Reviewed, UniProtKB/Swiss-Prot Q8FH42 (AROD_ECOL6)

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:	c2088

Organism

Escherichia coli O6 [Complete proteome] [HAMAP]

Taxonomic identifier

217992 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	252 AA.
Sequence status	Complete.
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. HAMAP MF_00214
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_0000138795
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)
	Q8FH42-1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 0E9F687C6D590F8C	FASTA	252	27,449
	10 20 30 40 50 60 MKTVTVKDLV IGTGAPKIIV SLMAKDIASV KSEALAYREA DFDILEWRVD HYADLSNVES 70 80 90 100 110 120 VIAAAKILRE 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 ASAPGQISVN 250 DLRTVLTILH QA

References

[1]

"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli." Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R. Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed: 12471157] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O6:H1 / CFT073 / ATCC 700928 / UPEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014075 Genomic DNA. Translation: AAN80548.1.
RefSeq	NP_753983.1.
3D structure databases
SMR	Q8FH42. Positions 1-252.
ModBase	Search...
Genome annotation databases
GeneID	1036367.
GenomeReviews	Gene locus c2088 in contig AE014075_GR.
KEGG	ecc:c2088.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG732926.
OMA	MSNHDFD.
Enzyme and pathway databases
BRENDA	4.2.1.10. 292881.
Family and domain databases
HAMAP	MF_00214. AroD. [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]
TIGRFAMs	TIGR01093. aroD. 1 hit.
PROSITE	PS01028. DEHYDROQUINASE_I. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AROD_ECOL6

Accession

Primary (citable) accession number: Q8FH42

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 22, 2003
Last sequence update:	March 1, 2003
Last modified:	February 9, 2010
This is version 45 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)