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Neisseria gonorrhoeae Search Results

Record: 1 of 1  
MiniMap tRNA-Leu-3 IGR0920 IGR0919 IGR0915 IGR0913 IGR0911 IGR0917 IGR0914 IGR0912 IGR0916 IGR0918 NG1139 NG1135 NG1138 tspB, - NG1140 NG1125 NG1127 NG1132 NG1129 NG1124 NG1131 NG1128 NG1133 NG1126 pivNG, - NG1137 NG1130 NG1139 NG1135 NG1138 tspB, - NG1140 NG1125 NG1127 NG1132 NG1129 NG1124 NG1131 NG1128 NG1133 NG1126 pivNG, - NG1137 NG1130 Type: inverse, Name:  - 145 Type: inverse, Name:  - 150 Type: inverse, Name:  - 139 Type: inverse, Name:  - 175 Type: direct, Name:  - 100 Type: inverse, Name:  - 149 Type: inverse, Name:  - 141 Type: direct, Name:  - 136 Type: direct, Name:  - 103 Type: inverse, Name:  - 146 Type: direct, Name:  - 135 Type: direct, Name:  - 127 Type: direct, Name:  - 125 NG1139 NG1135 NG1138 tspB, - NG1140 NG1131 NG1128 NG1133 NG1126 pivNG, - NG1137 NG1130 epsJ, - NG1136 gch2, - NG1134 epsJ, - NG1136 gch2, - NG1134 NG1127 NG1132 NG1129 NG1124 NG1125
* Calculated from Protein Sequence

Gene ID: NG1134

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
gch2  

Definition:
GTP cyclohydrolase II

Gene Start:
1079236

Gene Stop:
1079832

Gene Length:
597

Molecular Weight*:
22098

pI*:
5.90

Net Charge*:
-4.55

EC:
3.5.4.25  

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

Pathway: pathway table
Riboflavin metabolism

Secondary Evidence:
Richter,G., Ritz,H., Katzenmeier,G., Volk,R., Kohnle,A.,Lottspeich,F., Allendorf,D. and Bacher,A.
Biosynthesis of riboflavin: cloning, sequencing, mapping, and expression of the gene coding for GTP cyclohydrolase II inEscherichia coli.
J. Bacteriol. 175 (13): 4045-4051 (1993)
[Medline: 93308083].

Comment:
From GenBANK (gi:232153): In E. coli, this protein catalyzes the reaction: GTP + 3 H2O = formate + 2,5-diamino-6-hydroxy-4- (5-phosphoribosylamino )pyrimidine + pyrophosphate, requiring magnesium. This is involved in thr first step of riboflavin biosynthesis. Gch2 belongs to the GTP cyclohydrolase II family.

Oklahoma ID: NGO.1134

Blast Summary:  PSI-Blast Search
Numerous significant hits in gapped BLAST to GTP cyclohydrolase II; e.g. residues 7-199 in NG1134 have 60% similarity to residues 3-196 in X67876, E. coli GTP cyclohydrolase II.

Residues 3-199 in NG1134 have 96% similarity to residues 1-197 in AE002473, N. meningitidis MC58 GTP cyclohydrolase II.

COGS Summary:  COGS Search
BeTs to 10 clades of COG0807
COG name: GTP cyclohydrolase II
Functional Class:  H
The phylogenetic pattern of COG0807 is a---yqvcebRhUJ----in-
Number of proteins in this genome belonging to this COG is 1

Blocks Summary:  Blocks Search
***** IPB000926 (GTP cyclohydrolase II) with a combined E-value of 2.3e-83.
    IPB000926A    16-43
    IPB000926B    52-74
    IPB000926C    94-128
    IPB000926D    129-157
    IPB000926E    185-195


ProDom Summary:  Protein Domain Search
Residues 10-149 are 60% similar to a (GTP CYCLOHYDROLASE II HYDROLASE) protein domain (PD003336) which is seen in GCH2_ECOLI.

Residues 150-195 are 69% similar to a (GTP CYCLOHYDROLASE HYDROLASE II) protein domain (PD153000) which is seen in GCH2_HAEIN.



Paralogs:  Local Blast Search


NG1134 is paralogously related to NG0704 (GTP cyclohydrolase II / 3,4-dihydroxy-2-butanone 4-phosphate synthase) (2e-05).


Pfam Summary:  Pfam Search
Residues 5 to 174 (E-value = 4.9e-101) place NG1134 in the GTP_cyclohydro2 family which is described as GTP cyclohydrolase II (PF00925)

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

PDB Hit:
No hits to the PDB database.

Gene Protein Sequence:
MKMSELLDHVASCRLPTEWGVFTMHGFEEANGQEHVALTVGNCSDGNPVL
TRIHSECLTGDALFSRKCDCGPQLEAAMRAVQAEGRGIIVYLRQEGRGIG
LINKIRAYHLQEQGMDTVEANLALGLPVDARDFRLAQSIYEYLGIRSVKL
LTNNPEKIQTLKDAGINVVERIPLHVGENLENERYLQTKADKLGHLMSE

Gene Nucleotide Sequence:  Sequence Viewer
ATGAAAATGTCTGAATTATTAGACCATGTCGCTTCCTGCCGTCTGCCGAC
CGAATGGGGCGTATTTACGATGCACGGTTTTGAAGAGGCAAACGGGCAGG
AACACGTCGCGCTGACCGTCGGCAATTGTTCAGACGGCAATCCGGTGTTG
ACGCGCATCCACTCCGAATGTCTGACGGGCGACGCGCTGTTCTCGAGAAA
ATGCGACTGCGGACCGCAACTTGAAGCGGCAATGAGGGCGGTACAGGCAG
AGGGGCGCGGCATCATCGTCTATCTGCGTCAGGAAGGACGCGGCATCGGG
CTGATTAACAAAATCCGCGCCTATCATCTGCAAGAACAAGGTATGGATAC
CGTTGAAGCCAATTTGGCACTCGGGCTGCCCGTCGATGCCCGCGATTTCC
GTTTGGCGCAATCTATCTACGAATATCTGGGCATCCGCTCGGTCAAACTG
TTGACCAACAACCCCGAAAAAATCCAAACCCTGAAAGATGCGGGGATTAA
CGTGGTCGAACGCATTCCCCTGCACGTCGGGGAAAATCTGGAAAACGAGC
GTTATCTCCAAACCAAAGCAGACAAGCTGGGGCATTTGATGTCGGAA


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