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

Neisseria gonorrhoeae Search Results

Record: 1 of 1  
MiniMap IGR0725 IGR0726 IGR0721 IGR0722 IGR0727 IGR0728.1 IGR0724 IGR0719.1 IGR0728 IGR0723 IGR0720 NG0867.1 NG0871 sbp, - NG0877 NG0876 NG0878 dedA, - NG0869 opcA, - NG0868 dcrD, - NG0874 dcmD, - NG0873 purK, - NG0875 trpE, - NG0872 uup,abcZ, - NG0870 NG0867.1 NG0871 sbp, - NG0877 NG0876 NG0878 dedA, - NG0869 opcA, - NG0868 dcrD, - NG0874 dcmD, - NG0873 purK, - NG0875 trpE, - NG0872 uup,abcZ, - NG0870 NG0871 NG0876 NG0878 dedA, - NG0869 opcA, - NG0868 dcrD, - NG0874 dcmD, - NG0873 purK, - NG0875 trpE, - NG0872 uup,abcZ, - NG0870 NG0867.1 sbp, - NG0877
* Calculated from Protein Sequence

Gene ID: NG0872

DNA Molecule Name:
1  

Genbank ID:
0

Gene Name:
trpE  

Definition:
anthranilate synthase component I

Gene Start:
855504

Gene Stop:
856976

Gene Length:
1473

Molecular Weight*:
54738

pI*:
5.40

Net Charge*:
-10.78

EC:
4.1.3.27  

Functional Class:
Amino acid biosynthesis; Aromatic amino acid family  

Pathway: pathway table
Phenylalanine, tyrosine and tryptophan biosynthesis

Primary Evidence:
Zhu,P., Morelli,G. and Achtman,M.,
The opcA and (psi)opcB regions in Neisseria: genes, pseudogenes, deletions, insertion elements and DNA islands,
Mol. Microbiol. 33 (3), 635-650 (1999)
Medline: 99348393


Secondary Evidence:
Makoff,A., Parry,N. and Dicken,L.
Translational fusions with fragments of the trpE gene improve the
expression of a poorly expressed heterologous gene in Escherichia
coli
J. Gen. Microbiol. 135 (Pt 1), 11-24 (1989)
Medline: 89381668

Kolter,R. and Yanofsky,C.
Genetic analysis of the tryptophan operon regulatory region using
site-directed mutagenesis
J. Mol. Biol. 175 (3), 299-312 (1984)
Medline: 84216335

Nichols,B.P., van Cleemput,M. and Yanofsky,C.
Nucleotide sequence of Escherichia coli trpE. Anthranilate
synthetase component I contains no tryptophan residues
J. Mol. Biol. 146 (1), 45-54 (1981)
Medline: 81267360

Yanofsky,C., Platt,T., Crawford,I.P., Nichols,B.P., Christie,G.E.,
Horowitz,H., VanCleemput,M. and Wu,A.M.
The complete nucleotide sequence of the tryptophan operon of
Escherichia coli
Nucleic Acids Res. 9 (24), 6647-6668 (1981)
Medline: 82150258






Comment:
Oklahoma ID: NGO.872

For other trp genes, see NG0248 (trpA), NG0274 (trpB), NG0261 (trpF), NG1203 (trpD), NG1204 (trpG), NG1721 (trpC)

For component II see NG1204.

Blast Summary:  PSI-Blast Search
NG0872 is 100% identical to a previously sequenced Neisseria gonorrhoeae protein in GenBank, 5051430.

Residues 1-491 are 95% similar to anthranilate synthase component I in Neisseria meningitidis group A strain Z2491 (11268487|).

Numerous hits in gapped BLAST to anthranilate synthase component I sequences,e.g.residues 102-481 are 39% similar to anthranilate synthase component I in Escherichia coli O157:H7 (13361301|).

COGS Summary:  COGS Search
BeTs to 11 clades of COG0147
COG name: Anthranilate/para-aminobenzoate synthases component II
Functional Class:  E,H
The phylogenetic pattern of COG0147 is amt-YQvCEBRHUJ-------
Number of proteins in this genome belonging to this COG is 2

Blocks Summary:  Blocks Search
***** PR00095 (Anthranilate synthase component I signature) with a combined E-value of 1.7e-30.
    PR00095A    322-335
    PR00095B    336-349
    PR00095C    416-430
    PR00095D    431-445


ProDom Summary:  Protein Domain Search
Residues 222-474 are 69% similar to a (SYNTHASE ANTHRANILATE BIOSYNTHESIS LYASE COMPONENT I) protein domain (PD000779) which is seen in TRPE_PSEAE.

Residues 25-174 are 54% similar to a (SYNTHASE ANTHRANILATE COMPONENT I) protein domain (PD001313) which is seen in TRPE_PSESS.



Paralogs:  Local Blast Search


NG0872 is paralogously related to NG2112 (para-aminobenzoate synthase component I) (5e-27).


Pfam Summary:  Pfam Search
Residues 20 to 172 (E-value = 8.1e-43) place NG0872 in the Anth_synt_I_N family which is described as Anthranilate synthase component I, N terminal region (PF04715)
Residues 220 to 482 (E-value = 1.9e-161) place NG0872 in the Chorismate_bind family which is described as chorismate binding enzyme (PF00425)

Structural Feature(s):
Feature Type  Start  Stop
No predicted structural features.  
  

PDB Hit:
pdb|1QDL|1QDL-A THE CRYSTAL STRUCTURE OF ANTHRANILATE SYNTHASE 250.0 3e-67
pdb|1I1Q|1I1Q-A STRUCTURE OF THE COOPERATIVE ALLOSTERIC 218.0 2e-57
pdb|1I7Q|1I7Q-A ANTHRANILATE SYNTHASE FROM S. MARCESCENS 210.0 6e-55
pdb|1K0E|1K0E-A THE

Gene Protein Sequence:
MISKQEYQAQAAQGYNRIPLVQELLADLDTPLSLYLKLANRPYTYLLESV
VGGERFGRYSFIGLPCSHYLKAGGKHVDVYQNGEIVEQYDGNPLPFIEAF
HNRFKTPEIPSLPRFTGGLVGYFGYETVYNFEHFAHRLKNTAKANPLGTP
DILLMLSQELAVIDNLSGKIHLIVYADPSQPDSYERARERLEDIRTQLRQ
SCAIPLSLGSKQTQAVSEFGEEPFKACVDKIKDYIFAGDCMQVVPSQRMS
MEFTDNPLALYRALRTLNPSPYLFYYDFGDFHIVGSSPEILVRRERDDVI
VRPIAGTRLRGKTPAEDLANEQDLLSDAKEIAEHVMLIDLGRNDVGRISK
TGEVKVTDKMVIEKYSHVMHIVSNVEGCLKEGVTNMDILAATFPAGTLSG
APKVRAMEIIEEIEPEKRGIYGGAVGVWGFNNDMDLAIAIRTAVIKNNTL
FIQSGAGVVADSDPTSEWQETQNKARAVVRAAQMVQEGLDK

Gene Nucleotide Sequence:  Sequence Viewer
ATGATCAGCAAACAAGAATACCAAGCCCAAGCCGCCCAAGGCTACAACCG
CATCCCGCTCGTGCAAGAACTCCTTGCCGACTTGGATACGCCGCTTTCCC
TCTATCTCAAACTCGCCAACCGCCCCTATACCTACCTGCTCGAATCCGTT
GTCGGCGGCGAACGTTTCGGCCGCTATTCCTTTATCGGCCTGCCTTGCAG
CCACTATCTCAAAGCCGGCGGCAAACACGTCGATGTTTATCAAAACGGCG
AAATCGTCGAACAATACGACGGCAATCCGCTACCCTTTATCGAAGCTTTC
CACAACCGTTTCAAAACACCCGAAATCCCAAGCCTGCCGCGCTTTACCGG
CGGCTTGGTCGGCTACTTCGGTTACGAAACCGTCTACAATTTCGAACACT
TCGCCCACCGCCTGAAAAACACCGCCAAAGCCAACCCGCTCGGCACGCCC
GATATTTTGCTGATGCTGTCGCAAGAGTTGGCGGTAATCGACAATTTGAG
CGGCAAAATCCACCTCATCGTTTATGCTGATCCCTCGCAGCCCGACAGCT
ACGAACGCGCCCGCGAACGCCTCGAAGACATCCGCACCCAGTTGCGCCAA
AGCTGCGCCATCCCACTTTCCCTCGGCAGCAAACAAACCCAAGCAGTCAG
CGAGTTCGGCGAAGAACCTTTCAAAGCCTGCGTCGATAAAATCAAAGACT
ACATTTTCGCAGGCGACTGTATGCAGGTCGTCCCCAGCCAACGCATGAGC
ATGGAATTTACCGACAATCCGCTTGCCCTCTACCGCGCCCTGCGCACGCT
CAACCCTTCGCCTTACCTCTTTTACTACGATTTCGGCGATTTCCACATCG
TCGGTTCCTCGCCCGAAATCCTCGTCCGCCGCGAACGCGACGACGTCATC
GTCCGCCCCATCGCCGGCACGCGCCTGCGCGGCAAAACCCCCGCCGAAGA
CCTTGCCAACGAACAAGATTTGTTAAGCGACGCCAAAGAAATCGCCGAAC
ACGTTATGCTTATCGATTTGGGGCGCAACGATGTCGGACGCATCAGCAAA
ACAGGCGAAGTCAAAGTCACCGACAAAATGGTGATTGAAAAATACTCCCA
TGTGATGCACATCGTTTCCAACGTCGAAGGCTGTTTGAAAGAGGGCGTTA
CCAATATGGACATCCTCGCCGCCACCTTCCCTGCCGGCACACTCTCCGGC
GCGCCAAAAGTCCGCGCGATGGAAATCATCGAAGAAATCGAACCGGAGAA
ACGCGGCATCTACGGCGGCGCCGTCGGCGTATGGGGCTTCAACAACGATA
TGGATTTGGCAATCGCCATCCGCACCGCCGTGATTAAAAACAATACCCTC
TTCATCCAAAGCGGCGCGGGCGTGGTTGCCGACTCCGACCCAACTTCCGA
ATGGCAGGAAACTCAAAACAAAGCCCGCGCAGTGGTTCGGGCGGCGCAGA
TGGTGCAGGAAGGGTTGGATAAA


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