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Protein

Inositol-3-phosphate synthase

Gene

INO1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Pathwayi: myo-inositol biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes myo-inositol from D-glucose 6-phosphate.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Inositol-3-phosphate synthase (INO1)
  2. Inositol monophosphatase 2 (INM2), Inositol monophosphatase 1 (INM1)
This subpathway is part of the pathway myo-inositol biosynthesis, which is itself part of Polyol metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes myo-inositol from D-glucose 6-phosphate, the pathway myo-inositol biosynthesis and in Polyol metabolism.

GO - Molecular functioni

  • inositol-3-phosphate synthase activity Source: UniProtKB

GO - Biological processi

  • inositol biosynthetic process Source: UniProtKB
  • phospholipid biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

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.
ReactomeiR-SCE-1855183. 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
Proteomesi
  • UP000002311 Componenti: Chromosome X

Organism-specific databases

EuPathDBiFungiDB:YJL153C.
SGDiS000003689. INO1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001951851 – 533Inositol-3-phosphate synthaseAdd BLAST533

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei368PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP11986.
PRIDEiP11986.

PTM databases

iPTMnetiP11986.

Interactioni

Protein-protein interaction databases

BioGridi33607. 56 interactors.
DIPiDIP-5687N.
IntActiP11986. 20 interactors.
MINTiMINT-551495.

Structurei

Secondary structure

1533
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi11 – 14Combined sources4
Beta strandi19 – 22Combined sources4
Beta strandi25 – 39Combined sources15
Beta strandi43 – 59Combined sources17
Beta strandi64 – 71Combined sources8
Turni72 – 74Combined sources3
Helixi76 – 89Combined sources14
Beta strandi94 – 96Combined sources3
Beta strandi99 – 101Combined sources3
Helixi109 – 112Combined sources4
Beta strandi114 – 119Combined sources6
Beta strandi121 – 123Combined sources3
Beta strandi125 – 129Combined sources5
Helixi130 – 132Combined sources3
Helixi139 – 141Combined sources3
Beta strandi142 – 147Combined sources6
Helixi154 – 161Combined sources8
Helixi166 – 176Combined sources11
Helixi188 – 190Combined sources3
Helixi193 – 198Combined sources6
Beta strandi207 – 209Combined sources3
Helixi216 – 233Combined sources18
Beta strandi239 – 243Combined sources5
Turni255 – 257Combined sources3
Beta strandi258 – 260Combined sources3
Helixi261 – 269Combined sources9
Helixi277 – 287Combined sources11
Beta strandi292 – 294Combined sources3
Beta strandi296 – 298Combined sources3
Helixi303 – 312Combined sources10
Beta strandi316 – 321Combined sources6
Helixi325 – 338Combined sources14
Beta strandi342 – 352Combined sources11
Helixi355 – 360Combined sources6
Helixi363 – 375Combined sources13
Helixi378 – 382Combined sources5
Turni385 – 387Combined sources3
Turni390 – 392Combined sources3
Beta strandi397 – 404Combined sources8
Helixi406 – 408Combined sources3
Beta strandi411 – 421Combined sources11
Helixi423 – 425Combined sources3
Beta strandi427 – 437Combined sources11
Helixi438 – 457Combined sources20
Beta strandi459 – 463Combined sources5
Beta strandi466 – 468Combined sources3
Helixi482 – 487Combined sources6
Beta strandi488 – 490Combined sources3
Helixi503 – 517Combined sources15
Helixi528 – 531Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11986.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00390000018395.
HOGENOMiHOG000013469.
InParanoidiP11986.
KOiK01858.
OMAiGVPYING.
OrthoDBiEOG092C1EEM.

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.
SUPFAMiSSF51735. SSF51735. 2 hits.

Sequencei

Sequence statusi: Complete.

P11986-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTEDNIAPIT SVKVVTDKCT YKDNELLTKY SYENAVVTKT ASGRFDVTPT
60 70 80 90 100
VQDYVFKLDL KKPEKLGIML IGLGGNNGST LVASVLANKH NVEFQTKEGV
110 120 130 140 150
KQPNYFGSMT QCSTLKLGID AEGNDVYAPF NSLLPMVSPN DFVVSGWDIN
160 170 180 190 200
NADLYEAMQR SQVLEYDLQQ RLKAKMSLVK PLPSIYYPDF IAANQDERAN
210 220 230 240 250
NCINLDEKGN VTTRGKWTHL QRIRRDIQNF KEENALDKVI VLWTANTERY
260 270 280 290 300
VEVSPGVNDT MENLLQSIKN DHEEIAPSTI FAAASILEGV PYINGSPQNT
310 320 330 340 350
FVPGLVQLAE HEGTFIAGDD LKSGQTKLKS VLAQFLVDAG IKPVSIASYN
360 370 380 390 400
HLGNNDGYNL SAPKQFRSKE ISKSSVIDDI IASNDILYND KLGKKVDHCI
410 420 430 440 450
VIKYMKPVGD SKVAMDEYYS ELMLGGHNRI SIHNVCEDSL LATPLIIDLL
460 470 480 490 500
VMTEFCTRVS YKKVDPVKED AGKFENFYPV LTFLSYWLKA PLTRPGFHPV
510 520 530
NGLNKQRTAL ENFLRLLIGL PSQNELRFEE RLL
Length:533
Mass (Da):59,642
Last modified:December 6, 2005 - v3
Checksum:i282E2AE5D156289D
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti14V → RL (PubMed:2642902).Curated1
Sequence conflicti14V → RL (PubMed:7975896).Curated1
Sequence conflicti60L → FE (PubMed:2642902).Curated1
Sequence conflicti60L → FE (PubMed:7975896).Curated1
Sequence conflicti66 – 93LGIML…KHNVE → TRNYAHWVRWLQQWLTLWPR YWRISTMWS (PubMed:2642902).CuratedAdd BLAST28
Sequence conflicti66 – 93LGIML…KHNVE → TRNYAHWVRWLQQWLTLWPR YWRISTMWS (PubMed:7975896).CuratedAdd BLAST28
Sequence conflicti98E → AK (PubMed:2642902).Curated1
Sequence conflicti98E → AK (PubMed:7975896).Curated1
Sequence conflicti140 – 141ND → KH (PubMed:2642902).Curated2
Sequence conflicti140 – 141ND → KH (PubMed:7975896).Curated2
Sequence conflicti201N → Q (PubMed:2642902).Curated1
Sequence conflicti201N → Q (PubMed:7975896).Curated1
Sequence conflicti444P → A (PubMed:2642902).Curated1
Sequence conflicti444P → A (PubMed:7975896).Curated1
Sequence conflicti476 – 497NFYPV…TRPGF → ELLSSFNLLELLVKSSINKN QDL in AAA66310 (PubMed:2642902).CuratedAdd BLAST22
Sequence conflicti524 – 533NELRFEERLL → KRTKIRREIVVISFQRLSFS FSAYL in AAA34706 (PubMed:2642902).Curated10

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33607. 56 interactors.
DIPiDIP-5687N.
IntActiP11986. 20 interactors.
MINTiMINT-551495.

PTM databases

iPTMnetiP11986.

Proteomic databases

MaxQBiP11986.
PRIDEiP11986.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YJL153C.
SGDiS000003689. INO1.

Phylogenomic databases

GeneTreeiENSGT00390000018395.
HOGENOMiHOG000013469.
InParanoidiP11986.
KOiK01858.
OMAiGVPYING.
OrthoDBiEOG092C1EEM.

Enzyme and pathway databases

UniPathwayiUPA00823; UER00787.
BioCyciYEAST:YJL153C-MONOMER.
ReactomeiR-SCE-1855183. Synthesis of IP2, IP, and Ins in the cytosol.
SABIO-RKP11986.

Miscellaneous databases

EvolutionaryTraceiP11986.
PROiP11986.

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.
SUPFAMiSSF51735. SSF51735. 2 hits.
ProtoNetiSearch...

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: November 2, 2016
This is version 160 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

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.