Reviewed, UniProtKB/Swiss-Prot P32449 (AROG_YEAST)

Names and origin

Protein names

Recommended name:
    Phospho-2-dehydro-3-deoxyheptonate aldolase, tyrosine-inhibited
    EC=2.5.1.54
Alternative name(s):
    Phospho-2-keto-3-deoxyheptonate aldolase
    3-deoxy-D-arabino-heptulosonate 7-phosphate synthase
    DAHP synthase

Gene names

Name:	ARO4
Ordered Locus Names:	YBR249C
ORF Names:	YBR1701

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	370 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Stereospecific condensation of phosphoenolpyruvate (PEP) and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP).
Catalytic activity	Phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate.
Enzyme regulation	Inhibited by tyrosine.
Pathway	Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 1/7.
Induction	By amino acid starvation.
Miscellaneous	Present with 26300 molecules/cell in log phase SD medium. Ref.6
Sequence similarities	Belongs to the class-I DAHP synthase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Aromatic amino acid biosynthesis Stress response
Molecular function	Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	aromatic amino acid family biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW response to stress Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from direct assay. Source: SGD nucleus Inferred from direct assay. Source: SGD
Molecular function	3-deoxy-7-phosphoheptulonate synthase activity Inferred from direct assay. Source: SGD identical protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		1	EBI-2915,EBI-2915
SSA2	P10592	1	EBI-2915,EBI-8603

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 370

370

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

PRO_0000140851

Amino acid modifications

Modified residue

2

1

Phosphoserine Ref.7

Modified residue

4

1

Phosphoserine Ref.7

Modified residue

44

1

Phosphothreonine Ref.7

Modified residue

47

1

Phosphoserine Ref.7

Secondary structure

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370

Helix Strand Turn

Details...

Beta strand

25 – 29

5

Helix

34 – 40

7

Helix

45 – 62

18

Beta strand

68 – 74

7

Helix

81 – 98

18

Turn

99 – 101

3

Beta strand

102 – 107

6

Beta strand

115 – 118

4

Turn

122 – 124

3

Beta strand

128 – 130

3

Helix

134 – 149

16

Turn

150 – 152

3

Beta strand

155 – 158

4

Beta strand

161 – 163

3

Helix

165 – 168

4

Helix

169 – 171

3

Beta strand

173 – 177

5

Turn

179 – 183

5

Helix

185 – 191

7

Beta strand

198 – 201

4

Helix

209 – 218

10

Beta strand

223 – 227

5

Beta strand

231 – 238

8

Beta strand

244 – 248

5

Helix

259 – 267

9

Beta strand

276 – 281

6

Helix

282 – 284

3

Turn

285 – 287

3

Helix

289 – 291

3

Helix

292 – 304

13

Beta strand

309 – 317

9

Beta strand

319 – 323

5

Beta strand

339 – 342

4

Helix

347 – 367

21

Sequences

	Sequence		Length	Mass (Da)
	P32449-1 [UniParc]. Last modified February 1, 1994. Version 2. Checksum: 594ED48F24175979	FASTA	370	39,749
	10 20 30 40 50 60 MSESPMFAAN GMPKVNQGAE EDVRILGYDP LASPALLQVQ IPATPTSLET AKRGRREAID 70 80 90 100 110 120 IITGKDDRVL VIVGPCSIHD LEAAQEYALR LKKLSDELKG DLSIIMRAYL EKPRTTVGWK 130 140 150 160 170 180 GLINDPDVNN TFNINKGLQS ARQLFVNLTN IGLPIGSEML DTISPQYLAD LVSFGAIGAR 190 200 210 220 230 240 TTESQLHREL ASGLSFPVGF KNGTDGTLNV AVDACQAAAH SHHFMGVTKH GVAAITTTKG 250 260 270 280 290 300 NEHCFVILRG GKKGTNYDAK SVAEAKAQLP AGSNGLMIDY SHGNSNKDFR NQPKVNDVVC 310 320 330 340 350 360 EQIANGENAI TGVMIESNIN EGNQGIPAEG KAGLKYGVSI TDACIGWETT EDVLRKLAAA 370 VRQRREVNKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, primary structure and regulation of the ARO4 gene, encoding the tyrosine-inhibited 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Saccharomyces cerevisiae." Kuenzler M., Paravicini G., Egli C., Irniger S., Braus G.H. Gene 113:67-74(1992) [PubMed: 1348717] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	Kuenzler M. Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO 205-207.
[3]	"The complete sequence of a 6794 bp segment located on the right arm of chromosome II of Saccharomyces cerevisiae. Finding of a putative dUTPase in a yeast." Doignon F., Biteau N., Aigle M., Crouzet M. Yeast 9:1131-1137(1993) [PubMed: 8256522] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	"Complete DNA sequence of yeast chromosome II." Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K. EMBO J. 13:5795-5809(1994) [PubMed: 7813418] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"Cloning, primary structure, and regulation of the HIS7 gene encoding a bifunctional glutamine amidotransferase: cyclase from Saccharomyces cerevisiae." Kuenzler M., Balmelli T., Egli C.M., Paravicini G., Braus G.H. J. Bacteriol. 175:5548-5558(1993) [PubMed: 8366040] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 352-370.
[6]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-4; THR-44 AND SER-47, MASS SPECTROMETRY.
[8]	"Evolution of feedback-inhibited beta/alpha barrel isoenzymes by gene duplication and a single mutation." Hartmann M., Schneider T.R., Pfeil A., Heinrich G., Lipscomb W.N., Braus G.H. Proc. Natl. Acad. Sci. U.S.A. 100:862-867(2003) [PubMed: 12540830] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 23-369.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X61107 Genomic DNA. Translation: CAA43419.1.
L20296 Genomic DNA. Translation: AAA65607.1.
Z36118 Genomic DNA. Translation: CAA85212.1.

PIR

S38185.

RefSeq

NP_009808.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1HFB	X-ray	1.90	A/B/C/D/E/F/G/H	1-370	[»]
1OAB	X-ray	1.90	A/B	1-370	[»]
1OF6	X-ray	2.10	A/B/C/D/E/F/G/H	1-370	[»]
1OF8	X-ray	1.50	A/B	1-370	[»]
1OFA	X-ray	2.01	A/B	1-370	[»]
1OFB	X-ray	2.00	A/B	1-370	[»]
1OFO	X-ray	1.85	A/B	1-370	[»]
1OFP	X-ray	2.10	A/B/C/D	1-370	[»]
1OFQ	X-ray	2.70	A/B/C/D	1-370	[»]
1OFR	X-ray	2.70	A/B/C/D/E/F/G/H	1-370	[»]
1OG0	X-ray	2.70	A/B/C/D/E/F/G/H	1-370	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-4175N.

IntAct

P32449. 11 interactions.

STRING

P32449.

Proteomic databases

PeptideAtlas

P32449.

PRIDE

P32449.

Genome annotation databases

Ensembl

YBR249C; YBR249C; YBR249C; Saccharomyces cerevisiae. [Genome view]

GeneID

852551.

KEGG

sce:YBR249C.

NMPDR

fig|4932.3.peg.523.

Organism-specific databases

CYGD

YBR249c.

SGD

S000000453. ARO4.

Phylogenomic databases

eggNOG

fuNOG04423.

HOGENOM

HBG670536.

OMA

ITTTKGN.

OrthoDB

EOG9XSN62.

PhylomeDB

P32449.

Enzyme and pathway databases

BRENDA

2.5.1.54. 250.

Gene expression databases

ArrayExpress

P32449.

Genevestigator

P32449.

GermOnline

YBR249C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR013785. Aldolase_TIM.
IPR006218. DAHP1/KDSA.
IPR006219. DHAP_synth_1.
[Graphical view]

Gene3D

G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.

PANTHER

PTHR21225. AroFGH. 1 hit.

Pfam

PF00793. DAHP_synth_1. 1 hit.
[Graphical view]

PIRSF

PIRSF001361. DAHP_synthase. 1 hit.

TIGRFAMs

TIGR00034. aroFGH. 1 hit.

ProtoNet

Search...

Other Resources

NextBio

971640.

Entry information

Entry name

AROG_YEAST

Accession

Primary (citable) accession number: P32449

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	February 1, 1994
Last modified:	February 9, 2010
This is version 101 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)