UniProtKB - P0AB91 (AROG_ECOLI)

BLAST

>sp|P0AB91|AROG_ECOLI Phospho-2-dehydro-3-deoxyheptonate aldolase, Phe-sensitive OS=Escherichia coli (strain K12) OX=83333 GN=aroG PE=1 SV=1
MNYQNDDLRIKEIKELLPPVALLEKFPATENAANTVAHARKAIHKILKGNDDRLLVVIGP
CSIHDPVAAKEYATRLLALREELKDELEIVMRVYFEKPRTTVGWKGLINDPHMDNSFQIN
DGLRIARKLLLDINDSGLPAAGEFLDMITPQYLADLMSWGAIGARTTESQVHRELASGLS
CPVGFKNGTDGTIKVAIDAINAAGAPHCFLSVTKWGHSAIVNTSGNGDCHIILRGGKEPN
YSAKHVAEVKEGLNKAGLPAQVMIDFSHANSSKQFKKQMDVCADVCQQIAGGEKAIIGVM
VESHLVEGNQSLESGEPLAYGKSITDACIGWEDTDALLRQLANAVKARRG

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History
Entry version 106 (07 Nov 2018)
Sequence version 1 (21 Jul 1986)
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Protein

Phospho-2-dehydro-3-deoxyheptonate aldolase, Phe-sensitive

Gene

aroG

Organism

Escherichia coli (strain K12)

Status

Reviewed-Annotation score: -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).

Miscellaneous

There are 3 DAHP synthases, AroG is feedback-inhibited by Phe. The other 2 DAHP synthases are Tyr- and Trp-sensitive, respectively.

Catalytic activityⁱ

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

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:

Phospho-2-dehydro-3-deoxyheptonate aldolase, Phe-sensitive (aroG), Phospho-2-dehydro-3-deoxyheptonate aldolase, Trp-sensitive (aroH), Phospho-2-dehydro-3-deoxyheptonate aldolase, Tyr-sensitive (aroF)
3-dehydroquinate synthase (aroB)
3-dehydroquinate dehydratase (aroD)
Shikimate dehydrogenase (NADP(+)) (aroE), Quinate/shikimate dehydrogenase (ydiB)
Shikimate kinase 2 (aroL), Shikimate kinase 1 (aroK)
3-phosphoshikimate 1-carboxyvinyltransferase (aroA)
Chorismate synthase (aroC)

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: EcoCyc
Inferred from direct assayⁱ
- 12952
identical protein binding
Source: EcoCyc
Inferred from direct assayⁱ
- 26682

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

aromatic amino acid family biosynthetic process
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
chorismate biosynthetic process Source: UniProtKB-UniPathway

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Transferase
Biological process	Amino-acid biosynthesis, Aromatic amino acid biosynthesis

Enzyme and pathway databases

BioCycⁱ	EcoCyc:AROG-MONOMER MetaCyc:AROG-MONOMER
BRENDAⁱ	2.5.1.54 2026
SABIO-RKⁱ	P0AB91
UniPathwayⁱ	UPA00053;UER00084

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Phospho-2-dehydro-3-deoxyheptonate aldolase, Phe-sensitive (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:aroG Ordered Locus Names:b0754, JW0737
Organismⁱ	Escherichia coli (strain K12)
Taxonomic identifierⁱ	83333 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli
Proteomesⁱ	UP000000318 Componentⁱ: Chromosome UP000000625 Componentⁱ: Chromosome

Organism-specific databases

EcoGeneⁱ	EG10079 aroG

EcoGeneⁱ

EG10079 aroG

Subcellular locationⁱ

GO - Cellular componentⁱ

cytoplasm
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
cytosol
Source: EcoCyc
Inferred from direct assayⁱ
- 15911532
- 18304323

View the complete GO annotation on QuickGO ...

Pathology & Biotechⁱ

Chemistry databases

Drug and drug target database More...DrugBankⁱ	DB02726 2-Phosphoglycolic Acid DB01819 Phosphoenolpyruvate

DrugBankⁱ

DB02726 2-Phosphoglycolic Acid
DB01819 Phosphoenolpyruvate

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000140835	1 – 350	Phospho-2-dehydro-3-deoxyheptonate aldolase, Phe-sensitiveAdd BLAST		350

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Modified residueⁱ	244	N6-acetyllysine1 Publication		1

Keywords - PTMⁱ

Acetylation

Proteomic databases

EPDⁱ	P0AB91
PaxDbⁱ	P0AB91
PRIDEⁱ	P0AB91

2D gel databases

SWISS-2DPAGEⁱ	P0AB91

SWISS-2DPAGEⁱ

P0AB91

PTM databases

iPTMnetⁱ	P0AB91

iPTMnetⁱ

P0AB91

Interactionⁱ

Subunit structureⁱ

Homotetramer.

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
itself		5	EBI-1120055,EBI-1120055

With

Entry

#Exp.

IntAct

Notes

itself

EBI-1120055,EBI-1120055

GO - Molecular functionⁱ

identical protein binding
Source: EcoCyc
Inferred from direct assayⁱ
- 26682

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	4261709, 17 interactors
Database of interacting proteins More...DIPⁱ	DIP-35898N
IntActⁱ	P0AB91, 3 interactors
STRINGⁱ	316385.ECDH10B_0821

Chemistry databases

BindingDBⁱ

P0AB91

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	10 – 14	Combined sources	5
Helixⁱ	19 – 25	Combined sources	7
Helixⁱ	30 – 47	Combined sources	18
Beta strandⁱ	54 – 59	Combined sources	6
Helixⁱ	66 – 82	Combined sources	17
Turnⁱ	83 – 86	Combined sources	4
Beta strandⁱ	87 – 92	Combined sources	6
Beta strandⁱ	100 – 103	Combined sources	4
Turnⁱ	107 – 109	Combined sources	3
Beta strandⁱ	113 – 115	Combined sources	3
Helixⁱ	119 – 135	Combined sources	17
Beta strandⁱ	140 – 143	Combined sources	4
Beta strandⁱ	146 – 148	Combined sources	3
Helixⁱ	150 – 153	Combined sources	4
Helixⁱ	154 – 156	Combined sources	3
Beta strandⁱ	158 – 162	Combined sources	5
Turnⁱ	164 – 168	Combined sources	5
Helixⁱ	170 – 177	Combined sources	8
Beta strandⁱ	183 – 186	Combined sources	4
Helixⁱ	194 – 203	Combined sources	10
Beta strandⁱ	208 – 212	Combined sources	5
Beta strandⁱ	216 – 223	Combined sources	8
Beta strandⁱ	229 – 233	Combined sources	5
Beta strandⁱ	236 – 238	Combined sources	3
Helixⁱ	243 – 255	Combined sources	13
Beta strandⁱ	262 – 265	Combined sources	4
Helixⁱ	268 – 270	Combined sources	3
Turnⁱ	271 – 273	Combined sources	3
Helixⁱ	275 – 277	Combined sources	3
Helixⁱ	278 – 290	Combined sources	13
Beta strandⁱ	295 – 303	Combined sources	9
Beta strandⁱ	305 – 309	Combined sources	5
Beta strandⁱ	312 – 314	Combined sources	3
Beta strandⁱ	323 – 326	Combined sources	4
Helixⁱ	331 – 349	Combined sources	19

Show more details

3D structure databases

ProteinModelPortalⁱ	P0AB91
SMRⁱ	P0AB91
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P0AB91

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the class-I DAHP synthase family.Curated

Phylogenomic databases

eggNOGⁱ	ENOG4105E99 Bacteria COG0722 LUCA
HOGENOMⁱ	HOG000220501
InParanoidⁱ	P0AB91
KEGG Orthology (KO) More...KOⁱ	K01626
PhylomeDBⁱ	P0AB91

Family and domain databases

Gene3Dⁱ	3.20.20.70, 1 hit
InterProⁱ	View protein in InterPro IPR013785 Aldolase_TIM IPR006218 DAHP1/KDSA IPR006219 DHAP_synth_1
PANTHERⁱ	PTHR21225 PTHR21225, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00793 DAHP_synth_1, 1 hit
PIRSFⁱ	PIRSF001361 DAHP_synthase, 1 hit
TIGRFAMsⁱ	TIGR00034 aroFGH, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P0AB91-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MNYQNDDLRI KEIKELLPPV ALLEKFPATE NAANTVAHAR KAIHKILKGN 
        60         70         80         90        100
DDRLLVVIGP CSIHDPVAAK EYATRLLALR EELKDELEIV MRVYFEKPRT 
       110        120        130        140        150
TVGWKGLIND PHMDNSFQIN DGLRIARKLL LDINDSGLPA AGEFLDMITP 
       160        170        180        190        200
QYLADLMSWG AIGARTTESQ VHRELASGLS CPVGFKNGTD GTIKVAIDAI 
       210        220        230        240        250
NAAGAPHCFL SVTKWGHSAI VNTSGNGDCH IILRGGKEPN YSAKHVAEVK 
       260        270        280        290        300
EGLNKAGLPA QVMIDFSHAN SSKQFKKQMD VCADVCQQIA GGEKAIIGVM 
       310        320        330        340        350
VESHLVEGNQ SLESGEPLAY GKSITDACIG WEDTDALLRQ LANAVKARRG

Length:350

Mass (Da):38,010

Last modified:July 21, 1986 - v1

Checksum:ⁱ7477D361962E8710

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	J01591 Genomic DNA Translation: AAA23492.1 U00096 Genomic DNA Translation: AAC73841.1 AP009048 Genomic DNA Translation: BAA35416.1
PIRⁱ	A01106 ADECHF
NCBI Reference Sequences More...RefSeqⁱ	NP_415275.1, NC_000913.3 WP_001109196.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC73841; AAC73841; b0754 BAA35416; BAA35416; BAA35416
GeneIDⁱ	945605
KEGGⁱ	ecj:JW0737 eco:b0754
PATRICⁱ	fig\|1411691.4.peg.1525

Protein	Similar proteins		Species	Score	Length	Source
P0AB91	Phospho-2-dehydro-3-deoxyheptonate aldolase, Phe-sensitive		ECO57		350	UniRef100_P0AB92
Phospho-2-dehydro-3-deoxyheptonate aldolase Phe-sensitive		Shigella sp.		350
Phospho-2-dehydro-3-deoxyheptonate aldolase		Escherichia coli M8		350
Phospho-2-dehydro-3-deoxyheptonate aldolase		SHIBO		350
Phospho-2-dehydro-3-deoxyheptonate aldolase		ECOLX		350
+77

Protein	Similar proteins		Species	Score	Length	Source
P0AB91	Phospho-2-dehydro-3-deoxyheptonate aldolase, Phe-sensitive		ECO57		350	UniRef90_P0AB92
Phospho-2-dehydro-3-deoxyheptonate aldolase Phe-sensitive		Shigella sp.		350
Phospho-2-dehydro-3-deoxyheptonate aldolase		Escherichia coli M8		350
Phospho-2-dehydro-3-deoxyheptonate aldolase		SHIBO		350
Phospho-2-dehydro-3-deoxyheptonate aldolase		ECOLX		350
+1173

Protein	Similar proteins		Species	Score	Length	Source
P0AB91	Phospho-2-dehydro-3-deoxyheptonate aldolase, Phe-sensitive		ECO57		350	UniRef50_P0AB92
Phospho-2-dehydro-3-deoxyheptonate aldolase Phe-sensitive		Shigella sp.		350
Phospho-2-dehydro-3-deoxyheptonate aldolase		Escherichia coli M8		350
Phospho-2-dehydro-3-deoxyheptonate aldolase		SHIBO		350
Phospho-2-dehydro-3-deoxyheptonate aldolase		ECOLX		350
+1234

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	J01591 Genomic DNA Translation: AAA23492.1 U00096 Genomic DNA Translation: AAC73841.1 AP009048 Genomic DNA Translation: BAA35416.1
PIRⁱ	A01106 ADECHF
RefSeqⁱ	NP_415275.1, NC_000913.3 WP_001109196.1, NZ_LN832404.1

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1GG1	X-ray	2.00	A/B/C/D	1-350	[»]
	1KFL	X-ray	2.80	A/B/C/D/E/F/G/H	2-350	[»]
	1N8F	X-ray	1.75	A/B/C/D	1-350	[»]
	1QR7	X-ray	2.60	A/B/C/D	1-350	[»]
	5CKS	X-ray	2.12	A/B/C/D	1-350	[»]
ProteinModelPortalⁱ	P0AB91
SMRⁱ	P0AB91
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	4261709, 17 interactors
DIPⁱ	DIP-35898N
IntActⁱ	P0AB91, 3 interactors
STRINGⁱ	316385.ECDH10B_0821

Chemistry databases

BindingDBⁱ	P0AB91
DrugBankⁱ	DB02726 2-Phosphoglycolic Acid DB01819 Phosphoenolpyruvate

PTM databases

iPTMnetⁱ	P0AB91

iPTMnetⁱ

P0AB91

2D gel databases

SWISS-2DPAGEⁱ	P0AB91

SWISS-2DPAGEⁱ

P0AB91

Proteomic databases

EPDⁱ	P0AB91
PaxDbⁱ	P0AB91
PRIDEⁱ	P0AB91

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAC73841; AAC73841; b0754 BAA35416; BAA35416; BAA35416
GeneIDⁱ	945605
KEGGⁱ	ecj:JW0737 eco:b0754
PATRICⁱ	fig\|1411691.4.peg.1525

Organism-specific databases

EchoBASEⁱ	EB0077
EcoGeneⁱ	EG10079 aroG

Phylogenomic databases

eggNOGⁱ	ENOG4105E99 Bacteria COG0722 LUCA
HOGENOMⁱ	HOG000220501
InParanoidⁱ	P0AB91
KOⁱ	K01626
PhylomeDBⁱ	P0AB91

Enzyme and pathway databases

UniPathwayⁱ	UPA00053;UER00084
BioCycⁱ	EcoCyc:AROG-MONOMER MetaCyc:AROG-MONOMER
BRENDAⁱ	2.5.1.54 2026
SABIO-RKⁱ	P0AB91

Miscellaneous databases

EvolutionaryTraceⁱ	P0AB91
Protein Ontology More...PROⁱ	PR:P0AB91

Family and domain databases

Gene3Dⁱ	3.20.20.70, 1 hit
InterProⁱ	View protein in InterPro IPR013785 Aldolase_TIM IPR006218 DAHP1/KDSA IPR006219 DHAP_synth_1
PANTHERⁱ	PTHR21225 PTHR21225, 1 hit
Pfamⁱ	View protein in Pfam PF00793 DAHP_synth_1, 1 hit
PIRSFⁱ	PIRSF001361 DAHP_synthase, 1 hit
TIGRFAMsⁱ	TIGR00034 aroFGH, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	AROG_ECOLI
Accessionⁱ	P0AB91Primary (citable) accession number: P0AB91 Secondary accession number(s): P00886
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
	Last sequence update:	July 21, 1986
	Last modified:	November 7, 2018
	This is version 106 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

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

Documents

SIMILARITY comments
Index of protein domains and families
PATHWAY comments
Index of metabolic and biosynthesis pathways
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Escherichia coli
Escherichia coli (strain K12): entries and cross-references to EcoGene

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P0AB91 (AROG_ECOLI)

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Phospho-2-dehydro-3-deoxyheptonate aldolase, Phe-sensitive

aroG

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Miscellaneous

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: chorismate biosynthesis

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

2D gel databases

PTM databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

UniProt is an ELIXIR core data resource

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Functionⁱ

Pathwayⁱ: chorismate biosynthesis

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ