   Harms U., Thauer R.K.;
RT   "Identification of the active site histidine in the corrinoid protein MtrA
RT   of the energy-conserving methyltransferase complex from Methanobacterium
RT   thermoautotrophicum.";
RL   Eur. J. Biochem. 250:783-788(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX   PubMed=11930014; DOI=10.1073/pnas.032671499;
RA   Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA   Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA   Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA   Koonin E.V., Kozyavkin S.A.;
RT   "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT   monophyly of archaeal methanogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
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 MtrD family. {ECO:0000305}.
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DR   EMBL; Y14428; CAA74768.1; -; Genomic_DNA.
DR   EMBL; AE009439; AAM01872.1; -; Genomic_DNA.
DR   AlphaFoldDB; O32864; -.
DR   STRING; 190192.MK0657; -.
DR   EnsemblBacteria; AAM01872; AAM01872; MK0657.
DR   KEGG; mka:MK0657; -.
DR   PATRIC; fig|190192.8.peg.696; -.
DR   HOGENOM; CLU_1109510_0_0_2; -.
DR   OMA; HDPKFKR; -.
DR   UniPathway; UPA00640; UER00698.
DR   Proteomes; UP000001826; 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_01097; MtrD; 1.
DR   InterPro; IPR005779; MeTrfase_D.
DR   Pfam; PF04207; MtrD; 1.
DR   PIRSF; PIRSF016552; MtrD; 1.
DR   TIGRFAMs; TIGR01112; mtrD; 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..225
FT                   /note="Tetrahydromethanopterin S-methyltransferase subunit
FT                   D"
FT                   /id="PRO_0000147531"
FT   TRANSMEM        5..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        40..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        67..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        132..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        161..181
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        204..224
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   225 AA;  22872 MW;  6FA9546897670D36 CRC64;
     MDKLIAVLVL ITLGSIMVNV GVHYVPVGGA PAAMATATGV GTGTTQLAAG SGLTGLITAA
     AMSQKPFLVI LWNGALGAAT MMAITMLVGN FIYVYGVGCP PCSAKVDKDP ITGWDQEAYV
     TPGTEGHGIP TVSFVSGILG GLLGGSGGAM VYYALYKVLG MSAALAGILA MGFFYANAVL
     ASYNIGGTIE GYHDPKFTRL PKAVVCSLVF GIVASVIAYY LSTLM
 
 
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