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

Neisseria gonorrhoeae Search Results

Record: 1 of 1  
MiniMap IGR0587 IGR0590 IGR0589 IGR0588 IGR0592 IGR0591 NG0703 NG0705 ribB,ribA, - NG0704 hecA, - NG0706 NG0701 hsdS, - NG0699 hsdM, - NG0702 NG0706.2 NG0703 NG0705 ribB,ribA, - NG0704 hecA, - NG0706 NG0701 hsdS, - NG0699 hsdM, - NG0702 NG0706.2 NG0703 NG0705 ribB,ribA, - NG0704 hecA, - NG0706 NG0701 hsdS, - NG0699 hsdM, - NG0702 NG0706.2 NG0700 NG0706.1 NG0700 NG0706.1
* Calculated from Protein Sequence

Gene ID: NG0704

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
ribB  ribA  

Definition:
GTP cyclohydrolase II / 3,4-dihydroxy-2-butanone 4-phosphate synthase

Gene Start:
699091

Gene Stop:
698003

Gene Length:
1089

Molecular Weight*:
39217

pI*:
5.60

Net Charge*:
-9.94

EC:
3.5.4.25  

Functional Class:
Biosynthesis of cofactors, prosthetic groups, and carriers; Riboflavin  

Pathway: pathway table
Riboflavin metabolism

Secondary Evidence:
Richter,G., Fischer,M., Krieger,C., Eberhardt,S., Luttgen,H.,
Gerstenschlager,I. and Bacher,A.
Biosynthesis of riboflavin: characterization of the bifunctional
deaminase-reductase of Escherichia coli and Bacillus subtilis
J. Bacteriol. 179 (6), 2022-2028 (1997)
Medline: 97221604.

Lee,C.Y. and Meighen,E.A. The lux genes in Photobacterium leiognathi are closely linked with genes corresponding in sequence to riboflavin synthesis genes.
Biochem. Biophys. Res. Commun. 186 (2): 690-697 (1992)
[Medline: 92360014].

Comment:
From GenBANK (gi:399537): In E. coli, RibB is involved in riboflavin biosynthesis. In the n-terminal section, RibB belongs to the DHBP synthase family. In the c-terminal section, RibB belongs to the GTP cyclohydrolase II family.

For other riboflavin synthesis proteins, see NG0068, NG0089, NG0257, NG0755.

Oklahoma ID: NGO.704c

Blast Summary:  PSI-Blast Search
Numerous hits in gapped BLAST to GTP cyclohydrolase II / 3,4-dihydroxy-2-butanone 4-phosphate synthases; residues 4-362 are 51% similar to 11348655 of Pseudomonas aeruginosa.

NG0704 is orthologous to AL162755,N. meningitidis Z2491 putative bifunctional 3,4-dihydroxy-2-butanone 4-phosphate synthase/GTP cyclohydrolase II : residues 1-363 have 97% similarity to residues 1-363 in NG0704.

COGS Summary:  COGS Search
BeTs to 12 clades of COG0108
COG name: 3,4-dihydroxy-2-butanone 4-phosphate synthase
Functional Class:  H
The phylogenetic pattern of COG0108 is Amt-yqvcebRhuj----in-
Number of proteins in this genome belonging to this COG is 1

Blocks Summary:  Blocks Search
***** IPB000422 (3,4-Dihydroxy-2-butanone 4-phosphate synthase) with a combined E-value of 5.4e-90.
    IPB000422A    10-57
    IPB000422B    82-93
    IPB000422C    98-109
    IPB000422D    121-171
***** IPB000926 (GTP cyclohydrolase II) with a combined E-value of 2.5e-11.
    IPB000926A    216-243
    IPB000926D    317-345


ProDom Summary:  Protein Domain Search
Residues 204-337 are 31% similar to a (GTP CYCLOHYDROLASE II HYDROLASE) protein domain (PD003336) which is seen in RIBB_PHOPO.

Residues 9-200 are 61% similar to a (GTP CYCLOHYDROLASE SYNTHASE HYDROLASE) protein domain (PD003034) which is seen in GCH2_PHOLE.



Paralogs:  Local Blast Search


NG0704 is paralogously related to NG1134 (GTP cyclohydrolase II) (3e-05).


Pfam Summary:  Pfam Search
Residues 7 to 202 (E-value = 1.6e-122) place NG0704 in the DHBP_synthase family which is described as 3,4-dihydroxy-2-butanone 4-phosphate synthase (PF00926)
Residues 205 to 360 (E-value = 6.9e-09) place NG0704 in the GTP_cyclohydro2 family which is described as GTP cyclohydrolase II (PF00925)

Structural Feature(s):
Feature Type  Start  Stop
transmembrane  
151  
167

PDB Hit:
pdb|1IEZ|1IEZ-A SOLUTION STRUCTURE OF 3,4-DIHYDROXY-2-BUTANONE 213.0 3e-56
pdb|1G57|1G57-A CRYSTAL STRUCTURE OF 3,4-DIHYDROXY-2-BUTANONE 213.0 3e-56
pdb|1K49|1K49-A CRYSTAL STRUCTURE OF 3,4-DIHYDROXY-2-BUTANONE 173.0 5e-44
pdb|1IEZ|1IEZ-A SOLU

Gene Protein Sequence:
MSHISPIPEILADIKAGKMVIITDAEDRENEGDLLMAAQFVTPEAVNFMI
KHARGLVCLPMEGAMVEKLGLPMMTQKNGAQYGTNFTVSIEAAHGITTGI
SAADRALTIQTAVSPTAKPADIVQPGHIFPLRAQKGGVLVRAGHTEAGVD
LAQMNGLIPAAVICEIINDDGTMARMPELMKFAEEHKLKIGTIADLIEYR
SRTESLLEDMGDAPVQTPWGEFQQHVYVDKLSGETHLALVKGTPSADTET
LVRVHEPFSVMDFIQANPRHSWSLPKALERVQQAESGVVILLHHTEDGAS
LLDRTLPKGANQAYKWDSKSYGIGAQILAGLHVKKLRVLGQPSSFTGLTG
FGLEVVGFEEAEK

Gene Nucleotide Sequence:  Sequence Viewer
ATGTCCCATATTTCCCCCATCCCCGAAATCCTAGCCGACATCAAAGCCGG
TAAAATGGTCATCATCACCGATGCCGAAGACCGCGAAAACGAAGGCGACC
TGCTGATGGCGGCGCAATTCGTTACCCCCGAAGCCGTCAACTTTATGATC
AAACACGCGCGCGGCTTAGTCTGCCTGCCTATGGAAGGTGCAATGGTCGA
AAAACTCGGTCTGCCGATGATGACCCAAAAAAACGGCGCGCAATACGGTA
CCAACTTTACCGTTTCCATCGAAGCCGCGCACGGCATTACCACCGGCATT
TCCGCCGCCGACCGCGCCCTGACTATTCAAACCGCCGTTTCCCCGACCGC
CAAACCCGCAGACATCGTCCAACCCGGTCATATCTTCCCGCTTCGCGCCC
AAAAAGGCGGCGTACTCGTCCGTGCCGGACACACCGAAGCCGGCGTCGAC
TTGGCGCAAATGAACGGGCTGATTCCCGCCGCCGTCATCTGCGAAATCAT
CAACGACGACGGCACGATGGCGCGTATGCCCGAACTGATGAAATTCGCCG
AAGAACACAAGCTCAAAATCGGCACGATTGCCGACCTCATCGAATACCGC
AGCCGCACCGAAAGCCTGCTCGAAGATATGGGCGACGCGCCCGTACAAAC
TCCGTGGGGCGAGTTCCAACAACACGTTTACGTCGACAAACTCTCCGGCG
AAACCCACCTCGCCCTCGTCAAAGGCACACCCTCCGCCGACACCGAAACC
CTCGTCCGTGTCCACGAACCCTTCAGCGTGATGGACTTCATCCAAGCCAA
TCCGCGCCATTCCTGGTCGCTGCCCAAAGCCCTTGAGCGCGTCCAACAGG
CCGAAAGCGGCGTCGTCATCCTCCTGCACCACACCGAAGACGGCGCATCC
CTGCTCGACCGCACCCTACCCAAAGGCGCAAACCAAGCCTACAAATGGGA
CAGCAAAAGCTACGGCATCGGCGCGCAAATCCTCGCCGGCCTCCACGTCA
AAAAACTGCGCGTCCTCGGCCAACCGTCATCTTTCACCGGCCTCACCGGC
TTCGGCCTCGAAGTCGTCGGCTTTGAAGAAGCGGAAAAA


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