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Reviewed, UniProtKB/Swiss-Prot P11986 (INO1_YEAST)

Last modified November 24, 2009. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Inositol-3-phosphate synthase
    EC=5.5.1.4
Alternative name(s):
    Myo-inositol-1-phosphate synthase
      Short name=MI-1-P synthase
      Short name=IPS
Gene names
Name: INO1
Ordered Locus Names: YJL153C
ORF Names: J0610
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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Protein attributes

Sequence length533 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

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

Cofactor

NAD.

Pathway

Polyol metabolism; myo-inositol biosynthesis; myo-inositol from D-glucose 6-phosphate: step 1/2.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the myo-inositol-1-phosphate synthase family.

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Ontologies

Keywords
   Biological processInositol biosynthesis
Phospholipid biosynthesis
   Cellular componentCytoplasm
   LigandNAD
   Molecular functionIsomerase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processinositol biosynthetic process Ref.3

Inferred from direct assay. Source: UniProtKB

phospholipid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm Ref.3

Inferred from direct assay. Source: UniProtKB

   Molecular functionidentical protein binding

Inferred from physical interaction. Source: IntAct

inositol-3-phosphate synthase activity Ref.3

Inferred from direct assay. Source: UniProtKB

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 533533Inositol-3-phosphate synthase
PRO_0000195185

Experimental info

Sequence conflict141V → RL Ref.1
Sequence conflict141V → RL Ref.2
Sequence conflict601L → FE Ref.1
Sequence conflict601L → FE Ref.2
Sequence conflict66 – 9328LGIML…KHNVE → TRNYAHWVRWLQQWLTLWPR YWRISTMWS Ref.1
Sequence conflict66 – 9328LGIML…KHNVE → TRNYAHWVRWLQQWLTLWPR YWRISTMWS Ref.2
Sequence conflict981E → AK Ref.1
Sequence conflict981E → AK Ref.2
Sequence conflict140 – 1412ND → KH Ref.1
Sequence conflict140 – 1412ND → KH Ref.2
Sequence conflict2011N → Q Ref.1
Sequence conflict2011N → Q Ref.2
Sequence conflict4441P → A Ref.1
Sequence conflict4441P → A Ref.2
Sequence conflict476 – 49722NFYPV…TRPGF → ELLSSFNLLELLVKSSINKN QDL in AAA66310. Ref.1
Sequence conflict524 – 53310NELRFEERLL → KRTKIRREIVVISFQRLSFS FSAYL in AAA34706. Ref.1

Secondary structure

1 .............................................................................. 533
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P11986-1 [UniParc].

Last modified December 6, 2005. Version 3.
Checksum: 282E2AE5D156289D

FASTA53359,642
        10         20         30         40         50         60 
MTEDNIAPIT SVKVVTDKCT YKDNELLTKY SYENAVVTKT ASGRFDVTPT VQDYVFKLDL 

        70         80         90        100        110        120 
KKPEKLGIML IGLGGNNGST LVASVLANKH NVEFQTKEGV KQPNYFGSMT QCSTLKLGID 

       130        140        150        160        170        180 
AEGNDVYAPF NSLLPMVSPN DFVVSGWDIN NADLYEAMQR SQVLEYDLQQ RLKAKMSLVK 

       190        200        210        220        230        240 
PLPSIYYPDF IAANQDERAN NCINLDEKGN VTTRGKWTHL QRIRRDIQNF KEENALDKVI 

       250        260        270        280        290        300 
VLWTANTERY VEVSPGVNDT MENLLQSIKN DHEEIAPSTI FAAASILEGV PYINGSPQNT 

       310        320        330        340        350        360 
FVPGLVQLAE HEGTFIAGDD LKSGQTKLKS VLAQFLVDAG IKPVSIASYN HLGNNDGYNL 

       370        380        390        400        410        420 
SAPKQFRSKE ISKSSVIDDI IASNDILYND KLGKKVDHCI VIKYMKPVGD SKVAMDEYYS 

       430        440        450        460        470        480 
ELMLGGHNRI SIHNVCEDSL LATPLIIDLL VMTEFCTRVS YKKVDPVKED AGKFENFYPV 

       490        500        510        520        530 
LTFLSYWLKA PLTRPGFHPV NGLNKQRTAL ENFLRLLIGL PSQNELRFEE RLL

« Hide

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References

« Hide 'large scale' references
[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: 2642902] [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: 7975896] [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: 8813765] [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. expand/collapse author list , 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: 8641269] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]"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: 11779862] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
+Additional computationally mapped references.

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Cross-references

Sequence databases

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.
PIRA30902. S55160.
RefSeqNP_012382.2.

3D structure databases

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[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:5687N.
IntActP11986. 52 interactions.
STRINGP11986.

Genome annotation databases

EnsemblYJL153C; YJL153C; YJL153C; Saccharomyces cerevisiae. [Genome view]
GeneID853288.
KEGGsce:YJL153C.
NMPDRfig|4932.3.peg.3347.

Organism-specific databases

CYGDYJL153c.
SGDS000003689. INO1.

Phylogenomic databases

HOGENOMP11986.
OMAVLYAPGE
OrthoDBEOG9RZ0G7

Enzyme and pathway databases

BRENDA5.5.1.4. 250.

Gene expression databases

ArrayExpressP11986.
GenevestigatorP11986.
GermOnlineYJL153C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR002587. Myo-inos-1-P_Synthase.
IPR013021. Myo-inos-1-P_Synthase_GAPDH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHERPTHR11510. Inos-1-P_synth. 1 hit.
PfamPF01658. Inos-1-P_synth. 1 hit.
PF07994. NAD_binding_5. 1 hit.
[Graphical view]
PIRSFPIRSF015578. Myoinos-ppht_syn. 1 hit.
ProtoNetSearch...

Other Resources

NextBio973591.

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Entry information

Entry nameINO1_YEAST
AccessionPrimary (citable) accession number: P11986
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: December 6, 2005
Last modified: November 24, 2009
This is version 97 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome X

Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents