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Neisseria gonorrhoeae Search Results

Record: 1 of 1  
MiniMap IGR0970 IGR0971 IGR0968 IGR0974 IGR0970.1 IGR0969 IGR0972 IGR0973 NG1201 trpG, - NG1204 psd, - NG1206 pivNG, - NG1200 trpD, - NG1203 NG1202 tonB, - NG1205 uvrA, - NG1207 hrpA, - NG1199 NG1201 trpG, - NG1204 psd, - NG1206 pivNG, - NG1200 trpD, - NG1203 NG1202 tonB, - NG1205 uvrA, - NG1207 hrpA, - NG1199 Type: inverse, Name:  - 167 Type: inverse, Name:  - 143 Type: inverse, Name:  - 144 Type: inverse, Name:  - 162 Type: inverse, Name:  - 182 NG1201 trpG, - NG1204 psd, - NG1206 pivNG, - NG1200 trpD, - NG1203 NG1202 tonB, - NG1205 uvrA, - NG1207 hrpA, - NG1199
* Calculated from Protein Sequence

Gene ID: NG1204

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
trpG  

Definition:
anthranilate synthase component II

Gene Start:
1151013

Gene Stop:
1150426

Gene Length:
588

Molecular Weight*:
21847

pI*:
5.60

Net Charge*:
-6.26

EC:
4.1.3.27  

Functional Class:
Amino acid biosynthesis; Aromatic amino acid family  

Pathway: pathway table
Phenylalanine, tyrosine and tryptophan biosynthesis

Secondary Evidence:
Essar,D.W., Eberly,L. and Crawford,I.P.
Evolutionary differences in chromosomal locations of four early
genes of the tryptophan pathway in fluorescent pseudomonads: DNA
sequences and characterization of Pseudomonas putida trpE and
trpGDC.
J. Bacteriol. 172 (2), 867-883 (1990)
MEDLINE: 90130325

Spraggon G, Kim C, Nguyen-Huu X, Yee MC, Yanofsky C, Mills SE.
The structures of anthranilate synthase of Serratia marcescens crystallized in the presence of (i) its substrates, chorismate and glutamine, and a product, glutamate, and (ii) its end-product inhibitor, L-tryptophan.
Proc Natl Acad Sci U S A. 2001 May;98(11):6021-6.
PMID: 11371633

Knöchel T, Ivens A, Hester G, Gonzalez A, Bauerle R, Wilmanns M, Kirschner K, Jansonius JN.
The crystal structure of anthranilate synthase from Sulfolobus solfataricus: functional implications.
Proc Natl Acad Sci U S A. 1999 Aug;96(17):9479-84.
PMID: 10449718

Lin C, Paradkar AS, Vining LC.
Regulation of an anthranilate synthase gene in Streptomyces venezuelae by a trp attenuator.
Microbiology. 1998 Jul;144 ( Pt 7):1971-80.
PMID: 9695930

Du H, Tarpey R, Babitzke P.
The trp RNA-binding attenuation protein regulates TrpG synthesis by binding to the trpG ribosome binding site of Bacillus subtilis.
J Bacteriol. 1997 Apr;179(8):2582-6.
PMID: 9098056

Comment:
Oklahoma ID: NGO.1204c

Component II provides glutamine amidotransferase activity. For component I see NG0872.

For other trp genes, see NG0248 (trpA), NG0274 (trpB), NG0872 (trpE), NG1203 (trpD), NG0261 (trpF), NG1721 (trpC)

Blast Summary:  PSI-Blast Search
Numerous matches in gapped BLAST to anthranilate synthase component II sequences. Residues 1-185 are 67% similar to the enzyme component in Pseudomonas putida ( gb|AAA80553).

Residues 1-196 are 95% similar to NMA1163 in N.meningitidis (AL162755).

COGS Summary:  COGS Search
BeTs to 11 clades of COG0512
COG name: Anthranilate/para-aminobenzoate synthases component I
Functional Class:  E,H
The phylogenetic pattern of COG0512 is amt-YqvcEbrHuj-------
Number of proteins in this genome belonging to this COG is 1

Blocks Summary:  Blocks Search
***** IPB001674 (GMP synthase C terminal domain) with a combined E-value of 2.3e-12.
    IPB001674B    74-83
    IPB001674D    163-184
***** IPB000991 (Glutamine amidotransferase class-I) with a combined E-value of 6.2e-11.
    IPB000991A    74-83
    IPB000991B    162-172


ProDom Summary:  Protein Domain Search
Residues 1-44 are 68% similar to a (SYNTHASE ANTHRANILATE COMPONENT II) protein domain (PD002064) which is seen in PABA_BACSU.

Residues 47-185 are 67% similar to a (SYNTHASE GLUTAMINE BIOSYNTHESIS AMIDOTRANSFERASE) protein domain (PD000306) which is seen in TRPG_PSEPU.



Paralogs:  Local Blast Search


NG1204 is paralogously related to NG2164 (GMP synthetase) (4e-13) and NG0053 (carbamoylphosphate synthase small subunit (CarA)) (2e-11).


Pfam Summary:  Pfam Search
Residues 3 to 188 (E-value = 2.4e-85) place NG1204 in the GATase family which is described as Glutamine amidotransferase class-I (PF00117)

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

PDB Hit:
pdb|1QDL|1QDL-B THE CRYSTAL STRUCTURE OF ANTHRANILATE SYNTHASE 167.0 1e-42
pdb|1I7Q|1I7Q-B ANTHRANILATE SYNTHASE FROM S. MARCESCENS 152.0 5e-38
pdb|1I1Q|1I1Q-B STRUCTURE OF THE COOPERATIVE ALLOSTERIC 142.0 4e-35
pdb|1M6V|1M6V-B CRYS

Gene Protein Sequence:
MLLFIDNYDSFTYNIVQYFAELGQEVAVRRNDDITLEEIEALNPQYLVIG
PGPCSPKEAGISVEAMRHFAGRLPIMGVCLGHQTIGEAFGGDVVRAKTLM
HGKVSPVSHSGKGMFKGLPNPVTCTRYHSLVIERGTLPDCLEITAWTEDG
EIMGVRHKEYAVEGVQFHPEALLTERGHDMLNNFLVEFQNFKPQKI

Gene Nucleotide Sequence:  Sequence Viewer
ATGCTTTTGTTTATCGACAATTACGACAGTTTTACTTACAACATCGTCCA
GTATTTCGCAGAATTGGGGCAGGAAGTCGCCGTGCGCCGCAACGATGATA
TTACGTTGGAGGAAATCGAGGCATTGAATCCGCAATATCTCGTTATCGGT
CCCGGACCGTGTTCCCCTAAGGAGGCGGGTATTTCAGTAGAAGCCATGCG
CCATTTTGCCGGCCGGCTGCCGATTATGGGCGTGTGCCTCGGGCATCAGA
CGATAGGCGAAGCGTTCGGTGGAGATGTGGTACGGGCAAAAACCTTGATG
CACGGTAAGGTGTCGCCCGTGTCCCATTCGGGCAAGGGTATGTTTAAGGG
TTTGCCCAATCCGGTTACCTGTACGCGTTATCACAGCCTCGTTATCGAAC
GCGGCACGCTGCCGGATTGCTTGGAAATCACGGCGTGGACGGAAGACGGC
GAAATTATGGGCGTGCGCCATAAGGAATATGCCGTCGAGGGCGTGCAGTT
CCACCCCGAAGCCCTCTTGACCGAACGCGGACATGATATGTTGAACAATT
TTTTAGTTGAATTTCAAAACTTCAAACCGCAAAAAATC


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