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Protein

Phospho-2-dehydro-3-deoxyheptonate aldolase, tyrosine-inhibited

Gene

ARO4

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Stereospecific condensation of phosphoenolpyruvate (PEP) and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP).

Catalytic activityi

Phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate.

Enzyme regulationi

Inhibited by tyrosine.

Pathwayi: chorismate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate.
Proteins known to be involved in the 7 steps of the subpathway in this organism are:
  1. Phospho-2-dehydro-3-deoxyheptonate aldolase, tyrosine-inhibited (ARO4), Phospho-2-dehydro-3-deoxyheptonate aldolase, phenylalanine-inhibited (ARO3)
  2. Pentafunctional AROM polypeptide (ARO1)
  3. Pentafunctional AROM polypeptide (ARO1)
  4. Pentafunctional AROM polypeptide (ARO1)
  5. Pentafunctional AROM polypeptide (ARO1)
  6. Pentafunctional AROM polypeptide (ARO1)
  7. Chorismate synthase (ARO2)
This subpathway is part of the pathway chorismate biosynthesis, which is itself part of Metabolic intermediate biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate, the pathway chorismate biosynthesis and in Metabolic intermediate biosynthesis.

GO - Molecular functioni

  • 3-deoxy-7-phosphoheptulonate synthase activity Source: SGD

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Aromatic amino acid biosynthesis, Stress response

Enzyme and pathway databases

BioCyciYEAST:YBR249C-MONOMER.
BRENDAi2.5.1.54. 984.
UniPathwayiUPA00053; UER00084.

Names & Taxonomyi

Protein namesi
Recommended name:
Phospho-2-dehydro-3-deoxyheptonate aldolase, tyrosine-inhibited (EC:2.5.1.54)
Alternative name(s):
3-deoxy-D-arabino-heptulosonate 7-phosphate synthase
DAHP synthase
Phospho-2-keto-3-deoxyheptonate aldolase
Gene namesi
Name:ARO4
Ordered Locus Names:YBR249C
ORF Names:YBR1701
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:YBR249C.
SGDiS000000453. ARO4.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00001408512 – 370Phospho-2-dehydro-3-deoxyheptonate aldolase, tyrosine-inhibitedAdd BLAST369

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP32449.
PRIDEiP32449.

PTM databases

iPTMnetiP32449.

Expressioni

Inductioni

By amino acid starvation.

Interactioni

Protein-protein interaction databases

BioGridi32944. 29 interactors.
DIPiDIP-4175N.
IntActiP32449. 6 interactors.
MINTiMINT-534785.

Structurei

Secondary structure

1370
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi25 – 29Combined sources5
Helixi34 – 40Combined sources7
Helixi45 – 62Combined sources18
Beta strandi68 – 74Combined sources7
Helixi81 – 98Combined sources18
Turni99 – 101Combined sources3
Beta strandi102 – 107Combined sources6
Beta strandi115 – 118Combined sources4
Turni122 – 124Combined sources3
Beta strandi128 – 130Combined sources3
Helixi134 – 149Combined sources16
Turni150 – 152Combined sources3
Beta strandi155 – 158Combined sources4
Beta strandi161 – 163Combined sources3
Helixi165 – 168Combined sources4
Helixi169 – 171Combined sources3
Beta strandi173 – 177Combined sources5
Turni179 – 183Combined sources5
Helixi185 – 192Combined sources8
Beta strandi198 – 201Combined sources4
Helixi209 – 218Combined sources10
Beta strandi223 – 227Combined sources5
Beta strandi231 – 238Combined sources8
Beta strandi244 – 248Combined sources5
Helixi259 – 268Combined sources10
Beta strandi276 – 281Combined sources6
Helixi282 – 285Combined sources4
Helixi289 – 291Combined sources3
Helixi292 – 304Combined sources13
Beta strandi309 – 317Combined sources9
Beta strandi319 – 323Combined sources5
Helixi330 – 333Combined sources4
Beta strandi339 – 342Combined sources4
Helixi347 – 367Combined sources21

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HFBX-ray1.90A/B/C/D/E/F/G/H1-370[»]
1OABX-ray1.90A/B1-370[»]
1OF6X-ray2.10A/B/C/D/E/F/G/H1-370[»]
1OF8X-ray1.50A/B1-370[»]
1OFAX-ray2.01A/B1-370[»]
1OFBX-ray2.00A/B1-370[»]
1OFOX-ray1.85A/B1-370[»]
1OFPX-ray2.10A/B/C/D1-370[»]
1OFQX-ray2.70A/B/C/D1-370[»]
1OFRX-ray2.70A/B/C/D/E/F/G/H1-370[»]
1OG0X-ray2.70A/B/C/D/E/F/G/H1-370[»]
ProteinModelPortaliP32449.
SMRiP32449.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32449.

Family & Domainsi

Sequence similaritiesi

Belongs to the class-I DAHP synthase family.Curated

Phylogenomic databases

HOGENOMiHOG000220501.
InParanoidiP32449.
KOiK01626.
OMAiSWETTDA.
OrthoDBiEOG092C2RSR.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR006218. DAHP1/KDSA.
IPR006219. DHAP_synth_1.
[Graphical view]
PANTHERiPTHR21225. PTHR21225. 1 hit.
PfamiPF00793. DAHP_synth_1. 1 hit.
[Graphical view]
PIRSFiPIRSF001361. DAHP_synthase. 1 hit.
TIGRFAMsiTIGR00034. aroFGH. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P32449-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSESPMFAAN GMPKVNQGAE EDVRILGYDP LASPALLQVQ IPATPTSLET
60 70 80 90 100
AKRGRREAID IITGKDDRVL VIVGPCSIHD LEAAQEYALR LKKLSDELKG
110 120 130 140 150
DLSIIMRAYL EKPRTTVGWK GLINDPDVNN TFNINKGLQS ARQLFVNLTN
160 170 180 190 200
IGLPIGSEML DTISPQYLAD LVSFGAIGAR TTESQLHREL ASGLSFPVGF
210 220 230 240 250
KNGTDGTLNV AVDACQAAAH SHHFMGVTKH GVAAITTTKG NEHCFVILRG
260 270 280 290 300
GKKGTNYDAK SVAEAKAQLP AGSNGLMIDY SHGNSNKDFR NQPKVNDVVC
310 320 330 340 350
EQIANGENAI TGVMIESNIN EGNQGIPAEG KAGLKYGVSI TDACIGWETT
360 370
EDVLRKLAAA VRQRREVNKK
Length:370
Mass (Da):39,749
Last modified:February 1, 1994 - v2
Checksum:i594ED48F24175979
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61107 Genomic DNA. Translation: CAA43419.1.
L20296 Genomic DNA. Translation: AAA65607.1.
Z36118 Genomic DNA. Translation: CAA85212.1.
BK006936 Genomic DNA. Translation: DAA07365.1.
PIRiS38185.
RefSeqiNP_009808.1. NM_001178597.1.

Genome annotation databases

EnsemblFungiiYBR249C; YBR249C; YBR249C.
GeneIDi852551.
KEGGisce:YBR249C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61107 Genomic DNA. Translation: CAA43419.1.
L20296 Genomic DNA. Translation: AAA65607.1.
Z36118 Genomic DNA. Translation: CAA85212.1.
BK006936 Genomic DNA. Translation: DAA07365.1.
PIRiS38185.
RefSeqiNP_009808.1. NM_001178597.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HFBX-ray1.90A/B/C/D/E/F/G/H1-370[»]
1OABX-ray1.90A/B1-370[»]
1OF6X-ray2.10A/B/C/D/E/F/G/H1-370[»]
1OF8X-ray1.50A/B1-370[»]
1OFAX-ray2.01A/B1-370[»]
1OFBX-ray2.00A/B1-370[»]
1OFOX-ray1.85A/B1-370[»]
1OFPX-ray2.10A/B/C/D1-370[»]
1OFQX-ray2.70A/B/C/D1-370[»]
1OFRX-ray2.70A/B/C/D/E/F/G/H1-370[»]
1OG0X-ray2.70A/B/C/D/E/F/G/H1-370[»]
ProteinModelPortaliP32449.
SMRiP32449.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32944. 29 interactors.
DIPiDIP-4175N.
IntActiP32449. 6 interactors.
MINTiMINT-534785.

PTM databases

iPTMnetiP32449.

Proteomic databases

MaxQBiP32449.
PRIDEiP32449.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBR249C; YBR249C; YBR249C.
GeneIDi852551.
KEGGisce:YBR249C.

Organism-specific databases

EuPathDBiFungiDB:YBR249C.
SGDiS000000453. ARO4.

Phylogenomic databases

HOGENOMiHOG000220501.
InParanoidiP32449.
KOiK01626.
OMAiSWETTDA.
OrthoDBiEOG092C2RSR.

Enzyme and pathway databases

UniPathwayiUPA00053; UER00084.
BioCyciYEAST:YBR249C-MONOMER.
BRENDAi2.5.1.54. 984.

Miscellaneous databases

EvolutionaryTraceiP32449.
PROiP32449.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR006218. DAHP1/KDSA.
IPR006219. DHAP_synth_1.
[Graphical view]
PANTHERiPTHR21225. PTHR21225. 1 hit.
PfamiPF00793. DAHP_synth_1. 1 hit.
[Graphical view]
PIRSFiPIRSF001361. DAHP_synthase. 1 hit.
TIGRFAMsiTIGR00034. aroFGH. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiAROG_YEAST
AccessioniPrimary (citable) accession number: P32449
Secondary accession number(s): D6VQP5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: February 1, 1994
Last modified: November 30, 2016
This is version 155 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 26300 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, 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 II
    Yeast (Saccharomyces cerevisiae) chromosome II: 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.