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Neisseria gonorrhoeae Search Results

Record: 1 of 1  
MiniMap IGR0518 IGR0519 IGR0521 IGR0515.1 IGR0517 IGR0522 IGR0515 IGR0520 IGR0516 IGR0514 NG0622 NG0616 NG0621 panD, - NG0620 NG0618 kdsA, - NG0619 eno, - NG0617 mfd, - NG0623 NG0615.1 rir2,nrdB, - NG0615 rir1,nrdA, - NG0614 NG0622 NG0616 NG0621 panD, - NG0620 NG0618 kdsA, - NG0619 eno, - NG0617 mfd, - NG0623 NG0615.1 rir2,nrdB, - NG0615 rir1,nrdA, - NG0614 NG0616 NG0621 panD, - NG0620 NG0618 kdsA, - NG0619 eno, - NG0617 mfd, - NG0623 NG0622 NG0615.1 rir2,nrdB, - NG0615 rir1,nrdA, - NG0614
* Calculated from Protein Sequence

Gene ID: NG0617

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
eno  

Definition:
enolase (2-phosphoglycerate dehydratase) (2-phospho-d-glycerate hydro-lyase)

Gene Start:
606218

Gene Stop:
604935

Gene Length:
1284

Molecular Weight*:
46101

pI*:
4.60

Net Charge*:
-19.79

EC:
4.2.1.11  

Functional Class:
Energy metabolism; Glycolysis and gluconeogenesis  

Pathway: pathway table
Glycolysis / Gluconeogenesis
Phenylalanine, tyrosine and tryptophan biosynthesis

Secondary Evidence:
Mahony,T.J. and Miller,D.J. Linkage of genes encoding enolase (eno) and CTP synthase (pyrG) in the beta-subdivision proteobacterium Nitrosomonas europaea. FEMS Microbiol. Lett. 165 (1): 153-157 (1998) [Medline: 98377731].

Py,B., Higgins,C.F., Krisch,H.M. and Carpousis,A.J. A DEAD-box RNA helicase in the Escherichia coli RNA degradosome . Nature 381 (6578): 169-172 (1996) [Medline: 96202365].

Weng,M., Makaroff,C.A. and Zalkin,H. Nucleotide sequence of Escherichia coli pyrG encoding CTP synthetase. J. Biol. Chem. 261 (12): 5568-5574 (1986) [Medline: 86168304].

Comment:
From GenBANK (gi:1706655): This protein is also involved in the RNA degradosome, a multi-enzyme complex important in RNA
processing and messenger RNA degradation. Catalytic activity:
2-phospho-d-glycerate = phosphoenolpyruvate + H2O. Magnesium is required for catalysis and for stabilizing the dimer. Pathway: glycolysis. This protein is a cytoplasmic homodimer, and belongs to the enolase family.

From Medline (96202365): The Escherichia coli RNA degradosome is a multi-enzyme complex that contains the exoribonuclease polynucleotide phosphorylase (PNPase) and the endoribonuclease RNase E. Both enzymes are important in RNA processing and messenger RNA degradation. Enolase and RhlB are two other major components of the degradosome. Enolase is a glycolytic enzyme with an unknown role in RNA metabolism. RhlB is a member of the DEAD-box family of ATP-dependent RNA helicases, which are found in both prokaryotes and eukaryotes. We show that the degradosome has an ATP-dependent activity that aids the degradation of structured RNA by PNPase. Incubation of the degradosome with affinity-purified antibody against RhlB inhibited the ATP-stimulated RNA, suggesting that RhlB acts by unwinding RNA structures that impede the processive activity of PNPase. RhlB is thus an important enzyme in mRNA turnover.

Oklahoma ID: NGO.617c

Blast Summary:  PSI-Blast Search
Numerous significant hits in gapped BLAST to enolases; e.g. residues 1-428 are 67% similar to L29475 of Bacillus subtilis.

Residues 1-428 are 98% similar to NMA1495 and NMB1285, both enolases of N.meningitidis (13124126, 13124130).

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
***** IPB000941 (Enolase) with a combined E-value of 3.4e-191.
    IPB000941A    9-22
    IPB000941B    34-55
    IPB000941C    90-135
    IPB000941D    142-178
    IPB000941E    200-231
    IPB000941F    279-296
    IPB000941G    307-342
    IPB000941H    375-412


ProDom Summary:  Protein Domain Search
Residues 3-421 are 59% similar to a (ENOLASE LYASE GLYCOLYSIS MAGNESIUM) protein domain (PD000902) which is seen in ENO_NITEU.



Paralogs:  Local Blast Search


NG0617 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.


Pfam Summary:  Pfam Search
Residues 3 to 134 (E-value = 2.2e-70) place NG0617 in the Enolase_N family which is described as Enolase, N-terminal domain (PF03952)
Residues 139 to 426 (E-value = 5.7e-171) place NG0617 in the Enolase_C family which is described as Enolase, C-terminal TIM barrel domain (PF00113)

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

PDB Hit:
pdb|1E9I|1E9I-A ENOLASE FROM E.COLI 484.0 0e+00
pdb|1ELS|1ELS ENOLASE (E.C.4.2.1.11) (2-PHOSPHO-D-GLYCERATE 360.0 0e+00
pdb|1EBG|1EBG-A ENOLASE (E.C.4.2.1.11) (2-PHOSPHO-D-GLYCERATE 359.0 0e+00
pdb|1L8P|1L8P-A MG-P

Gene Protein Sequence:
MSAIVDIFAREILDSRGNPTVECDVLLESGVMGRAAVPSGASTGQKEALE
LRDGDKSRYSGKGVLKAVEHVNNQIAQALIGIDANEQSYIDQIMIELDGT
ENKGNLGANATLAVSMAVARAAAEDSGLPLYRYLGGAGPMSLPVPMMNVI
NGGEHANNSLNIQEFMIMPVGAKSFREALRCGAEIFHALKKLCDSKGFPT
TVGDEGGFAPNLNSHKEALQLMVEAAEAAGYKAGEDVLFALDCASSEFYK
DGKYHLEAEGRSYTNAEFAEYLEGLVNEFPIISIEDGMDENDWEGWKLLT
EKLGKKVQLVGDDLFVTNPKILAEGIEKGVANALLVKVNQIGTLSETLKA
VDLAKCNRYASVMSHRSGETEDSTIADLAVATNCMQIKTGSLSRSDRMAK
YNQLLRIEEELAEAAYYPGKAAFYQLGK

Gene Nucleotide Sequence:  Sequence Viewer
ATGAGCGCAATCGTTGATATTTTCGCCCGCGAAATTTTGGACTCACGCGG
CAACCCCACAGTCGAGTGTGATGTATTGCTCGAATCCGGCGTAATGGGAC
GTGCGGCCGTACCGAGCGGCGCATCCACCGGTCAGAAAGAAGCTTTGGAA
CTTCGCGACGGCGACAAATCCCGCTATTCCGGCAAAGGCGTATTGAAGGC
CGTCGAACACGTCAACAACCAAATCGCCCAAGCCCTCATCGGTATCGATG
CCAACGAGCAATCTTATATCGACCAAATCATGATCGAATTGGACGGTACT
GAAAACAAAGGCAATTTGGGTGCGAATGCGACTTTGGCGGTCTCTATGGC
GGTTGCACGCGCCGCTGCCGAAGACTCAGGCCTGCCGCTTTACCGCTACT
TGGGGGGCGCAGGTCCGATGTCCCTGCCCGTACCGATGATGAACGTCATC
AACGGCGGCGAACACGCCAACAACAGCCTGAACATCCAAGAGTTTATGAT
TATGCCCGTCGGCGCAAAATCTTTCCGCGAAGCGTTGCGCTGCGGTGCGG
AAATTTTCCACGCCTTGAAAAAACTGTGCGACAGTAAAGGCTTCCCGACC
ACAGTCGGCGACGAAGGCGGTTTCGCCCCCAACCTGAACAGCCACAAAGA
AGCCCTGCAACTGATGGTCGAAGCGGCCGAAGCCGCCGGCTACAAGGCGG
GCGAAGACGTATTATTCGCATTGGACTGCGCGTCCAGCGAGTTCTACAAA
GACGGCAAATACCACTTGGAAGCCGAAGGCCGCTCCTACACCAACGCGGA
ATTTGCCGAATACTTGGAAGGCTTGGTTAACGAATTCCCGATTATTTCCA
TTGAAGACGGGATGGACGAAAACGACTGGGAAGGCTGGAAACTGCTGACC
GAAAAATTGGGCAAAAAAGTTCAATTGGTCGGCGACGACTTGTTCGTAAC
CAATCCGAAAATTCTTGCCGAAGGCATCGAAAAAGGCGTAGCAAACGCAT
TGCTGGTCAAAGTCAACCAAATCGGTACTTTAAGCGAAACCCTGAAAGCC
GTCGATCTGGCAAAATGCAACCGCTACGCCAGCGTGATGAGCCACCGCTC
CGGCGAAACCGAAGACAGTACCATTGCCGACTTGGCAGTCGCCACCAACT
GTATGCAGATTAAAACCGGTTCTTTGAGCCGTTCCGACCGCATGGCGAAA
TACAACCAACTGCTGCGTATCGAGGAAGAATTGGCGGAAGCCGCCTACTA
CCCCGGCAAAGCCGCATTCTACCAACTGGGCAAA


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