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P11986

- INO1_YEAST

UniProt

P11986 - INO1_YEAST

Protein

Inositol-3-phosphate synthase

Gene

INO1

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 139 (01 Oct 2014)
      Sequence version 3 (06 Dec 2005)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate.

    Cofactori

    NAD.

    Pathwayi

    GO - Molecular functioni

    1. inositol-3-phosphate synthase activity Source: UniProtKB

    GO - Biological processi

    1. inositol biosynthetic process Source: UniProtKB
    2. phospholipid biosynthetic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Isomerase

    Keywords - Biological processi

    Inositol biosynthesis, Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BioCyciYEAST:YJL153C-MONOMER.
    ReactomeiREACT_188936. Synthesis of IP2, IP, and Ins in the cytosol.
    SABIO-RKP11986.
    UniPathwayiUPA00823; UER00787.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Inositol-3-phosphate synthase (EC:5.5.1.4)
    Short name:
    MIP synthase
    Alternative name(s):
    Myo-inositol 1-phosphate synthase
    Short name:
    IPS
    Short name:
    MI-1-P synthase
    Gene namesi
    Name:INO1
    Ordered Locus Names:YJL153C
    ORF Names:J0610
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome X

    Organism-specific databases

    CYGDiYJL153c.
    SGDiS000003689. INO1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 533533Inositol-3-phosphate synthasePRO_0000195185Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei368 – 3681Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP11986.
    PaxDbiP11986.
    PRIDEiP11986.

    Expressioni

    Gene expression databases

    GenevestigatoriP11986.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself1EBI-9257,EBI-9257
    AAT2P235421EBI-9257,EBI-2002
    ADE17P380091EBI-9257,EBI-14223
    ALO1P547831EBI-9257,EBI-2519
    ARO8P530901EBI-9257,EBI-2042933
    ARP2P323811EBI-9257,EBI-2927
    BNA3P470391EBI-9257,EBI-25893
    CAR2P079911EBI-9257,EBI-12430
    CHC1P221371EBI-9257,EBI-4766
    CYS4P325821EBI-9257,EBI-4167
    EFT1P323241EBI-9257,EBI-6333
    GCY1P140651EBI-9257,EBI-7505
    GET3Q121541EBI-9257,EBI-2989
    GLN1P322881EBI-9257,EBI-7665
    HSP12P229431EBI-9257,EBI-8548
    HUG1Q6Q5K61EBI-9257,EBI-392766
    IPP1P008171EBI-9257,EBI-9338
    MBF1O144671EBI-9257,EBI-2043025
    MET13P531281EBI-9257,EBI-11572
    OYE2Q035581EBI-9257,EBI-12729
    RNR1P215241EBI-9257,EBI-15234
    RNR2P099381EBI-9257,EBI-15240
    SEC27P418111EBI-9257,EBI-4898
    SRV2P175551EBI-9257,EBI-4024
    SSD1P242761EBI-9257,EBI-18153
    VAS1P07806-11EBI-9257,EBI-1009942From a different organism.
    VMA4P222031EBI-9257,EBI-20268
    VMA8P326101EBI-9257,EBI-20264

    Protein-protein interaction databases

    BioGridi33607. 51 interactions.
    DIPiDIP-5687N.
    IntActiP11986. 20 interactions.
    MINTiMINT-551495.
    STRINGi4932.YJL153C.

    Structurei

    Secondary structure

    1
    533
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi11 – 144
    Beta strandi19 – 224
    Beta strandi25 – 3915
    Beta strandi43 – 5917
    Beta strandi64 – 718
    Turni72 – 743
    Helixi76 – 8914
    Beta strandi94 – 963
    Beta strandi99 – 1013
    Helixi109 – 1124
    Beta strandi114 – 1196
    Beta strandi121 – 1233
    Beta strandi125 – 1295
    Helixi130 – 1323
    Helixi139 – 1413
    Beta strandi142 – 1476
    Helixi154 – 1618
    Helixi166 – 17611
    Helixi188 – 1903
    Helixi193 – 1986
    Beta strandi207 – 2093
    Helixi216 – 23318
    Beta strandi239 – 2435
    Turni255 – 2573
    Beta strandi258 – 2603
    Helixi261 – 2699
    Helixi277 – 28711
    Beta strandi292 – 2943
    Beta strandi296 – 2983
    Helixi303 – 31210
    Beta strandi316 – 3216
    Helixi325 – 33814
    Beta strandi342 – 35211
    Helixi355 – 3606
    Helixi363 – 37513
    Helixi378 – 3825
    Turni385 – 3873
    Turni390 – 3923
    Beta strandi397 – 4048
    Helixi406 – 4083
    Beta strandi411 – 42111
    Helixi423 – 4253
    Beta strandi427 – 43711
    Helixi438 – 45720
    Beta strandi459 – 4635
    Beta strandi466 – 4683
    Helixi482 – 4876
    Beta strandi488 – 4903
    Helixi503 – 51715
    Helixi528 – 5314

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1JKFX-ray2.40A/B1-533[»]
    1JKIX-ray2.20A/B1-533[»]
    1LA2X-ray2.65A/B/C/D1-533[»]
    1P1FX-ray2.60A/B1-533[»]
    1P1HX-ray1.95A/B/C/D1-533[»]
    1P1IX-ray2.40A/B1-533[»]
    1P1JX-ray1.70A/B1-533[»]
    1P1KX-ray2.10A/B1-533[»]
    1RM0X-ray2.05A/B1-533[»]
    ProteinModelPortaliP11986.
    SMRiP11986. Positions 9-533.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP11986.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1260.
    GeneTreeiENSGT00390000018395.
    HOGENOMiHOG000013469.
    KOiK01858.
    OMAiNPVLYAP.
    OrthoDBiEOG7DZ8V4.

    Family and domain databases

    Gene3Di3.40.50.720. 2 hits.
    InterProiIPR002587. Myo-inos-1-P_Synthase.
    IPR013021. Myo-inos-1-P_Synthase_GAPDH.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PANTHERiPTHR11510. PTHR11510. 1 hit.
    PfamiPF01658. Inos-1-P_synth. 1 hit.
    PF07994. NAD_binding_5. 1 hit.
    [Graphical view]
    PIRSFiPIRSF015578. Myoinos-ppht_syn. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P11986-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTEDNIAPIT SVKVVTDKCT YKDNELLTKY SYENAVVTKT ASGRFDVTPT    50
    VQDYVFKLDL KKPEKLGIML IGLGGNNGST LVASVLANKH NVEFQTKEGV 100
    KQPNYFGSMT QCSTLKLGID AEGNDVYAPF NSLLPMVSPN DFVVSGWDIN 150
    NADLYEAMQR SQVLEYDLQQ RLKAKMSLVK PLPSIYYPDF IAANQDERAN 200
    NCINLDEKGN VTTRGKWTHL QRIRRDIQNF KEENALDKVI VLWTANTERY 250
    VEVSPGVNDT MENLLQSIKN DHEEIAPSTI FAAASILEGV PYINGSPQNT 300
    FVPGLVQLAE HEGTFIAGDD LKSGQTKLKS VLAQFLVDAG IKPVSIASYN 350
    HLGNNDGYNL SAPKQFRSKE ISKSSVIDDI IASNDILYND KLGKKVDHCI 400
    VIKYMKPVGD SKVAMDEYYS ELMLGGHNRI SIHNVCEDSL LATPLIIDLL 450
    VMTEFCTRVS YKKVDPVKED AGKFENFYPV LTFLSYWLKA PLTRPGFHPV 500
    NGLNKQRTAL ENFLRLLIGL PSQNELRFEE RLL 533
    Length:533
    Mass (Da):59,642
    Last modified:December 6, 2005 - v3
    Checksum:i282E2AE5D156289D
    GO

    Sequence cautioni

    The sequence CAA60802.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAA89448.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti14 – 141V → RL(PubMed:2642902)Curated
    Sequence conflicti14 – 141V → RL(PubMed:7975896)Curated
    Sequence conflicti60 – 601L → FE(PubMed:2642902)Curated
    Sequence conflicti60 – 601L → FE(PubMed:7975896)Curated
    Sequence conflicti66 – 9328LGIML…KHNVE → TRNYAHWVRWLQQWLTLWPR YWRISTMWS(PubMed:2642902)CuratedAdd
    BLAST
    Sequence conflicti66 – 9328LGIML…KHNVE → TRNYAHWVRWLQQWLTLWPR YWRISTMWS(PubMed:7975896)CuratedAdd
    BLAST
    Sequence conflicti98 – 981E → AK(PubMed:2642902)Curated
    Sequence conflicti98 – 981E → AK(PubMed:7975896)Curated
    Sequence conflicti140 – 1412ND → KH(PubMed:2642902)Curated
    Sequence conflicti140 – 1412ND → KH(PubMed:7975896)Curated
    Sequence conflicti201 – 2011N → Q(PubMed:2642902)Curated
    Sequence conflicti201 – 2011N → Q(PubMed:7975896)Curated
    Sequence conflicti444 – 4441P → A(PubMed:2642902)Curated
    Sequence conflicti444 – 4441P → A(PubMed:7975896)Curated
    Sequence conflicti476 – 49722NFYPV…TRPGF → ELLSSFNLLELLVKSSINKN QDL in AAA66310. (PubMed:2642902)CuratedAdd
    BLAST
    Sequence conflicti524 – 53310NELRFEERLL → KRTKIRREIVVISFQRLSFS FSAYL in AAA34706. (PubMed:2642902)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L23520 Genomic DNA. Translation: AAA34706.1.
    J04453 Genomic DNA. Translation: AAA66310.1.
    X87371 Genomic DNA. Translation: CAA60802.1. Different initiation.
    Z49428 Genomic DNA. Translation: CAA89448.1. Different initiation.
    BK006943 Genomic DNA. Translation: DAA08650.1.
    PIRiS55160. A30902.
    RefSeqiNP_012382.2. NM_001181586.1.

    Genome annotation databases

    EnsemblFungiiYJL153C; YJL153C; YJL153C.
    GeneIDi853288.
    KEGGisce:YJL153C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L23520 Genomic DNA. Translation: AAA34706.1 .
    J04453 Genomic DNA. Translation: AAA66310.1 .
    X87371 Genomic DNA. Translation: CAA60802.1 . Different initiation.
    Z49428 Genomic DNA. Translation: CAA89448.1 . Different initiation.
    BK006943 Genomic DNA. Translation: DAA08650.1 .
    PIRi S55160. A30902.
    RefSeqi NP_012382.2. NM_001181586.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1JKF X-ray 2.40 A/B 1-533 [» ]
    1JKI X-ray 2.20 A/B 1-533 [» ]
    1LA2 X-ray 2.65 A/B/C/D 1-533 [» ]
    1P1F X-ray 2.60 A/B 1-533 [» ]
    1P1H X-ray 1.95 A/B/C/D 1-533 [» ]
    1P1I X-ray 2.40 A/B 1-533 [» ]
    1P1J X-ray 1.70 A/B 1-533 [» ]
    1P1K X-ray 2.10 A/B 1-533 [» ]
    1RM0 X-ray 2.05 A/B 1-533 [» ]
    ProteinModelPortali P11986.
    SMRi P11986. Positions 9-533.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 33607. 51 interactions.
    DIPi DIP-5687N.
    IntActi P11986. 20 interactions.
    MINTi MINT-551495.
    STRINGi 4932.YJL153C.

    Proteomic databases

    MaxQBi P11986.
    PaxDbi P11986.
    PRIDEi P11986.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YJL153C ; YJL153C ; YJL153C .
    GeneIDi 853288.
    KEGGi sce:YJL153C.

    Organism-specific databases

    CYGDi YJL153c.
    SGDi S000003689. INO1.

    Phylogenomic databases

    eggNOGi COG1260.
    GeneTreei ENSGT00390000018395.
    HOGENOMi HOG000013469.
    KOi K01858.
    OMAi NPVLYAP.
    OrthoDBi EOG7DZ8V4.

    Enzyme and pathway databases

    UniPathwayi UPA00823 ; UER00787 .
    BioCyci YEAST:YJL153C-MONOMER.
    Reactomei REACT_188936. Synthesis of IP2, IP, and Ins in the cytosol.
    SABIO-RK P11986.

    Miscellaneous databases

    EvolutionaryTracei P11986.
    NextBioi 973591.
    PROi P11986.

    Gene expression databases

    Genevestigatori P11986.

    Family and domain databases

    Gene3Di 3.40.50.720. 2 hits.
    InterProi IPR002587. Myo-inos-1-P_Synthase.
    IPR013021. Myo-inos-1-P_Synthase_GAPDH.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    PANTHERi PTHR11510. PTHR11510. 1 hit.
    Pfami PF01658. Inos-1-P_synth. 1 hit.
    PF07994. NAD_binding_5. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF015578. Myoinos-ppht_syn. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Biosynthesis of inositol in yeast. Primary structure of myo-inositol-1-phosphate synthase (EC 5.5.1.4) and functional analysis of its structural gene, the INO1 locus."
      Dean-Johnson M., Henry S.A.
      J. Biol. Chem. 264:1274-1283(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
      Strain: ATCC 204510 / AB320.
    2. "Comparison of INO1 gene sequences and products in Candida albicans and Saccharomyces cerevisiae."
      Klig L.S., Zobel P.A., Devry C.G., Losberger C.
      Yeast 10:789-800(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: AB322.
    3. "Sequence analysis of a 40.7 kb segment from the left arm of yeast chromosome X reveals 14 known genes and 13 new open reading frames including homologues of genes clustered on the right arm of chromosome XI."
      Katsoulou C., Tzermia M., Tavernarakis N., Alexandraki D.
      Yeast 12:787-797(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 96604 / S288c / FY1679.
    4. "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
      Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K.
      , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
      EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    6. "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 SER-368, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. "The crystal structure and mechanism of 1-L-myo-inositol-1-phosphate synthase."
      Stein A.J., Geiger J.H.
      J. Biol. Chem. 277:9484-9491(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).

    Entry informationi

    Entry nameiINO1_YEAST
    AccessioniPrimary (citable) accession number: P11986
    Secondary accession number(s): D6VW34
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: December 6, 2005
    Last modified: October 1, 2014
    This is version 139 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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

    External Data

    Dasty 3