Reviewed, UniProtKB/Swiss-Prot A8A0N9 (AROD_ECOHS)

Names and origin

Protein names

Recommended name:
    3-dehydroquinate dehydratase
      Short name=3-dehydroquinase
    EC=4.2.1.10
Alternative name(s):
    Type I DHQase

Gene names

Name:	aroD
Ordered Locus Names:	EcHS_A1774

Organism

Escherichia coli O9:H4 (strain HS) [Complete proteome] [HAMAP]

Taxonomic identifier

331112 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	252 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	3-dehydroquinate = 3-dehydroshikimate + H2O. HAMAP MF_00214
Pathway	Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. HAMAP MF_00214
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the type-I 3-dehydroquinase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Aromatic amino acid biosynthesis
Ligand	Schiff base
Molecular function	Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	aromatic amino acid family biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular function	3-dehydroquinate dehydratase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 252	252	3-dehydroquinate dehydratase HAMAP MF_00214		PRO_1000058630
Sites
	Active site	143	1	Proton acceptor By similarity
	Active site	170	1	Schiff-base intermediate with substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	A8A0N9-1 [UniParc]. Last modified October 23, 2007. Version 1. Checksum: 1B02EC6C184B004F	FASTA	252	27,477
	10 20 30 40 50 60 MKTVTVKDLV IGAGAPKIIV SLMAKDIARV KSEALAYREA DFDILEWRVD HFADLSNVES 70 80 90 100 110 120 VMAAAKILRE TMPEKPLLFT FRSAKEGGEQ AISTEAYIAL NRAAIDSGLV DMIDLELFTG 130 140 150 160 170 180 DDQVKETVAY AHAHDVKVVM SNHDFHKTPE AEEIIARLRK MQSFDADIPK IALMPQSTSD 190 200 210 220 230 240 VLTLLAATLE MQEQYADRPI ITMSMAKTGV ISRLAGEVFG SAATFGAVKK ASAPGQISVT 250 DLRTVLTILH QA

References

[1]

"The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates." Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J. J. Bacteriol. 190:6881-6893(2008) [PubMed: 18676672] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000802 Genomic DNA. Translation: ABV06093.1.
RefSeq	YP_001458476.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A8A0N9.
Genome annotation databases
GeneID	5595051.
GenomeReviews	Gene locus EcHS_A1774 in contig CP000802_GR.
KEGG	ecx:EcHS_A1774.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	MSNHDFD.
Family and domain databases
HAMAP	MF_00214. [Tree]
InterPro	IPR018508. 3-dehydroquinate_DH_AS. IPR013785. Aldolase_TIM. IPR001381. DHquinase_I. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
Pfam	PF01487. DHquinase_I. 1 hit. [Graphical view]
ProDom	PD005337. DHquinase_I. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR01093. aroD. 1 hit.
PROSITE	PS01028. DEHYDROQUINASE_I. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AROD_ECOHS

Accession

Primary (citable) accession number: A8A0N9

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	October 23, 2007
Last modified:	November 3, 2009
This is version 14 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)