Basic Search | Intermediate Search | Advanced SQL Search | Gene Image Map |  Home

Haemophilus ducreyi Search Results

Record: 1 of 1  
MiniMap rRNA-5S-3 rRNA-23S-3 IGR440 IGR446 IGR443 IGR439 IGR445 IGR444 IGR438 IGR442 IGR441 IGR437 ftsN, - HD0639 mob, - HD0636 HD0637 arsC, - HD0631 aroD,aroQ, - HD0632 accB, - HD0634 por,dsbA, - HD0638 dapD, - HD0630 pqiA, - HD0629 accC, - HD0635 ftsN, - HD0639 mob, - HD0636 HD0637 arsC, - HD0631 aroD,aroQ, - HD0632 accB, - HD0634 por,dsbA, - HD0638 dapD, - HD0630 pqiA, - HD0629 accC, - HD0635 ftsN, - HD0639 mob, - HD0636 HD0637 arsC, - HD0631 aroD,aroQ, - HD0632 accB, - HD0634 por,dsbA, - HD0638 dapD, - HD0630 pqiA, - HD0629 accC, - HD0635
* Calculated from Protein Sequence

Gene ID: HD0632

DNA Molecule Name:
1  

Genbank ID:
0

Gene Name:
aroD  aroQ  

Definition:
probable 3-dehydroquinate dehydratase

Gene Start:
497409

Gene Stop:
497843

Gene Length:
435

Molecular Weight*:
16124

pI*:
6.80

Net Charge*:
-0.71

EC:
4.2.1.10  

Functional Class:
Amino acid biosynthesis; Aromatic amino acid family  

Pathway: pathway table
Phenylalanine, tyrosine and tryptophan biosynthesis

Secondary Evidence:
Gourley DG, Shrive AK, Polikarpov I, Krell T, Coggins JR, Hawkins AR, Isaacs NW, Sawyer L.
The two types of 3-dehydroquinase have distinct structures but catalyze the same overall reaction.
Nat Struct Biol. 1999 Jun;6(6):521-5.
PMID: 10360352

Florova G, Denoya CD, Morgenstern MR, Skinner DD, Reynolds KA.
Cloning, expression, and characterization of a type II 3-dehydroquinate dehydratase gene from Streptomyces hygroscopicus.
Arch Biochem Biophys. 1998 Feb 15;350(2):298-306.
PMID: 9473305

Boam DJ, Price NC, Kelly SM, Krell T, Coggins JR.
Evidence that the active site in type II dehydroquinase from Streptomyces coelicolor is near the single tryptophan.
Biochem Soc Trans. 1997 Feb;25(1):348; replaces 93S.
PMID: 9147947

Bottomley JR, Clayton CL, Chalk PA, Kleanthous C.
Cloning, sequencing, expression, purification and preliminary characterization of a type II dehydroquinase from Helicobacter pylori.
Biochem J. 1996 Oct 15;319 ( Pt 2):559-65.
PMID: 8912695

Comment:
For other "aro" genes, see HD1274 (aroC), HD1383 (aroA), HD1475 (aroG), HD0415 (aroE), HD0422 (aroB), HD0423 (aroK), HD0444 (aroF).

Blast Summary:  PSI-Blast Search
Numerous significant hits in gapped BLAST to 3-dehydroquinate dehydratase (3-dehydroquinase, Type II DHQase, or catabolic 3-dehydrogenase) proteins; e.g., residues 16-144 are 76% similar to AROQ_ACTPL [1168506], residues 16-143 are 57% similar to AROQ_HAEIN [1168508], and residues 16-144 are 58% similar to 3DHQ_EMENI [112781].

COGS Summary:  COGS Search
BeTs to 6 clades of COG0757
COG name: 3-dehydroquinate dehydratase II
Functional Class:  E
The phylogenetic pattern of COG0757 is ------vc-brhuj-------
Number of proteins in this genome belonging to this COG is 1

Blocks Summary:  Blocks Search
***** IPB001874 (Dehydroquinase class II) with a combined E-value of 6.8e-77.
    IPB001874A    4-38
    IPB001874B    39-79
    IPB001874C    95-136


ProDom Summary:  Protein Domain Search
Residues 111-144 are 76% similar to a (DEHYDRATASE 3-DEHYDROQUINATE) protein domain (PD015605) which is seen in AROQ_ACTPL.

Residues 26-110 are 75% similar to a (DEHYDRATASE 3-DEHYDROQUINATE) protein domain (PD004527) which is seen in AROQ_ACTPL.



Paralogs:  Local Blast Search
HD0632 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.


Pfam Summary:  Pfam Search
Residues 4 to 144 (E-value = 3.9e-92) place HD0632 in the DHquinase_II family which is described as Dehydroquinase class II (PF01220)

PDB Hit:
pdb|2DHQ|A Chain A, 3-Dehydroquinate Dehydratase From Mycobacte... 105 3e-024
pdb|1D0I|A Chain A, Crystal Structure Of Type Ii Dehydroquinase... 104 6e-024

Gene Protein Sequence:
MQNILLLNGPNLNMLGKREPHIYGDQTLLEIEQRLKQQAIKQGYNLLCFQ
ANGEEAIINRIHQAFGNIDFIIINPAAFTHTSIAIRDALLAVAIPFIEVH
LSNICSRESFRHHSYFSDISQGIICGLGPKGYDYALDFAISSLK$

Gene Nucleotide Sequence:  Sequence Viewer
ATGCAAAATATTCTTCTGTTAAATGGCCCTAACCTTAATATGTTAGGAAA
GCGTGAGCCACATATTTATGGCGATCAAACTTTATTAGAGATTGAACAAC
GCTTAAAACAGCAAGCGATTAAACAAGGTTATAATTTGCTATGTTTTCAA
GCTAATGGTGAGGAAGCGATCATTAATCGTATTCATCAAGCATTTGGTAA
CATTGATTTTATTATTATCAATCCAGCAGCGTTTACCCATACGAGTATTG
CAATCCGTGATGCATTGTTAGCCGTTGCTATTCCGTTTATTGAAGTGCAT
CTTTCAAATATTTGTAGTCGTGAAAGTTTTCGTCATCATTCCTATTTTAG
TGATATTTCACAAGGCATTATTTGTGGTTTAGGTCCGAAAGGTTATGATT
ATGCACTTGATTTTGCAATATCATCTTTAAAATAG


Los Alamos National Laboratory     
Operated by the University of California for the National Nuclear Security Administration,
of the US Department of Energy.     Copyright © 2001 UC | Disclaimer/Privacy