Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P37012

- PGM2_YEAST

UniProt

P37012 - PGM2_YEAST

Protein

Phosphoglucomutase-2

Gene

PGM2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 1 (01 Jun 1994)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    This enzyme participates in both the breakdown and synthesis of glucose. Can also act on mannose.

    Catalytic activityi

    Alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate.

    Cofactori

    Binds 1 magnesium ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei119 – 1191Phosphoserine intermediateBy similarity
    Metal bindingi119 – 1191Magnesium; via phosphate groupBy similarity
    Metal bindingi290 – 2901MagnesiumBy similarity
    Metal bindingi292 – 2921MagnesiumBy similarity
    Metal bindingi294 – 2941MagnesiumBy similarity

    GO - Molecular functioni

    1. magnesium ion binding Source: InterPro
    2. phosphoglucomutase activity Source: SGD

    GO - Biological processi

    1. cellular calcium ion homeostasis Source: SGD
    2. cellular cation homeostasis Source: SGD
    3. galactose catabolic process Source: SGD
    4. glucose 1-phosphate metabolic process Source: SGD
    5. glucose 6-phosphate metabolic process Source: SGD
    6. glucose metabolic process Source: UniProtKB-KW
    7. glycogen biosynthetic process Source: SGD
    8. trehalose biosynthetic process Source: SGD
    9. UDP-glucose metabolic process Source: SGD

    Keywords - Molecular functioni

    Isomerase

    Keywords - Biological processi

    Carbohydrate metabolism, Glucose metabolism

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-17136.
    YEAST:YMR105C-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphoglucomutase-2 (EC:5.4.2.2)
    Short name:
    PGM 2
    Alternative name(s):
    Glucose phosphomutase 2
    Gene namesi
    Name:PGM2
    Synonyms:GAL5
    Ordered Locus Names:YMR105C
    ORF Names:YM9718.04C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XIII

    Organism-specific databases

    CYGDiYMR105c.
    SGDiS000004711. PGM2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: SGD

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 569568Phosphoglucomutase-2PRO_0000147797Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei111 – 1111Phosphothreonine1 Publication
    Modified residuei117 – 1171Phosphothreonine1 Publication
    Modified residuei119 – 1191Phosphoserine2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP37012.
    PaxDbiP37012.
    PeptideAtlasiP37012.
    PRIDEiP37012.

    Expressioni

    Gene expression databases

    GenevestigatoriP37012.

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    BioGridi35280. 85 interactions.
    DIPiDIP-6499N.
    IntActiP37012. 13 interactions.
    MINTiMINT-705119.
    STRINGi4932.YMR105C.

    Structurei

    3D structure databases

    ProteinModelPortaliP37012.
    SMRiP37012. Positions 4-569.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the phosphohexose mutase family.Curated

    Phylogenomic databases

    eggNOGiCOG0033.
    GeneTreeiENSGT00390000011831.
    HOGENOMiHOG000009550.
    KOiK01835.
    OMAiRYYCKEA.
    OrthoDBiEOG70S7FF.

    Family and domain databases

    Gene3Di3.30.310.50. 1 hit.
    3.40.120.10. 3 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.
    IPR005846. A-D-PHexomutase_a/b/a-III.
    IPR005843. A-D-PHexomutase_C.
    IPR016066. A-D-PHexomutase_CS.
    IPR005841. Alpha-D-phosphohexomutase_SF.
    [Graphical view]
    PfamiPF02878. PGM_PMM_I. 1 hit.
    PF02879. PGM_PMM_II. 1 hit.
    PF02880. PGM_PMM_III. 1 hit.
    PF00408. PGM_PMM_IV. 1 hit.
    [Graphical view]
    PRINTSiPR00509. PGMPMM.
    SUPFAMiSSF53738. SSF53738. 3 hits.
    SSF55957. SSF55957. 1 hit.
    PROSITEiPS00710. PGM_PMM. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P37012-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSFQIETVPT KPYEDQKPGT SGLRKKTKVF KDEPNYTENF IQSIMEAIPE    50
    GSKGATLVVG GDGRYYNDVI LHKIAAIGAA NGIKKLVIGQ HGLLSTPAAS 100
    HIMRTYEEKC TGGIILTASH NPGGPENDMG IKYNLSNGGP APESVTNAIW 150
    EISKKLTSYK IIKDFPELDL GTIGKNKKYG PLLVDIIDIT KDYVNFLKEI 200
    FDFDLIKKFI DNQRSTKNWK LLFDSMNGVT GPYGKAIFVD EFGLPADEVL 250
    QNWHPSPDFG GMHPDPNLTY ASSLVKRVDR EKIEFGAASD GDGDRNMIYG 300
    YGPSFVSPGD SVAIIAEYAA EIPYFAKQGI YGLARSFPTS GAIDRVAKAH 350
    GLNCYEVPTG WKFFCALFDA KKLSICGEES FGTGSNHVRE KDGVWAIMAW 400
    LNILAIYNKH HPENEASIKT IQNEFWAKYG RTFFTRYDFE KVETEKANKI 450
    VDQLRAYVTK SGVVNSAFPA DESLKVTDCG DFSYTDLDGS VSDHQGLYVK 500
    LSNGARFVLR LSGTGSSGAT IRLYIEKYCD DKSQYQKTAE EYLKPIINSV 550
    IKFLNFKQVL GTEEPTVRT 569
    Length:569
    Mass (Da):63,089
    Last modified:June 1, 1994 - v1
    Checksum:i45B78AFF8197645E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X74823 Genomic DNA. Translation: CAA52820.1.
    U09499 Genomic DNA. Translation: AAA91282.1.
    Z49702 Genomic DNA. Translation: CAA89741.1.
    AY723853 Genomic DNA. Translation: AAU09770.1.
    BK006946 Genomic DNA. Translation: DAA10001.1.
    PIRiS41200.
    RefSeqiNP_013823.1. NM_001182605.1.

    Genome annotation databases

    EnsemblFungiiYMR105C; YMR105C; YMR105C.
    GeneIDi855131.
    KEGGisce:YMR105C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X74823 Genomic DNA. Translation: CAA52820.1 .
    U09499 Genomic DNA. Translation: AAA91282.1 .
    Z49702 Genomic DNA. Translation: CAA89741.1 .
    AY723853 Genomic DNA. Translation: AAU09770.1 .
    BK006946 Genomic DNA. Translation: DAA10001.1 .
    PIRi S41200.
    RefSeqi NP_013823.1. NM_001182605.1.

    3D structure databases

    ProteinModelPortali P37012.
    SMRi P37012. Positions 4-569.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 35280. 85 interactions.
    DIPi DIP-6499N.
    IntActi P37012. 13 interactions.
    MINTi MINT-705119.
    STRINGi 4932.YMR105C.

    Proteomic databases

    MaxQBi P37012.
    PaxDbi P37012.
    PeptideAtlasi P37012.
    PRIDEi P37012.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YMR105C ; YMR105C ; YMR105C .
    GeneIDi 855131.
    KEGGi sce:YMR105C.

    Organism-specific databases

    CYGDi YMR105c.
    SGDi S000004711. PGM2.

    Phylogenomic databases

    eggNOGi COG0033.
    GeneTreei ENSGT00390000011831.
    HOGENOMi HOG000009550.
    KOi K01835.
    OMAi RYYCKEA.
    OrthoDBi EOG70S7FF.

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-17136.
    YEAST:YMR105C-MONOMER.

    Miscellaneous databases

    NextBioi 978502.

    Gene expression databases

    Genevestigatori P37012.

    Family and domain databases

    Gene3Di 3.30.310.50. 1 hit.
    3.40.120.10. 3 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.
    IPR005846. A-D-PHexomutase_a/b/a-III.
    IPR005843. A-D-PHexomutase_C.
    IPR016066. A-D-PHexomutase_CS.
    IPR005841. Alpha-D-phosphohexomutase_SF.
    [Graphical view ]
    Pfami PF02878. PGM_PMM_I. 1 hit.
    PF02879. PGM_PMM_II. 1 hit.
    PF02880. PGM_PMM_III. 1 hit.
    PF00408. PGM_PMM_IV. 1 hit.
    [Graphical view ]
    PRINTSi PR00509. PGMPMM.
    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].
    2. Fu L., Bounelis P., Dey N., Browne B.L., Marchase R.B., Bedwell D.M.
      Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    7. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    8. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-111; THR-117 AND SER-119, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPGM2_YEAST
    AccessioniPrimary (citable) accession number: P37012
    Secondary accession number(s): D6VZS7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 133 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 3790 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3