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Chlamydia pneumoniae Search Results

Record: 1 of 1  
MiniMap IGR604 IGR607 IGR603 IGR599 IGR602 IGR605 IGR601 IGR600 IGR606 rs20, - CPn0754 ygfA, - CPn0763 CPn0753 recA, - CPn0762 CPn0764 CPn0761 CPn0760 CPn0755 folP, - CPn0758 rpoD, - CPn0756 rs20, - CPn0754 ygfA, - CPn0763 CPn0753 recA, - CPn0762 CPn0764 CPn0761 CPn0760 CPn0755 folP, - CPn0758 rpoD, - CPn0756 CPn0753 recA, - CPn0762 CPn0764 rs20, - CPn0754 ygfA, - CPn0763 CPn0761 CPn0755 folP, - CPn0758 rpoD, - CPn0756 folX, - CPn0757 folA, - CPn0759 folX, - CPn0757 folA, - CPn0759 CPn0760
* Calculated from Protein Sequence

Gene ID: CPn0758

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
folP  

Definition:
dihydropterin pyrophosphokinase/dihydropteroate synthase

Gene Start:
855110

Gene Stop:
856462

Gene Length:
1353

Molecular Weight*:
49804

pI*:
5.40

Net Charge*:
-9.23

EC:
2.5.1.15  2.7.6.3  

Functional Class:
biosynthesis of cofactors, prosthetic groups and carriers; folate  

Pathway: pathway table
Folate biosynthesis

Comment:
Dihydropteroate synthase catalyzes the condensation of
6-hydroxymethyl-7,8-dihydropteridine pyrophosphate and para-aminobenzoic
acid to form 7,8-dihydropteroate. See CT612, CT614 and CT078.

From Prosite PDOC00631:

All organisms require reduced folate cofactors for the synthesis of a
variety of metabolites. Most microorganisms must synthesize folate de novo
because they lack the active transport system of higher vertebrate cells
which allows these organisms to use dietary folates. Enzymes involved in
folate biosynthesis are therefore targets for a variety of antimicrobial
agents such as trimethoprim or sulfonamides.

7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase (EC 2.7.6.3) (HPPK)
catalyzes the attachment of pyrophosphate to
6-hydroxymethyl-7,8-dihydropterin to form
6-hydroxymethyl-7,8-dihydropteridine pyrophosphate. This is the first step
in a three-step pathway leading to 7,8-dihydrofolate.

Bacterial HPPK (gene folK or sulD) is a protein of 160 to 270 amino acids.
In the lower eukaryote Pneumocystis carinii, HPPK is the central domain of
a multifunctional folate synthesis enzyme (gene fas).

From Prosite PDOC00630:

All organisms require reduced folate cofactors for the synthesis of a
variety of metabolites. Most microorganisms must synthesize folate de novo
because they lack the active transport system of higher vertebrate cells
which allows these organisms to use dietary folates. Enzymes that are
involved in the biosynthesis of folates are therefore the target of a
variety of antimicrobial agents such as trimethoprim or sulfonamides.

Dihydropteroate synthase (EC 2.5.1.15) (DHPS) catalyzes the condensation of
6-hydroxymethyl-7,8-dihydropteridine pyrophosphate to para-aminobenzoic
acid to form 7,8-dihydropteroate. This is the second step in the three
steps pathway leading from 6-hydroxymethyl-7,8-dihydropterin to
7,8-dihydrofolate. DHPS is the target of sulfonamides which are substrates
analog that compete with para-aminobenzoic acid.

Bacterial DHPS (gene sul or folP) is a protein of about 275 to 315 amino
acid residues which is either chromosomally encoded or found on various
antibiotic resistance plasmids. In the lower eukaryote Pneumocystis
carinii, DHPS is the C-terminal domain of a multifunctional folate
synthesis enzyme (gene fas).



Blast Summary:  PSI-Blast Search
CPn0758 is orthologously related to CT613, a predicted dihydropterin pyrophosphokinase/dihydropteroate synthase:
residues 1-443 are 54% similar to CT613. No similarity to T.pallidum,
M.genitalium or U.urealyticum.

COGS Summary:  COGS Search
BeTs to 9 clades of COG0294
COG name: Dihydropteroate synthase
Functional Class:  H
The phylogenetic pattern of COG0294 is amtkyqvCebRHuj----in-
Number of proteins in this genome belonging to this COG is 1

Blocks Summary:  Blocks Search


ProDom Summary:  Protein Domain Search


Paralogs:  Local Blast Search
No paralogs in C.pneumoniae.

Pfam Summary:  Pfam Search
Residues 8 to 142 (E-value = 1.6e-64) place CPn0758 in the HPPK family which is described as 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase (HPPK) (PF01288)
Residues 186 to 401 (E-value = 5.4e-85) place CPn0758 in the Pterin_bind family which is described as Pterin binding enzyme (PF00809)

Structural Feature(s):
Feature Type  Start  Stop
transmembrane  
124  
141

PDB Hit:


Gene Protein Sequence:
MSEPRFVCLSLGSNLGNRFKNLQIARTLLGEQAVLGLRSSVILETEALLL
PGSPPEWDLPYFNSVLVGETTLSLRELLVTIKQIEKVVGRAEESPPWSPR
TIDVDILLYGDESFCCDHTEITIPLSNLLSRPFLIALIASLCPYRRFCTQ
GSPYHNFTFGELAHHLPSPPGMIRRSLSPDTMLMGVVNVTNDSMSDGGMF
LDPEKAVAQAEKLFTEGAAVIDFGAQATNPKVKQFLSVDQEWERLEPVLR
LLKETWSNRKQYPIISLDTFYPEIILRAMDIYPIQWINDVSGGSQSMAEV
ARDCELSLVMNHSSSLPVDPKNILSFSVPIGEQLLSWGEKQLKMFSDVGL
NANQVIFDPGIGFGKGAAQSLATLYEIAKFKRLGCPILIGHSRKSFLSLF
GNHDPKDRDWETVGLSILLQQQGVDYLRVHNVAAHQKALSVAACEACAPI
$

Gene Nucleotide Sequence:  Sequence Viewer
ATGTCCGAGCCCCGTTTTGTCTGCTTAAGTTTAGGATCAAATTTAGGAAA
TCGTTTTAAAAATCTACAGATTGCTCGTACTTTATTAGGCGAACAAGCTG
TTTTAGGTCTACGTAGTTCGGTAATTCTAGAAACAGAAGCCTTGTTATTA
CCGGGATCTCCTCCAGAGTGGGACCTTCCTTATTTTAATTCGGTACTTGT
AGGGGAAACCACCCTATCTTTGCGAGAACTACTGGTTACTATCAAACAGA
TAGAGAAGGTGGTAGGTAGAGCAGAGGAGTCGCCCCCATGGTCTCCTCGA
ACCATAGATGTAGATATTTTGCTTTATGGTGACGAGTCTTTTTGTTGTGA
TCACACCGAGATAACGATTCCTTTGTCCAATTTGTTATCACGTCCTTTTT
TGATTGCTTTAATAGCATCTCTTTGTCCTTATCGTCGATTTTGCACTCAA
GGTTCTCCTTATCACAACTTTACATTTGGAGAGTTGGCGCATCACCTTCC
CTCACCTCCAGGGATGATTCGTAGGAGTTTATCTCCAGATACGATGTTGA
TGGGGGTGGTAAATGTGACTAACGACTCTATGTCTGATGGGGGCATGTTT
TTAGATCCAGAAAAAGCAGTGGCTCAAGCTGAGAAGTTATTTACAGAGGG
CGCTGCAGTTATAGATTTTGGAGCTCAAGCAACAAACCCTAAAGTAAAGC
AGTTTTTATCTGTAGATCAAGAATGGGAGCGTCTGGAGCCTGTTTTAAGG
TTGTTAAAAGAGACTTGGTCCAATAGAAAACAATATCCAATCATCTCTTT
AGATACGTTTTATCCTGAAATTATTCTTAGGGCTATGGATATTTATCCGA
TCCAGTGGATTAATGATGTCTCTGGGGGATCACAGTCTATGGCTGAGGTC
GCTAGGGATTGTGAGCTATCCTTGGTTATGAATCACTCGTCTTCGCTTCC
TGTGGATCCTAAAAATATCTTGTCGTTTTCTGTCCCTATTGGAGAGCAAC
TGTTGAGCTGGGGTGAGAAGCAACTTAAGATGTTTTCTGATGTTGGTCTG
AACGCAAATCAGGTGATTTTTGATCCCGGTATAGGTTTTGGGAAGGGGGC
TGCGCAATCTTTGGCTACTTTGTATGAGATTGCGAAATTTAAGCGTTTGG
GATGCCCTATCCTTATTGGACATTCTCGAAAATCGTTCTTATCTTTATTT
GGTAATCATGATCCCAAGGATCGTGATTGGGAAACCGTAGGTCTATCTAT
ACTCTTACAACAACAAGGTGTGGACTACTTGCGAGTGCATAATGTTGCTG
CTCATCAAAAAGCTTTATCAGTAGCTGCTTGTGAAGCCTGTGCACCCATC
TAA


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