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

Neisseria gonorrhoeae Search Results

Record: 1 of 1  
MiniMap IGR0328 IGR0329 IGR0330 IGR0336 IGR0337 IGR0331 IGR0332 IGR0334 IGR0333 IGR0335 NG0393 htpX, - NG0399 murB, - NG0394 NG0395 NG0396 adk, - NG0400 pyrF, - NG0401 rfaE, - NG0402 gme,rfaD, - NG0403 hisZ,hisS, - NG0397 purA, - NG0398 NG0393 htpX, - NG0399 murB, - NG0394 NG0395 NG0396 adk, - NG0400 pyrF, - NG0401 rfaE, - NG0402 gme,rfaD, - NG0403 hisZ,hisS, - NG0397 purA, - NG0398 NG0393 htpX, - NG0399 murB, - NG0394 NG0395 NG0396 adk, - NG0400 pyrF, - NG0401 rfaE, - NG0402 gme,rfaD, - NG0403 hisZ,hisS, - NG0397 purA, - NG0398
* Calculated from Protein Sequence

Gene ID: NG0398

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
purA  

Definition:
adenylosuccinate synthetase

Gene Start:
389909

Gene Stop:
391210

Gene Length:
1302

Molecular Weight*:
45970

pI*:
6.40

Net Charge*:
-3.23

EC:
6.3.4.4  

Functional Class:
Purines, pyrimidines, nucleosides, and nucleotides; Purine ribonucleotide biosynthesis  

Pathway: pathway table
Alanine and aspartate metabolism
Purine metabolism

Secondary Evidence:
Lawrence,M.L., Cooper,R.K. and Thune,R.L. 1997. Attenuation, persistence, and vaccine potential of an Edwardsiella ictaluri purA mutant. Infect. Immun. 65 (11): 4642-4651. Medline: 98013094.

Dong,Q. and Fromm,H.J.
Chemical modification of adenylosuccinate synthetase from
Escherichia coli by pyridoxal 5'-phosphate. Identification of an
active site lysyl residue
J. Biol. Chem. 265 (11), 6235-6240 (1990)
M:90202896

Dong,Q., Liu,F., Myers,A.M. and Fromm,H.J.
Evidence for an arginine residue at the substrate binding site of
Escherichia coli adenylosuccinate synthetase as studied by chemical modification and site-directed mutagenesis
J. Biol. Chem. 266 (19), 12228-12233 (1991)
M:91286237

Liu,F., Dong,Q. and Fromm,H.J.
Site-directed mutagenesis of the phosphate-binding consensus
sequence in Escherichia coli adenylosuccinate synthetase
J. Biol. Chem. 267 (4), 2388-2392 (1992)
M:92129317

Silva,M.M., Poland,B.W., Hoffman,C.R., Fromm,H.J. and Honzatko,R.B.
Refined crystal structures of unligated adenylosuccinate synthetase from Escherichia coli
J. Mol. Biol. 254 (3), 431-446 (1995)
M:96095802

Poland,B.W., Lee,S.F., Subramanian,M.V., Siehl,D.L., Anderson,R.J., Fromm,H.J. and Honzatko,R.B.
Refined crystal structure of adenylosuccinate synthetase from
Escherichia coli complexed with hydantocidin 5'-phosphate, GDP,
HPO4(2-), Mg2+, and hadacidin
Biochemistry 35 (49), 15753-15759 (1996)
M:97121272

Poland,B.W., Fromm,H.J. and Honzatko,R.B.
Crystal structures of adenylosuccinate synthetase from Escherichia
coli complexed with GDP, IMP hadacidin, NO3-, and Mg2+
J. Mol. Biol. 264 (5), 1013-1027 (1996)
M:97153337

Choe,J.Y., Poland,B.W., Fromm,H.J. and Honzatko,R.B.
Mechanistic implications from crystalline complexes of wild-type
and mutant adenylosuccinate synthetases from Escherichia coli
Biochemistry 38 (21), 6953-6961 (1999)
M:99278141



Comment:
Oklahoma ID: NGO.398

For other 'pur' genes, see NG0333 (purC), NG0263 (purF), NG0526 (purM), NG0748 (purE), NG0875 (purK), NG1183 (purL), NG1224 (purN), NG1466 (purH), NG1711 (purB), NG1939 (purD)

Blast Summary:  PSI-Blast Search
NG0398 is orthologously related to AE002435, Neisseria meningitidis, strain MC58, a adenylosuccinate synthetase protein: residues 1-434 are 97% similar to residues 1-434 of NG0398.

Numerous significant hits to adenylosuccinate synthetase (adenylosuccinate synthase) in gapped BLAST; e.g. residues 3-434 are 61% similar to gb|AAG08323.1|AE004907_1 adenylosuccinate synthetase of Pseudomonas aeruginosa, residues 3-434 are 59% similar to gb|AAF95743.1| adenylosuccinate synthetase of Vibrio cholerae, residues 3-434 are 58% similar to gb|AAC23278.1| denylosuccinate synthetase of Haemophilus influenzae Rd.

COGS Summary:  COGS Search
BeTs to 12 clades of COG0104
COG name: Adenylosuccinate synthase
Functional Class:  F
The phylogenetic pattern of COG0104 is amtkyqvcebrhuj-------
Number of proteins in this genome belonging to this COG is 1

Blocks Summary:  Blocks Search
***** IPB001114 (Adenylosuccinate synthetase) with a combined E-value of 6e-162.
    IPB001114A    20-57
    IPB001114B    100-120
    IPB001114C    130-155
    IPB001114D    222-260
    IPB001114E    266-285
    IPB001114F    298-339
    IPB001114G    376-408


ProDom Summary:  Protein Domain Search
Residues 402-433 are 81% similar to a (LIGASE ADENYLOSUCCINATE SYNTHETASE) protein domain (PD003550) which is seen in O31047_BBBBB.

Residues 8-398 are 53% similar to a (LIGASE ADENYLOSUCCINATE SYNTHETASE PURINE) protein domain (PD001188) which is seen in PURA_HAEIN.

Residues 8-122 are 38% similar to a (ADENYLOSUCCINATE SYNTHETASE EC 6.3.4.4) protein domain (PD176155) which is seen in PURA_METJA.



Paralogs:  Local Blast Search


NG0398 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.


Pfam Summary:  Pfam Search
Residues 6 to 428 (E-value = 8e-248) place NG0398 in the Adenylsucc_synt family which is described as Adenylosuccinate synthetase (PF00709)

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

PDB Hit:
pdb|1KJX|1KJX-A IMP COMPLEX OF E. COLI ADENYLOSUCCINATE 462.0 0e+00
pdb|1ADE|1ADE-A STRUCTURE OF ADENYLOSUCCINATE SYNTHETASE PH=7 AT460.0 0e+00
pdb|1CG1|1CG1-A STRUCTURE OF THE MUTANT (K16Q) OF 458.0 0e+00
pdb|1CG3|1CG3-A STRU

Gene Protein Sequence:
MAMAKNVVVIGAQWGDEGKGKIVDWLAEEAGGVVRFQGGHNAGHTLVVGG
KKTILRLIPSGILHEGLDCFIGSGVVVSPEALLGEIDELNAAGVKNVEGR
LKIAPTCPLILPYHIALDQAREASRGKGKIGTTGRGIGPAYEDKVARRAI
RAADLLHPEKLREKLDAVLAYYNVQLQYLHNAGPVKAEDVMAVIEKVAPR
IAPMIADVSRVLNEKNKNGEKLLFEGAQGALLDIDYGTYPFVTSSNCLAG
AASAGAGVGPQMLDYVLGIVKAYTTRVGSGPFPTELFDEVGAGLAERGHE
FGSVTGRARRCGWFDAAALKRSIQINGISGMCITKLDVMDGVETINICVG
YELPGGGKTDILPCGSDAVETCKPIYETMPGWRESTVGVKSYDALPANAK
AYLKRIEEVCGAPVAIVSTGPDREETIVLHHPFA

Gene Nucleotide Sequence:  Sequence Viewer
ATGGCTATGGCTAAAAATGTTGTAGTAATCGGCGCACAGTGGGGCGACGA
GGGTAAAGGTAAAATCGTTGACTGGCTGGCGGAAGAAGCCGGCGGCGTCG
TGCGCTTCCAAGGCGGCCACAATGCGGGCCATACCTTGGTCGTCGGCGGC
AAAAAAACCATTTTGCGCCTGATTCCGAGCGGTATCCTGCACGAAGGATT
GGATTGCTTCATCGGTTCGGGCGTTGTCGTTTCCCCCGAAGCCCTGTTGG
GCGAAATCGACGAGTTGAACGCGGCAGGCGTGAAAAACGTCGAAGGCCGT
CTGAAAATCGCGCCGACCTGCCCGCTGATCCTGCCTTACCACATCGCGCT
CGACCAAGCCCGCGAAGCATCGCGCGGCAAAGGCAAAATCGGCACGACCG
GCCGCGGCATCGGCCCTGCCTACGAAGACAAAGTGGCACGCCGCGCCATT
CGCGCCGCCGATTTGCTGCATCCTGAAAAACTGCGTGAAAAACTGGATGC
CGTCCTTGCCTATTACAACGTCCAACTCCAATACCTGCATAACGCCGGAC
CGGTTAAAGCGGAAGACGTGATGGCGGTTATCGAAAAAGTCGCGCCGCGC
ATTGCGCCGATGATTGCCGACGTGTCCCGCGTGTTGAACGAAAAAAACAA
AAACGGCGAAAAACTGCTGTTTGAAGGCGCGCAAGGTGCGTTGTTGGACA
TCGACTACGGCACTTACCCCTTCGTTACCTCGTCCAACTGTCTCGCCGGC
GCGGCTTCGGCAGGCGCGGGCGTAGGTCCTCAAATGCTGGATTATGTTTT
GGGCATCGTCAAAGCCTATACCACGCGCGTCGGTTCGGGCCCGTTCCCGA
CCGAATTGTTCGACGAAGTAGGCGCAGGTTTGGCGGAGCGCGGACACGAA
TTCGGTTCGGTAACCGGCCGCGCGCGCCGCTGCGGCTGGTTTGATGCCGC
CGCCCTGAAACGCTCCATCCAAATCAACGGCATTTCCGGTATGTGCATTA
CCAAACTCGATGTAATGGACGGCGTTGAAACCATCAATATCTGCGTCGGC
TACGAATTGCCAGGCGGCGGCAAAACCGACATCCTGCCTTGCGGTTCGGA
TGCGGTGGAAACCTGCAAACCGATTTACGAAACCATGCCCGGCTGGCGCG
AATCGACTGTCGGCGTGAAAAGCTACGACGCATTGCCTGCCAATGCCAAA
GCATATTTGAAACGGATTGAAGAAGTCTGCGGCGCGCCGGTCGCCATCGT
CTCCACCGGCCCCGACCGCGAAGAAACGATTGTGCTGCATCATCCGTTCG
CA


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