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Neisseria gonorrhoeae Search Results

Record: 1 of 1  
MiniMap IGR0504 IGR0508 IGR0502.2 IGR0502 IGR0502.1 IGR0505 IGR0503 IGR0506 IGR0507 hip,ihfB, - NG0603 NG0601 kcy,mssA,cmk, - NG0605 rsuA,psi, - NG0607 estD, - NG0600 NG0601.1 NG0606 rpS1, - NG0604 mltD, - NG0608 merR, - NG0602 hip,ihfB, - NG0603 NG0601 kcy,mssA,cmk, - NG0605 rsuA,psi, - NG0607 estD, - NG0600 NG0601.1 NG0606 rpS1, - NG0604 mltD, - NG0608 merR, - NG0602 hip,ihfB, - NG0603 kcy,mssA,cmk, - NG0605 rsuA,psi, - NG0607 estD, - NG0600 NG0601.1 NG0606 rpS1, - NG0604 mltD, - NG0608 NG0601 merR, - NG0602
* Calculated from Protein Sequence

Gene ID: NG0605

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
kcy  mssA  cmk  

Definition:
cytidylate kinase (CK) (cytidine monophosphate kinase) (CMP kinase)

Gene Start:
591812

Gene Stop:
591159

Gene Length:
654

Molecular Weight*:
24012

pI*:
9.10

Net Charge*:
2.20

EC:
2.7.4.14  

Functional Class:
Purines, pyrimidines, nucleosides, and nucleotides; Nucleotide and nucleoside interconversions  

Pathway: pathway table
Pyrimidine metabolism

Secondary Evidence:
Fricke,J., Neuhard,J., Kelln,R.A. and Pedersen,S. The cmk gene encoding cytidine monophosphate kinase is located in the rpsA operon and is required for normal replication rate inEscherichia coli. J. Bacteriol. 177 (3): 517-523 (1995) [Medline: 95138007].

Bucurenci,N., Sakamoto,H., Briozzo,P., Palibroda,N., Serina,L., Sarfati,R.S., Labesse,G., Briand,G., Danchin,A., Barzu,O. andGilles,A.M. CMP kinase from Escherichia coli is structurally related to other nucleoside monophosphate kinases. J. Biol. Chem. 271 (5): 2856-2862 (1996) [Medline: 96162036].

Briozzo,P., Golinelli-Pimpaneau,B., Gilles,A.M., Gaucher,J.F., Burlacu-Miron,S., Sakamoto,H., Janin,J. and Barzu,O. Structures of escherichia coli CMP kinase alone and in complex with CDP: a new fold of the nucleoside monophosphate binding domain andinsights into cytosine nucleotide specificity. Structure 6 (12): 1517-1527 (1998) [Medline: 99081882].

Yamanaka,K., Ogura,T., Koonin,E.V., Niki,H. and Hiraga, S. Multicopy suppressors, mssA and mssB, of an smbA mutation of Escherichia coli. Mol. Gen. Genet. 243 (1): 9-16 (1994) [Medline: 94247361].

Schultz,C.P., Ylisastigui-Pons,L., Serina,L., Sakamoto,H., Mantsch,H.H., Neuhard,J., Barzu,O. and Gilles,A.M. Structural and catalytic properties of CMP kinase from Bacillus subtilis: a comparative analysis with the homologous enzyme fromEscherichia coli. Arch. Biochem. Biophys. 340 (1): 144-153 (1997) [Medline: 97271336].

Comment:
From GenBANK (gi:2506790): In E. coli, ATP, dATP, and GTP are equally effective as phosphate donors. CMP and dCMP are the best phosphate acceptors.

From Medline (95138007): A gene encoding CMP kinase, cmk, is located immediately upstream of the gene for ribosomal protein S1, rpsA. In high gene copy number, this gene, mssA, was previously found to suppress defects in smbA, which is now known to be identical to pyrH, encoding UMP kinase. In a strain deleted for cmk, the pools of CMP and dCMP were elevated approximately 30-fold.

From Medline (94247361):We have isolated and characterized two multicopy suppressors, mssA and mssB, which suppress the cold-sensitive growth phenotype of the smbA2 mutant of Escherichia coli. The mssA gene is located immediately upstream of the rpsA gene (20.5 min). MssA protein was found to be related to nucleoside monophosphate kinases. The mssB gene was found to be identical to the deaD gene (69 min), which encodes a putative RNA helicase. The SmbA protein belongs to the aspartokinase family and probably represents a new, fourth aspartokinase species in E. coli. Expression of the smbA gene is essential for cell growth. SmbA may be a regulatory factor in the expression of a battery of genes. MssA and MssB might also relate to the expression of some of these genes. Multiple copies mssA and mssB suppressed the various phenotypic features of the smbA2 mutant to various extents, suppressing the cold-sensitive growth completely.

Oklahoma ID: NGO.605c

Blast Summary:  PSI-Blast Search
Numerous significant hits in gapped BLAST to cytidylate kinases; e.g. residues 1-217 are 48% similar to AE006118 of Pasteurella multocida.

Residues 1-218 are 95% similar to NMB1300 and NMA1514, both cytidylate kinases of N.meningitidis (9973518, 9973515).

COGS Summary:  COGS Search
BeTs to 11 clades of COG0283
COG name: Cytidylate kinase
Functional Class:  F
The phylogenetic pattern of COG0283 is -----qvcebrH--gpolinx
Number of proteins in this genome belonging to this COG is 1

Blocks Summary:  Blocks Search
***** IPB003136 (Cytidylate kinase) with a combined E-value of 3e-87.
    IPB003136A    7-40
    IPB003136B    81-115
    IPB003136C    124-161
    IPB003136D    169-200


ProDom Summary:  Protein Domain Search
Residues 71-217 are 50% similar to a (KINASE CYTIDYLATE CMP CK) protein domain (PD005731) which is seen in KCY_ECOLI.



Paralogs:  Local Blast Search


NG0605 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.


Pfam Summary:  Pfam Search
Residues 60 to 213 (E-value = 8.6e-56) place NG0605 in the Cytidylate_kin family which is described as Cytidylate kinase (PF02224)

Structural Feature(s):
Feature Type  Start  Stop
non-globular  
1  
46

PDB Hit:
pdb|1CKE|1CKE-A CMP KINASE FROM ESCHERICHIA COLI FREE ENZYME 183.0 2e-47
pdb|1KDO|1KDO-A CYTIDINE MONOPHOSPHATE KINASE FROM E. COLI IN 181.0 9e-47
pdb|1CKE|1CKE-A CMP KINASE FROM ESCHERICHIA COLI FREE ENZYME 147.0 2e-36
pdb|1KDO|1KDO-A CYTI

Gene Protein Sequence:
MNRQKVIAIDGPGASGKGTVAARVAAALGYDYLDTGALYRLTALYAQKQG
VEWHDEENVSALAKKLPAVFSGNRILLDGEDVSDGIRTEAIGMGASAVAQ
WPKVRAALLQRQRDFLTEKGLVADGRDTGSVVFPQAELKIFLTAESKIRA
ERRAKQIGIPCEGFTFERILSDIETRDEADRNRKVAPLKQQPDALLLDTS
RLTIEETVKKVLDWYRKV

Gene Nucleotide Sequence:  Sequence Viewer
ATGAACAGACAAAAAGTCATCGCCATCGACGGTCCGGGCGCATCGGGCAA
AGGCACGGTCGCCGCCCGCGTTGCCGCCGCATTGGGATACGATTATCTCG
ATACCGGCGCGCTCTACCGCCTGACCGCCCTATATGCACAAAAACAAGGC
GTGGAATGGCACGATGAAGAAAACGTTTCCGCACTTGCCAAAAAACTGCC
CGCCGTATTTTCAGGCAACCGCATCCTACTTGATGGCGAAGACGTTTCAG
ACGGCATCCGGACAGAAGCCATCGGTATGGGCGCATCCGCAGTTGCGCAA
TGGCCCAAAGTCCGCGCCGCACTGCTGCAACGCCAACGCGATTTTCTGAC
CGAAAAAGGACTGGTTGCCGACGGACGGGACACCGGATCGGTCGTCTTCC
CCCAAGCCGAACTCAAAATTTTTCTGACAGCCGAATCTAAAATCCGTGCC
GAACGCCGCGCCAAACAAATCGGCATTCCCTGCGAAGGTTTCACATTCGA
GCGCATCCTGTCCGACATCGAGACCAGAGACGAAGCAGACCGAAACCGCA
AGGTTGCCCCCCTGAAACAACAGCCCGATGCCCTGCTTTTGGATACGAGC
CGCCTAACTATAGAAGAAACTGTAAAAAAAGTGCTTGATTGGTATCGTAA
AGTT


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