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Protein

Phosphatidylethanolamine N-methyltransferase

Gene

CHO2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the first step of the methylation pathway of phosphatidylcholine biosynthesis, the SAM-dependent methylation of phosphatidylethanolamine (PE) to phosphatidylmonomethylethanolamine (PMME). Preferentially converts di-C16:1 substrates.UniRule annotation8 Publications

Catalytic activityi

S-adenosyl-L-methionine + phosphatidylethanolamine = S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine.UniRule annotation4 Publications

Kineticsi

  1. KM=60 µM for S-adenosyl-L-methionine1 Publication
  2. KM=110 µM for S-adenosyl-L-methionine1 Publication
  3. KM=57 µM for phosphatidylethanolamine (PE)1 Publication

    pH dependencei

    Optimum pH is 9.9.1 Publication

    Pathwayi: phosphatidylcholine biosynthesis

    This protein is involved in the pathway phosphatidylcholine biosynthesis, which is part of Phospholipid metabolism.UniRule annotation2 Publications
    View all proteins of this organism that are known to be involved in the pathway phosphatidylcholine biosynthesis and in Phospholipid metabolism.

    GO - Molecular functioni

    • phosphatidylethanolamine N-methyltransferase activity Source: SGD

    GO - Biological processi

    • phosphatidylcholine biosynthetic process Source: SGD
    Complete GO annotation...

    Keywords - Molecular functioni

    Methyltransferase, Transferase

    Keywords - Biological processi

    Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

    Keywords - Ligandi

    S-adenosyl-L-methionine

    Enzyme and pathway databases

    BioCyciMetaCyc:YGR157W-MONOMER.
    YEAST:YGR157W-MONOMER.
    UniPathwayiUPA00753.

    Chemistry databases

    SwissLipidsiSLP:000000085.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphatidylethanolamine N-methyltransferase1 PublicationUniRule annotation (EC:2.1.1.17UniRule annotation4 Publications)
    Short name:
    PE methyltransferase1 PublicationUniRule annotation
    Short name:
    PEAMTUniRule annotation
    Short name:
    PEMT1 PublicationUniRule annotation
    Alternative name(s):
    Choline-requiring protein 21 Publication
    Gene namesi
    Name:CHO21 Publication
    Synonyms:PEM11 Publication
    Ordered Locus Names:YGR157WImported
    ORF Names:G6673
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    Proteomesi
    • UP000002311 Componenti: Chromosome VII

    Organism-specific databases

    EuPathDBiFungiDB:YGR157W.
    SGDiS000003389. CHO2.

    Subcellular locationi

    Topology

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Topological domaini2 – 55LumenalUniRule annotation1 PublicationAdd BLAST54
    Transmembranei56 – 76HelicalUniRule annotationAdd BLAST21
    Topological domaini77 – 86CytoplasmicUniRule annotation1 Publication10
    Transmembranei87 – 107HelicalUniRule annotationAdd BLAST21
    Topological domaini108 – 187LumenalUniRule annotation1 PublicationAdd BLAST80
    Transmembranei188 – 208HelicalUniRule annotationAdd BLAST21
    Topological domaini209 – 212CytoplasmicUniRule annotation1 Publication4
    Transmembranei213 – 233HelicalUniRule annotationAdd BLAST21
    Topological domaini234 – 258LumenalUniRule annotation1 PublicationAdd BLAST25
    Transmembranei259 – 279HelicalUniRule annotationAdd BLAST21
    Topological domaini280 – 291CytoplasmicUniRule annotation1 PublicationAdd BLAST12
    Transmembranei292 – 310HelicalUniRule annotationAdd BLAST19
    Topological domaini311 – 362LumenalUniRule annotation1 PublicationAdd BLAST52
    Transmembranei363 – 383HelicalUniRule annotationAdd BLAST21
    Topological domaini384 – 389CytoplasmicUniRule annotation1 Publication6
    Transmembranei390 – 410HelicalUniRule annotationAdd BLAST21
    Topological domaini411 – 439LumenalUniRule annotation1 PublicationAdd BLAST29
    Transmembranei440 – 460HelicalUniRule annotationAdd BLAST21
    Topological domaini461 – 463CytoplasmicUniRule annotation1 Publication3
    Transmembranei464 – 484HelicalUniRule annotationAdd BLAST21
    Topological domaini485 – 534LumenalUniRule annotation1 PublicationAdd BLAST50
    Transmembranei535 – 555HelicalUniRule annotationAdd BLAST21
    Topological domaini556 – 869CytoplasmicUniRule annotation1 PublicationAdd BLAST314

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemovedCombined sources
    ChainiPRO_00000583042 – 869Phosphatidylethanolamine N-methyltransferaseAdd BLAST868

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei2N-acetylserineCombined sources1

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP05374.
    PRIDEiP05374.

    PTM databases

    iPTMnetiP05374.

    Expressioni

    Inductioni

    Repressed by myo-inositol and choline.4 Publications

    Interactioni

    Protein-protein interaction databases

    BioGridi33405. 355 interactors.
    DIPiDIP-8037N.
    IntActiP05374. 2 interactors.
    MINTiMINT-1358409.

    Structurei

    3D structure databases

    ProteinModelPortaliP05374.
    SMRiP05374.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the class VI-like SAM-binding methyltransferase superfamily. CHO2 family.UniRule annotation

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    InParanoidiP05374.
    KOiK16369.
    OMAiEAWRQWK.
    OrthoDBiEOG092C0F70.

    Family and domain databases

    HAMAPiMF_03217. PEMT. 1 hit.
    InterProiIPR007318. Phopholipid_MeTrfase.
    IPR016219. Phosphatid-EA_MeTrfase_fun.
    [Graphical view]
    PfamiPF04191. PEMT. 2 hits.
    [Graphical view]
    PIRSFiPIRSF000383. PEAMT. 1 hit.
    PROSITEiPS51598. SAM_CHO2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P05374-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSSCKTTLSE MVGSVTKDRG TINVEARTRS SNVTFKPPVT HDMVRSLFDP
    60 70 80 90 100
    TLKKSLLEKC IALAIISNFF ICYWVFQRFG LQFTKYFFLV QYLFWRIAYN
    110 120 130 140 150
    LGIGLVLHYQ SHYETLTNCA KTHAIFSKIP QNKDANSNFS TNSNSFSEKF
    160 170 180 190 200
    WNFIRKFCQY EIRSKMPKEY DLFAYPEEIN VWLIFRQFVD LILMQDFVTY
    210 220 230 240 250
    IIYVYLSIPY SWVQIFNWRS LLGVILILFN IWVKLDAHRV VKDYAWYWGD
    260 270 280 290 300
    FFFLEESELI FDGVFNISPH PMYSIGYLGY YGLSLICNDY KVLLVSVFGH
    310 320 330 340 350
    YSQFLFLKYV ENPHIERTYG DGTDSDSQMN SRIDDLISKE NYDYSRPLIN
    360 370 380 390 400
    MGLSFNNFNK LRFTDYFTIG TVAALMLGTI MNARFINLNY LFITVFVTKL
    410 420 430 440 450
    VSWLFISTIL YKQSQSKWFT RLFLENGYTQ VYSYEQWQFI YNYYLVLTYT
    460 470 480 490 500
    LMIIHTGLQI WSNFSNINNS QLIFGLILVA LQTWCDKETR LAISDFGWFY
    510 520 530 540 550
    GDFFLSNYIS TRKLTSQGIY RYLNHPEAVL GVVGVWGTVL MTNFAVTNII
    560 570 580 590 600
    LAVLWTLTNF ILVKFIETPH VNKIYGKTKR VSGVGKTLLG LKPLRQVSDI
    610 620 630 640 650
    VNRIENIIIK SLVDESKNSN GGAELLPKNY QDNKEWNILI QEAMDSVATR
    660 670 680 690 700
    LSPYCELKIE NEQVETNFVL PTPVTLNWKM PIELYNGDDW IGLYKVIDTR
    710 720 730 740 750
    ADREKTRVGS GGHWSATSKD SYMNHGLRHK ESVTEIKATE KYVQGKVTFD
    760 770 780 790 800
    TSLLYFENGI YEFRYHSGNS HKVLLISTPF EISLPVLNTT TPELFEKDLT
    810 820 830 840 850
    EFLTKVNVLK DGKFRPLGNK FFGMDSLKQL IKNSIGVELS SEYMRRVNGD
    860
    AHVISHRAWD IKQTLDSLA
    Length:869
    Mass (Da):101,204
    Last modified:November 1, 1988 - v1
    Checksum:iA273F179B4E46A20
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M16987 Genomic DNA. Translation: AAA34850.1.
    X85807 Genomic DNA. Translation: CAA59814.1.
    Z72942 Genomic DNA. Translation: CAA97171.1.
    BK006941 Genomic DNA. Translation: DAA08248.1.
    PIRiA28443.
    RefSeqiNP_011673.1. NM_001181286.1.

    Genome annotation databases

    EnsemblFungiiYGR157W; YGR157W; YGR157W.
    GeneIDi853061.
    KEGGisce:YGR157W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M16987 Genomic DNA. Translation: AAA34850.1.
    X85807 Genomic DNA. Translation: CAA59814.1.
    Z72942 Genomic DNA. Translation: CAA97171.1.
    BK006941 Genomic DNA. Translation: DAA08248.1.
    PIRiA28443.
    RefSeqiNP_011673.1. NM_001181286.1.

    3D structure databases

    ProteinModelPortaliP05374.
    SMRiP05374.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi33405. 355 interactors.
    DIPiDIP-8037N.
    IntActiP05374. 2 interactors.
    MINTiMINT-1358409.

    Chemistry databases

    SwissLipidsiSLP:000000085.

    PTM databases

    iPTMnetiP05374.

    Proteomic databases

    MaxQBiP05374.
    PRIDEiP05374.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYGR157W; YGR157W; YGR157W.
    GeneIDi853061.
    KEGGisce:YGR157W.

    Organism-specific databases

    EuPathDBiFungiDB:YGR157W.
    SGDiS000003389. CHO2.

    Phylogenomic databases

    InParanoidiP05374.
    KOiK16369.
    OMAiEAWRQWK.
    OrthoDBiEOG092C0F70.

    Enzyme and pathway databases

    UniPathwayiUPA00753.
    BioCyciMetaCyc:YGR157W-MONOMER.
    YEAST:YGR157W-MONOMER.

    Miscellaneous databases

    PROiP05374.

    Family and domain databases

    HAMAPiMF_03217. PEMT. 1 hit.
    InterProiIPR007318. Phopholipid_MeTrfase.
    IPR016219. Phosphatid-EA_MeTrfase_fun.
    [Graphical view]
    PfamiPF04191. PEMT. 2 hits.
    [Graphical view]
    PIRSFiPIRSF000383. PEAMT. 1 hit.
    PROSITEiPS51598. SAM_CHO2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiCHO2_YEAST
    AccessioniPrimary (citable) accession number: P05374
    Secondary accession number(s): D6VUT7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1988
    Last sequence update: November 1, 1988
    Last modified: November 30, 2016
    This is version 135 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 1810 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome VII
      Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.