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Chlamydia trachomatis Search Results

Record: 1 of 1  
MiniMap IGR487 IGR483 IGR486 IGR485 IGR484 IGR482 CT590 gp6D, - CT583 trpS, - CT585 eno, - CT587 CT589 rsbU, - CT588 uvrB, - CT586 CT590 gp6D, - CT583 trpS, - CT585 eno, - CT587 CT589 rsbU, - CT588 uvrB, - CT586 CT590 trpS, - CT585 eno, - CT587 CT589 rsbU, - CT588 uvrB, - CT586 CT584 gp6D, - CT583 CT584
* Calculated from Protein Sequence

Gene ID: CT587

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
eno  

Definition:
enolase (phosphopyruvate hydratase) (2-phosphoglycerate dehydratase)

Gene Start:
661850

Gene Stop:
663121

Gene Length:
1272

Molecular Weight*:
45427

pI*:
4.44

Net Charge*:
-21.23

EC:
4.2.1.11  

Functional Class:
energy metabolism; glycolysis and gluconeogenesis  

Pathway: pathway table
Amino Acid Metabolism; Phenylalanine, tyrosine and tryptophan biosynthesis
Carbohydrate Metabolism; Glycolysis / Gluconeogenesis

Comment:
From Prosite PDOC00148:

Enolase (EC 4.2.1.11) is a glycolytic enzyme that catalyzes the dehydration of 2-phospho-D-glycerate to phosphoenolpyruvate. It is a dimeric enzyme that requires magnesium both for catalysis and stabilizing the dimer. Enolase is probably found in all organisms that metabolize sugars. In vertebrates, there are three different tissue-specific isozymes: alpha present in most tissues, beta in muscles and gamma found only in nervous tissues.

Tau-crystallin, one of the major lens proteins in some fish, reptiles and birds, has been shown to be evolutionary related to enolase.

Blast Summary:  PSI-Blast Search
Numerous hits in gapped BLAST to enolases. e.g. residues 6-421 are
58% similar to ENO_BACSU. Residues 6-421 are 55% similar to an enolase of
B.burgdorferi (AE001140). CT587 is also similar to MG407 of M.genitalium.
No similarities to T.pallidum.

CT587 is orthologously related to CPn0800:
residues 1-422 are 73% similar to that of CPN0800.

COGS Summary:  COGS Search
BeTs to 16 clades of COG0148
COG name: Enolase
Functional Class:  G
The phylogenetic pattern of COG0148 is aMtKYqvcebrhujgpolin-
Number of proteins in this genome belonging to this COG is 1


Blocks Summary:  Blocks Search
Residues 36-74, 92-141, 151-200, 143-189, 219-263, 217-261, 277-294,
305-355, 372-410, 341-379 are matched to blocks BL00164A,B,C,D,E,F,G,
concerned with enolase protein sequences, e.g. ENO_MYCPN.
Residues 112-138, 243-297 are matched to blocks BL00908A,B,
concerned with lactonizing enzyme family signa, e.g. RSPA_ECOLI.

ProDom Summary:  Protein Domain Search
Residues 9-409 are 58% similar to an enolase domain from ENO_BACSU.

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

Pfam Summary:  Pfam Search
Residues 5 to 136 (E-value = 2e-56) place CT587 in the Enolase_N family which is described as Enolase, N-terminal domain (PF03952)
Residues 141 to 424 (E-value = 2.8e-145) place CT587 in the Enolase_C family which is described as Enolase, C-terminal TIM barrel domain (PF00113)

Structural Feature(s):
Feature Type  Start  Stop
non-globular  
279  
424

PDB Hit:
gi|1311141|pdb|1PDZ| Mol_id: 1; Molecule: Enolase; Chain: Null; Synonym: 2-Phospho-D-Glycerate Dehydratase; Ec: 4.2.1.11; Heterogen: Phosphoglycolate; Heterogen: Mn 2+

Gene Protein Sequence:
MFDVVISDIEAREILDSRGYPTLCVKVITNTGTFGEACVPSGASTGIKEA
LELRDKDPKRYQGKGVLQAISNVEKVLMPALQGFSVFDQITADAIMIDAD
GTPNKEKLGANAILGVSLALAKAAANTLQRPLYRYLGGSFSHVLPCPMMN
LINGGMHATNGLQFQEFMIRPISAPSLTEAVRMGAEVFNALKKILQNRQL
ATGVGDEGGFAPNLASNAEALDLLLTAIETAGFTPREDISLALDCAASSF
YNTQDKTYDGKSYADQVGILAELCEHYPIDSIEDGLAEEDFEGWKLLSET
LGDRVQLVGDDLFVTNSALIAEGIAQGLANAVLIKPNQIGTLTETAEAIR
LATIQGYATILSHRSGETEDTTIADLAVAFNTGQIKTGSLSRSERIAKYN
RLMAIEEEMGPEALFQDSNPFSKA

Gene Nucleotide Sequence:  Sequence Viewer
ATGTTTGATGTCGTCATCTCCGATATAGAAGCGAGAGAAATTTTAGATTC
TCGAGGCTATCCCACATTATGTGTTAAAGTCATCACTAATACAGGAACCT
TTGGTGAAGCGTGCGTTCCTTCTGGAGCATCTACAGGCATCAAGGAAGCT
TTGGAACTGCGTGACAAAGATCCTAAACGTTACCAAGGGAAAGGGGTCTT
ACAAGCCATTTCTAATGTCGAAAAAGTGCTGATGCCCGCTTTACAAGGAT
TCAGCGTATTTGACCAAATTACAGCTGATGCGATTATGATTGATGCTGAT
GGAACTCCGAACAAAGAAAAGTTAGGAGCTAATGCGATTCTTGGAGTCTC
CCTAGCATTAGCAAAAGCTGCTGCAAATACTTTACAGAGACCTTTATATC
GGTATCTTGGTGGATCTTTCTCGCATGTGCTTCCTTGCCCTATGATGAAT
CTTATCAATGGCGGTATGCATGCTACAAATGGTCTCCAATTCCAAGAATT
TATGATTCGTCCAATTAGCGCTCCTTCTCTAACAGAGGCTGTGCGGATGG
GAGCAGAAGTCTTCAACGCCTTAAAAAAAATCTTACAGAATCGACAGCTG
GCTACAGGTGTTGGTGATGAAGGCGGATTTGCTCCTAATCTTGCCTCTAA
TGCCGAAGCTCTGGATCTACTCTTAACAGCAATCGAAACTGCAGGATTCA
CACCTAGAGAAGATATTTCTTTAGCTCTCGACTGCGCTGCTTCTTCTTTC
TATAATACCCAAGATAAAACCTATGATGGGAAATCGTATGCAGATCAAGT
GGGTATACTTGCAGAACTCTGTGAGCACTATCCTATAGATTCTATCGAAG
ATGGGCTAGCCGAAGAAGATTTTGAGGGCTGGAAACTCCTATCCGAGACT
TTAGGAGATCGTGTGCAACTAGTTGGAGACGACCTATTTGTGACGAATTC
TGCATTGATTGCTGAAGGAATCGCTCAAGGACTTGCCAATGCCGTTCTCA
TCAAACCAAACCAAATTGGAACACTTACAGAAACTGCAGAAGCTATTCGT
TTAGCAACTATACAAGGCTACGCTACCATTCTTTCGCATAGATCAGGAGA
AACAGAAGATACTACCATAGCAGACCTTGCTGTCGCTTTTAATACAGGTC
AGATTAAAACAGGGTCTCTTTCCCGTTCTGAGCGTATCGCTAAGTATAAC
CGTCTAATGGCAATTGAAGAAGAGATGGGTCCAGAAGCTCTATTCCAAGA
TTCAAATCCCTTTTCTAAAGCA


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