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P38628

- AGM1_YEAST

UniProt

P38628 - AGM1_YEAST

Protein

Phosphoacetylglucosamine mutase

Gene

PCM1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 2 (01 Feb 1995)
      Previous versions | rss
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    Functioni

    Interconverts GlcNAc-6-P and GlcNAc-1-P.

    Catalytic activityi

    N-acetyl-alpha-D-glucosamine 1-phosphate = N-acetyl-D-glucosamine 6-phosphate.

    Cofactori

    Binds 1 magnesium ion per subunit.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei67 – 671Phosphoserine intermediate
    Metal bindingi67 – 671Magnesium; via phosphate groupBy similarity
    Metal bindingi298 – 2981MagnesiumBy similarity
    Metal bindingi300 – 3001MagnesiumBy similarity
    Metal bindingi302 – 3021MagnesiumBy similarity

    GO - Molecular functioni

    1. magnesium ion binding Source: InterPro
    2. phosphoacetylglucosamine mutase activity Source: SGD
    3. protein binding Source: IntAct

    GO - Biological processi

    1. fungal-type cell wall chitin biosynthetic process Source: SGD
    2. UDP-N-acetylglucosamine biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Isomerase

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-13178.
    YEAST:YEL058W-MONOMER.
    ReactomeiREACT_189213. Synthesis of UDP-N-acetyl-glucosamine.
    UniPathwayiUPA00113; UER00530.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphoacetylglucosamine mutase (EC:5.4.2.3)
    Short name:
    PAGM
    Alternative name(s):
    Acetylglucosamine phosphomutase
    N-acetylglucosamine-phosphate mutase
    Gene namesi
    Name:PCM1
    Synonyms:AGM1
    Ordered Locus Names:YEL058W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome V

    Organism-specific databases

    CYGDiYEL058w.
    SGDiS000000784. PCM1.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 557557Phosphoacetylglucosamine mutasePRO_0000148019Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei67 – 671Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylation at Ser-67 is involved in the reaction mechanism.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP38628.
    PaxDbiP38628.
    PeptideAtlasiP38628.

    Expressioni

    Gene expression databases

    GenevestigatoriP38628.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MGS1P401512EBI-2351,EBI-29152

    Protein-protein interaction databases

    BioGridi36671. 14 interactions.
    DIPiDIP-6760N.
    IntActiP38628. 1 interaction.
    MINTiMINT-637715.
    STRINGi4932.YEL058W.

    Structurei

    3D structure databases

    ProteinModelPortaliP38628.
    SMRiP38628. Positions 17-554.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the phosphohexose mutase family.Curated

    Phylogenomic databases

    eggNOGiCOG1109.
    GeneTreeiENSGT00390000000509.
    HOGENOMiHOG000210027.
    KOiK01836.
    OMAiDIVRVYA.
    OrthoDBiEOG7V1G0D.

    Family and domain databases

    Gene3Di3.30.310.50. 1 hit.
    3.40.120.10. 2 hits.
    InterProiIPR005844. A-D-PHexomutase_a/b/a-I.
    IPR016055. A-D-PHexomutase_a/b/a-I/II/III.
    IPR005845. A-D-PHexomutase_a/b/a-II.
    IPR005843. A-D-PHexomutase_C.
    IPR016066. A-D-PHexomutase_CS.
    IPR016657. PAGM.
    [Graphical view]
    PfamiPF02878. PGM_PMM_I. 1 hit.
    PF02879. PGM_PMM_II. 1 hit.
    PF00408. PGM_PMM_IV. 1 hit.
    [Graphical view]
    PIRSFiPIRSF016408. PAGM. 1 hit.
    SUPFAMiSSF53738. SSF53738. 3 hits.
    SSF55957. SSF55957. 1 hit.
    PROSITEiPS00710. PGM_PMM. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P38628-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKVDYEQLCK LYDDTCRTKN VQFSYGTAGF RTLAKNLDTV MFSTGILAVL    50
    RSLKLQGQYV GVMITASHNP YQDNGVKIVE PDGSMLLATW EPYAMQLANA 100
    ASFATNFEEF RVELAKLIEH EKIDLNTTVV PHIVVGRDSR ESSPYLLRCL 150
    TSSMASVFHA QVLDLGCVTT PQLHYITDLS NRRKLEGDTA PVATEQDYYS 200
    FFIGAFNELF ATYQLEKRLS VPKLFIDTAN GIGGPQLKKL LASEDWDVPA 250
    EQVEVINDRS DVPELLNFEC GADYVKTNQR LPKGLSPSSF DSLYCSFDGD 300
    ADRVVFYYVD SGSKFHLLDG DKISTLFAKF LSKQLELAHL EHSLKIGVVQ 350
    TAYANGSSTA YIKNTLHCPV SCTKTGVKHL HHEAATQYDI GIYFEANGHG 400
    TIIFSEKFHR TIKSELSKSK LNGDTLALRT LKCFSELINQ TVGDAISDML 450
    AVLATLAILK MSPMDWDEEY TDLPNKLVKC IVPDRSIFQT TDQERKLLNP 500
    VGLQDKIDLV VAKYPMGRSF VRASGTEDAV RVYAECKDSS KLGQFCDEVV 550
    EHVKASA 557
    Length:557
    Mass (Da):62,067
    Last modified:February 1, 1995 - v2
    Checksum:i76F17D47D07C920A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti15 – 151T → M in CAA53452. (PubMed:8119301)Curated
    Sequence conflicti196 – 1961Q → R in CAA53452. (PubMed:8119301)Curated
    Sequence conflicti406 – 4061E → G in CAA53452. (PubMed:8119301)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X75816 Genomic DNA. Translation: CAA53452.1.
    U18795 Genomic DNA. Translation: AAB65029.1.
    BK006939 Genomic DNA. Translation: DAA07596.1.
    PIRiS50531.
    RefSeqiNP_010856.1. NM_001178873.1.

    Genome annotation databases

    EnsemblFungiiYEL058W; YEL058W; YEL058W.
    GeneIDi856652.
    KEGGisce:YEL058W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X75816 Genomic DNA. Translation: CAA53452.1 .
    U18795 Genomic DNA. Translation: AAB65029.1 .
    BK006939 Genomic DNA. Translation: DAA07596.1 .
    PIRi S50531.
    RefSeqi NP_010856.1. NM_001178873.1.

    3D structure databases

    ProteinModelPortali P38628.
    SMRi P38628. Positions 17-554.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 36671. 14 interactions.
    DIPi DIP-6760N.
    IntActi P38628. 1 interaction.
    MINTi MINT-637715.
    STRINGi 4932.YEL058W.

    Proteomic databases

    MaxQBi P38628.
    PaxDbi P38628.
    PeptideAtlasi P38628.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YEL058W ; YEL058W ; YEL058W .
    GeneIDi 856652.
    KEGGi sce:YEL058W.

    Organism-specific databases

    CYGDi YEL058w.
    SGDi S000000784. PCM1.

    Phylogenomic databases

    eggNOGi COG1109.
    GeneTreei ENSGT00390000000509.
    HOGENOMi HOG000210027.
    KOi K01836.
    OMAi DIVRVYA.
    OrthoDBi EOG7V1G0D.

    Enzyme and pathway databases

    UniPathwayi UPA00113 ; UER00530 .
    BioCyci MetaCyc:MONOMER-13178.
    YEAST:YEL058W-MONOMER.
    Reactomei REACT_189213. Synthesis of UDP-N-acetyl-glucosamine.

    Miscellaneous databases

    NextBioi 982631.
    PROi P38628.

    Gene expression databases

    Genevestigatori P38628.

    Family and domain databases

    Gene3Di 3.30.310.50. 1 hit.
    3.40.120.10. 2 hits.
    InterProi IPR005844. A-D-PHexomutase_a/b/a-I.
    IPR016055. A-D-PHexomutase_a/b/a-I/II/III.
    IPR005845. A-D-PHexomutase_a/b/a-II.
    IPR005843. A-D-PHexomutase_C.
    IPR016066. A-D-PHexomutase_CS.
    IPR016657. PAGM.
    [Graphical view ]
    Pfami PF02878. PGM_PMM_I. 1 hit.
    PF02879. PGM_PMM_II. 1 hit.
    PF00408. PGM_PMM_IV. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF016408. PAGM. 1 hit.
    SUPFAMi SSF53738. SSF53738. 3 hits.
    SSF55957. SSF55957. 1 hit.
    PROSITEi PS00710. PGM_PMM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A family of hexosephosphate mutases in Saccharomyces cerevisiae."
      Boles E., Liebetrau W., Hofmann M., Zimmermann F.K.
      Eur. J. Biochem. 220:83-96(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: EBY21-8.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. "Characterization of the essential yeast gene encoding N-acetylglucosamine-phosphate mutase."
      Hofmann M., Boles E., Zimmermann F.K.
      Eur. J. Biochem. 221:741-747(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
      Strain: EBY21-8.
    5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    6. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    7. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiAGM1_YEAST
    AccessioniPrimary (citable) accession number: P38628
    Secondary accession number(s): D3DLJ2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 137 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 14700 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 V
      Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

    External Data

    Dasty 3