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

Neisseria gonorrhoeae Search Results

Record: 1 of 1  
MiniMap IGR0224 IGR0222 IGR0223 IGR0225 IGR0219 IGR0220 IGR0221 IGR0218 IGR0218.1 IGR0218.2 NG0268 folI, - NG0267 greB, - NG0262 trpF, - NG0261 glnQ, - NG0269 tpc, - NG0265 folC, - NG0266 purF, - NG0263 lbpA, - NG0260.1 era, - NG0260 lbpA, - NG0260.2 NG0268 folI, - NG0267 greB, - NG0262 trpF, - NG0261 glnQ, - NG0269 tpc, - NG0265 folC, - NG0266 purF, - NG0263 lbpA, - NG0260.1 era, - NG0260 lbpA, - NG0260.2 folI, - NG0267 greB, - NG0262 trpF, - NG0261 glnQ, - NG0269 tpc, - NG0265 folC, - NG0266 purF, - NG0263 NG0264 NG0264 NG0268 lbpA, - NG0260.1 era, - NG0260 lbpA, - NG0260.2
* Calculated from Protein Sequence

Gene ID: NG0263

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
purF  

Definition:
amidophosphoribosyltransferase (glutamine phosphoribosylpyrophosphate amidotransferase)

Gene Start:
263409

Gene Stop:
261868

Gene Length:
1542

Molecular Weight*:
55980

pI*:
6.40

Net Charge*:
-4.87

EC:
2.4.2.14  

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

Pathway: pathway table
Glutamate metabolism
Purine metabolism

Secondary Evidence:
Sampei,G. and Mizobuchi,K. 1988. Nucleotide sequence of the Escherichia coli purF gene encoding amidophosphoribosyltransferase for de novo purine nucleotide synthesis. Nucleic Acids Res. 16 (17): 8717. Medline: 88335626.
Tso,J.Y., Hermodson,M.A. and Zalkin,H. 1982. Glutamine phosphoribosylpyrophosphate amidotransferase from cloned
Escherichia coli purF. NH2-terminal amino acid sequence,
identification of the glutamine site, and trace metal analysis. J. Biol. Chem. 257 (7): 3532-3536. Medline: 82142517.


Comment:
Oklahoma ID: NGO.263c

For other 'pur' genes, see NG0333 (purC), NG0398 (purA), NG0526 (purM), NG0748 (purE), NG0875 (purK), NG1183 (purL), NG1224 (purN), NG1466 (purH), NG1711 (purB), NG1939 (purD).

Blast Summary:  PSI-Blast Search
NG0263 is orthologously related to AE002423, Neisseria meningitidis, strain MC58, a amidophosphoribosyltransferase protein: residues 1-514 are 97% similar to residues 1-514 of NG0263.

Numerous significant hits to amidophosphoribosyltransferase (glutamine phosphoribosylpyrophosphate amidotransferase) in gapped BLAST; e.g. residues 1-484 are 59% similar to dbj|BAB36619.1| amidophosphoribosyltransferase of Escherichia coli O157:H7, residues 1-489 are 56% similar to gb|AAF94165.1| midophosphoribosyltransferase of Vibrio cholerae, residues 1-495 are 56% similar to 7716501 amidophosphoribosyltransferase of Pasteurella multocida.

COGS Summary:  COGS Search
BeTs to 11 clades of COG0034
COG name: Glutamine phosphoribosylpyrophosphate amidotransferase
Functional Class:  F
The phylogenetic pattern of COG0034 is amtkyqvcebrh---------
Number of proteins in this genome belonging to this COG is 1

Blocks Summary:  Blocks Search
***** IPB000583 (Glutamine amidotransferase class-II) with a combined E-value of 2.3e-20.
    IPB000583A    24-34
    IPB000583B    69-78
    IPB000583C    101-129
    IPB000583D    337-352
    IPB000583C    166-194


ProDom Summary:  Protein Domain Search
Residues 1-178 are 51% similar to a (AMIDOTRANSFERASE GLUTAMINE ASPARAGINE SYNTHETASE) protein domain (PD000635) which is seen in PUR1_SCHPO.

Residues 352-397 are 67% similar to a (TRANSFERASE GLYCOSYLTRANSFERASE) protein domain (PD000249) which is seen in PUR1_METJA.

Residues 401-473 are 52% similar to a (TRANSFERASE GLYCOSYLTRANSFERASE) protein domain (PD002836) which is seen in PUR1_ECOLI.

Residues 189-348 are 57% similar to a (TRANSFERASE GLYCOSYLTRANSFERASE) protein domain (PD002872) which is seen in PUR1_ECOLI.



Paralogs:  Local Blast Search


NG0263 is paralogously related to NG2045 (glucosamine--fructose-6-phosphate aminotransferase (GlmS)) (3e-13).


Pfam Summary:  Pfam Search
Residues 2 to 138 (E-value = 3.1e-52) place NG0263 in the GATase_2 family which is described as Glutamine amidotransferases class-II (PF00310)
Residues 269 to 416 (E-value = 5.2e-10) place NG0263 in the Pribosyltran family which is described as Phosphoribosyl transferase domain (PF00156)

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

PDB Hit:
pdb|1ECB|1ECB-A ESCHERICHIA COLI GLUTAMINE 552.0 0e+00
pdb|1AO0|1AO0-A GLUTAMINE PHOSPHORIBOSYLPYROPHOSPHATE (PRPP) 294.0 3e-80
pdb|1GPH|1GPH-1 GLUTAMINE PHOSPHORIBOSYLPYROPHOSPHATE (PRPP) 294.0 3e-80
pdb|1GDO|1GDO-A GLUT

Gene Protein Sequence:
MCGVLGLVSHEPVNQLLYDGLQMLQHRGQDAAGIATAEGGTFHMHKGKGM
VSEVFRTRNMRDLTGNAGIAHVRYPTAGNAGSSAEAQPFYVSSPFGIVLA
HNGNLTNTAELYENVCNKHLRHINTGSDSEVLLNVFAHELRREVSKNADP
HRLNADNIFNAVAEVHRLVRGAYGVVAMIAGYGMLAFRDPYGIRPLALGS
QTDSEGRKSYAVASESVAFNALAYDLERDIRPGEAVFVGFNGTIIARQCS
DRAKLSPCLFEYVYFARPDSVIDGVSVYQSRLDMGVSLAEKIKRELPVDG
IDVVMPIPDTSRPSAMELAVHLNKPYREGLIKNRYIGRTFIMPGQSTRKK
SVRQKLSPMETEFAGKSVLLVDDSIVRGTTSREIVEMVRAAGARKVYIAS
AAPEVRYPNVYGIDMPTREELIANGRSAAEIAAEIGADGIVFQDLGDLEA
VVKALNPKIESFDSSCFNGIYRTGDIDDAYLDRLSAEKSGCAGLKIHPSR
MEHSISISDAGDEE

Gene Nucleotide Sequence:  Sequence Viewer
ATGTGCGGCGTATTAGGTTTGGTCAGTCATGAACCCGTGAACCAGCTTCT
GTACGACGGTTTGCAGATGTTGCAGCACAGGGGGCAGGATGCGGCGGGCA
TTGCAACGGCGGAAGGCGGTACCTTCCATATGCACAAAGGCAAAGGGATG
GTGAGCGAAGTGTTCCGCACGCGCAATATGCGCGATTTGACCGGCAACGC
CGGCATCGCCCACGTCCGTTATCCCACGGCGGGCAACGCCGGCAGCAGCG
CGGAGGCGCAGCCTTTCTACGTCAGCTCGCCTTTCGGCATCGTTTTGGCG
CACAACGGCAACCTCACCAACACTGCCGAACTGTATGAAAACGTGTGTAA
CAAACACCTGCGCCACATCAACACCGGCTCCGATTCCGAAGTTTTGCTCA
ACGTATTCGCGCACGAATTGCGCCGCGAAGTCTCTAAAAACGCCGACCCG
CACCGGCTCAATGCCGACAATATTTTCAACGCCGTTGCCGAAGTCCACCG
CCTAGTGCGCGGTGCATACGGCGTGGTTGCCATGATTGCGGGCTACGGTA
TGCTCGCCTTCCGCGACCCTTACGGCATCCGCCCGCTGGCATTGGGTTCG
CAAACCGACAGCGAAGGCAGGAAATCCTATGCCGTCGCCTCCGAATCCGT
CGCCTTCAATGCGCTTGCCTACGATTTGGAACGCGATATCCGGCCGGGCG
AAGCGGTATTTGTCGGCTTTAACGGCACAATCATCGCCCGACAATGCAGC
GACCGTGCCAAACTCAGCCCCTGCCTTTTTGAATATGTTTATTTTGCCCG
CCCCGACTCTGTGATTGACGGTGTATCGGTTTACCAATCGCGCTTGGATA
TGGGCGTGTCCTTGGCGGAAAAAATCAAACGCGAGCTGCCCGTGGACGGC
ATCGACGTCGTGATGCCCATTCCCGATACCAGCCGCCCCAGTGCAATGGA
GCTTGCCGTCCACCTCAACAAACCCTACCGCGAGGGTTTGATTAAAAACC
GCTATATCGGCCGCACCTTTATTATGCCCGGTCAGTCGACGCGCAAAAAA
TCCGTGCGCCAAAAACTCAGCCCGATGGAAACCGAATTTGCAGGCAAAAG
CGTGTTGCTGGTGGACGACTCCATCGTGCGCGGGACGACCAGCCGCGAAA
TCGTCGAAATGGTACGCGCGGCGGGCGCGCGCAAAGTCTATATCGCCTCC
GCCGCGCCCGAAGTGCGCTATCCCAATGTGTACGGCATCGATATGCCCAC
GCGCGAAGAGTTGATTGCCAACGGGCGCAGCGCGGCGGAAATCGCCGCCG
AAATCGGCGCGGACGGCATCGTGTTTCAAGACTTGGGCGATTTGGAAGCC
GTCGTCAAAGCACTCAACCCGAAAATCGAATCCTTCGATTCGTCCTGTTT
CAACGGCATTTATCGGACCGGCGACATCGATGATGCCTACCTCGACCGCC
TGTCTGCCGAGAAATCCGGCTGCGCCGGTCTGAAAATCCACCCGAGCAGG
ATGGAACACAGCATCAGCATCAGCGATGCGGGCGACGAAGAA


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