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Chlamydia trachomatis Search Results

Record: 1 of 1  
MiniMap IGR502 IGR504 IGR503 IGR505 IGR507 IGR506 folX, - CT614 CT610 CT611 CT616 folP, - CT613 rpoD, - CT615 rs20, - CT617 rpoN, - CT609 uvrD, - CT608 folX, - CT614 CT610 CT611 CT616 folP, - CT613 rpoD, - CT615 rs20, - CT617 rpoN, - CT609 uvrD, - CT608 folX, - CT614 CT610 CT611 CT616 folP, - CT613 rpoD, - CT615 folA, - CT612 folA, - CT612 rs20, - CT617 rpoN, - CT609 uvrD, - CT608
* Calculated from Protein Sequence

Gene ID: CT613

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
folP  

Definition:
dihydropterin pyrophosphokinase/dihydropteroate synthase

Gene Start:
693649

Gene Stop:
692300

Gene Length:
1350

Molecular Weight*:
50301

pI*:
5.73

Net Charge*:
-8.02

EC:
2.5.1.15  2.7.6.3  

Functional Class:
cofactor biosynthesis; folate  

Pathway: pathway table
Metabolism of Cofactors, Vitamins, and Other Substances; 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
Hits in gapped BLAST to dihydropteroate synthase sequences,
e.g. residues 7-433 are 29% similar to FAS_PNECA. No similarities to T.pallidum
or M.genitalium.

CT613 is orthologously related to CPn0758: residues 1-444 are 54% similar to CPn0758.

COGS Summary:  COGS Search
BeTs to 7 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
Residues 182-197, 217-251, 264-290, 348-366, 385-398, 424-433 are
matched to blocks BL00792A,B,C,D,E,F, concerned with dihydropteroate
synthase protein sequences. Examples of sequences represented by
these blocks are DHP2_ECOLI, FAS_YEAST.
Residues 7-26, 52-92, 103-140 are matched to blocks BL00794A,B,C,
concerned with 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase
proteins,e.g. FAS_PNECA.

ProDom Summary:  Protein Domain Search
Residues 7-140 are 37% similar to a HPPK Folic synthase domain represented by FAS_PNECA.
Residues 182-363 are 31% similar to a dihydropteroate synthase domain
represented by DHPS_NEIME.

Paralogs:  Local Blast Search
No evidence of paralogs in C.trachomatis.

Pfam Summary:  Pfam Search
Residues 8 to 141 (E-value = 6.2e-75) place CT613 in the HPPK family which is described as 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase (HPPK) (PF01288)
Residues 185 to 402 (E-value = 1.3e-85) place CT613 in the Pterin_bind family which is described as Pterin binding enzyme (PF00809)

PDB Hit:
gi|3212431|pdb|1AJ0| Crystal Structure Of A Ternary Complex Of E. Coli Dihydropteroate Synthase Antibiotic, Resistance, Transferase, Folate, Biosynthesis, Synthase Mol_id: 1; Molecule: Dihydropteroate Synthase; Chain: Null; Synonym: Dhps; Ec: 2.5.1.15; B

Gene Protein Sequence:
MTSWNFVCLSLGSNLGNRHEHIRRAYASLKKAGIRNLKSSVILETKALLL
EGAPKEWDLPYFNSVVIGETQLSPDELIEEIKMIESRFGQDASLKWGPRP
IDIDVLFYGDEAFSYHSDKCTIPHPKVLERPFLLSMIASLCPYRRFRLEG
SSCNGKTFAELAAIYPLTEEDALGSFGSATQIMGIVNITDNSISDTGLFL
EARRAAAHAERLFAEGASIIDLGAQATNPRVKDLGSVEQEWERLEPVLRL
LAERWGAAQQCPDVSIDTFRPEIIRRAVEVFPIRWINDVSGGSLEMAHLA
KEFGLRLLINHSCSLPPRPDCVLSYEESPIEQMLRWGESQLEQFAQVGLD
TSWQVVFDPGIGFGKTPVQSMLLMDGVKQFKRVLECPVLIGHSRKSCLSM
LGRFNSNDRDWETIGCSVSLHDRGVDYLRVHQVEGNRRALAAAAWAGMFV


Gene Nucleotide Sequence:  Sequence Viewer
ATGACTAGTTGGAATTTTGTTTGTTTAAGTTTGGGTTCCAATTTAGGTAA
CCGGCATGAGCATATAAGACGCGCTTATGCAAGTTTAAAGAAGGCTGGGA
TCCGAAATTTAAAAAGTTCTGTGATTTTAGAGACGAAGGCTTTGTTGTTA
GAAGGGGCTCCGAAAGAATGGGATCTTCCTTATTTTAACTCTGTGGTTAT
TGGGGAAACGCAGCTATCTCCAGACGAGTTGATTGAAGAAATCAAGATGA
TAGAAAGTCGTTTTGGACAAGATGCTTCTTTGAAATGGGGGCCTCGACCG
ATTGATATTGATGTGCTTTTCTATGGAGACGAAGCTTTTTCTTATCATAG
TGACAAATGTACAATCCCACATCCTAAGGTATTAGAAAGACCTTTTCTTC
TTTCTATGATAGCTTCTTTATGTCCGTATCGTCGTTTCCGTTTGGAAGGA
TCTTCTTGTAATGGGAAAACGTTTGCAGAGCTTGCTGCTATTTATCCATT
GACGGAGGAGGATGCGTTAGGCAGTTTCGGTTCTGCTACCCAAATTATGG
GTATTGTTAATATTACGGATAACTCGATCTCCGATACAGGATTGTTTCTG
GAGGCGAGAAGAGCCGCAGCCCATGCTGAGAGACTCTTTGCAGAAGGAGC
TTCTATTATTGATTTAGGGGCGCAAGCAACCAATCCTCGTGTAAAAGATT
TAGGAAGCGTAGAACAAGAGTGGGAGCGTCTAGAACCTGTTTTGCGTTTA
TTAGCGGAGCGGTGGGGGGCTGCTCAACAATGCCCTGATGTATCTATCGA
TACATTTCGTCCAGAGATTATTCGACGAGCTGTTGAAGTATTTCCGATTC
GTTGGATCAATGATGTTTCTGGAGGCTCTTTGGAAATGGCTCATTTGGCG
AAGGAGTTTGGGCTACGGCTATTAATAAATCATTCGTGTTCGCTGCCTCC
AAGACCAGATTGTGTACTTTCTTATGAAGAATCTCCTATTGAGCAAATGT
TGCGTTGGGGAGAGTCTCAGTTAGAACAATTTGCTCAAGTAGGTTTAGAT
ACAAGTTGGCAAGTTGTTTTCGATCCAGGAATAGGATTTGGGAAGACTCC
CGTTCAGTCGATGTTATTGATGGATGGAGTAAAGCAGTTTAAACGTGTTT
TAGAGTGTCCTGTATTAATAGGCCATTCTAGAAAATCGTGTTTGAGTATG
TTGGGCCGATTTAATAGTAACGATCGTGATTGGGAAACGATCGGCTGTTC
TGTATCTCTTCATGATCGAGGAGTTGATTATCTACGCGTGCATCAGGTTG
AAGGTAACAGACGTGCCTTAGCCGCTGCTGCTTGGGCTGGTATGTTTGTA



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