Reviewed, UniProtKB/Swiss-Prot P05194 (AROD_ECOLI)

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:	b1693, JW1683

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [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	Evidence at protein level.

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 PEP: step 3/7. HAMAP MF_00214
Subunit structure	Homodimer. 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 Direct protein sequencing
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_0000138794
Sites
	Active site	143	1	Proton acceptor Ref.6
	Active site	170	1	Schiff-base intermediate with substrate Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P05194-1 [UniParc]. Last modified October 1, 1994. Version 2. Checksum: 0D4E7FAEAD5FCD48	FASTA	252	27,467
	10 20 30 40 50 60 MKTVTVKDLV IGTGAPKIIV SLMAKDIASV KSEALAYREA DFDILEWRVD HYADLSNVES 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 ASAPGQISVN 250 DLRTVLTILH QA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The overexpression and complete amino acid sequence of Escherichia coli 3-dehydroquinase." Duncan K., Chaudhuri S., Campbell M.S., Coggins J.R. Biochem. J. 238:475-483(1986) [PubMed: 3541912] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Identification of the active-site lysine residues of two biosynthetic 3-dehydroquinases." Chaudhuri S., Duncan K., Graham L.D., Coggins J.R. Biochem. J. 275:1-6(1991) [PubMed: 1826831] [Abstract] Cited for: PROTEIN SEQUENCE OF 162-172, SEQUENCE REVISION, ACTIVE SITE LYS-170.
[3]	"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T. DNA Res. 3:363-377(1996) [PubMed: 9097039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"Identification of the essential histidine residue at the active site of Escherichia coli dehydroquinase." Deka R.K., Kleanthous C., Coggins J.R. J. Biol. Chem. 267:22237-22242(1992) [PubMed: 1429576] [Abstract] Cited for: ACTIVE SITE HIS-143, PROTEIN SEQUENCE OF 141-158.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X59503 Genomic DNA. Translation: CAA42091.1. X04306 Genomic DNA. Translation: CAA27849.1. Sequence problems. U00096 Genomic DNA. Translation: AAC74763.1. AP009048 Genomic DNA. Translation: BAA15448.1.
PIR	DWECDQ. S14750.
RefSeq	AP_002313.1. NP_416208.1.
3D structure databases
HSSP	HSSP built from PDB template 1L9W based on UniProtKB P24670.
SMR	P05194. Positions 1-252.
ModBase	Search...
2-D gel databases
SWISS-2DPAGE	P05194.
Genome annotation databases
GeneID	946210.
GenomeReviews	Gene locus JW1683 in contig AP009048_GR. Gene locus b1693 in contig U00096_GR.
KEGG	ecj:JW1683. eco:b1693.
Organism-specific databases
EchoBASE	EB0074.
EcoGene	EG10076. aroD.
CMR	Search...
Phylogenomic databases
HOGENOM	P05194.
OMA	P05194. MSNHDFD.
Enzyme and pathway databases
BioCyc	EcoCyc:AROD-MON. MetaCyc:AROD-MON.
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_ECOLI

Accession

Primary (citable) accession number: P05194

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	October 1, 1994
Last modified:	June 16, 2009
This is version 79 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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