Basic Search | Intermediate Search | Advanced SQL Search | Gene Image Map |  Home

Neisseria gonorrhoeae Search Results

Record: 1 of 1  
MiniMap IGR1534 IGR1542 IGR1537 IGR1541 IGR1539 IGR1535 IGR1536 IGR1538 IGR1540 IGR1543 NG1872 pyrI, - NG1876 def, - NG1871 NG1875 pryB, - NG1877 fmt, - NG1870 fmu, - NG1869 hydH,atoS, - NG1867 NG1874 NG1878 NG1873 NG1872 pyrI, - NG1876 def, - NG1871 NG1875 pryB, - NG1877 fmt, - NG1870 fmu, - NG1869 hydH,atoS, - NG1867 NG1874 NG1878 NG1873 Type: tandem, Name:  - 86 pyrI, - NG1876 def, - NG1871 NG1875 pryB, - NG1877 fmt, - NG1870 fmu, - NG1869 hydH,atoS, - NG1867 NG1868 NG1868 NG1872 NG1874 NG1878 NG1873
* Calculated from Protein Sequence

Gene ID: NG1871

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
def  

Definition:
polypeptide deformylase

Gene Start:
1843038

Gene Stop:
1842496

Gene Length:
543

Molecular Weight*:
20978

pI*:
9.20

Net Charge*:
4.12

EC:
3.5.1.31  

Functional Class:
Translation; Protein modification and translation factors  

Pathway: pathway table
Glyoxylate and dicarboxylate metabolism
Methionine metabolism

Secondary Evidence:
Hao,B., Gong,W., Rajagopalan,P.T., Zhou,Y., Pei,D. and Chan,M.K.
Structural basis for the design of antibiotics targeting peptide
deformylase
Biochemistry 38 (15), 4712-4719 (1999)
Medline: 99218079

Becker,A., Schlichting,I., Kabsch,W., Schultz,S. and Wagner,A.F.
Structure of peptide deformylase and identification of the
substrate binding site
J. Biol. Chem. 273 (19), 11413-11416 (1998)
Medline: 98234316

Becker,A., Schlichting,I., Kabsch,W., Groche,D., Schultz,S. and
Wagner,A.F.
Iron center, substrate recognition and mechanism of peptide
deformylase
Nat. Struct. Biol. 5 (12), 1053-1058 (1998)
Medline: 99061332

Chan,M.K., Gong,W., Rajagopalan,P.T., Hao,B., Tsai,C.M. and Pei,D.
Crystal structure of the Escherichia coli peptide deformylase
Biochemistry 36 (45), 13904-13909 (1997)
Medline: 98042282

Meinnel,T. and Blanquet,S.
Enzymatic properties of Escherichia coli peptide deformylase
J. Bacteriol. 177 (7), 1883-1887 (1995)
Medline: 95204359

Mazel,D., Pochet,S. and Marliere,P.
Genetic characterization of polypeptide deformylase, a distinctive
enzyme of eubacterial translation
EMBO J. 13 (4), 914-923 (1994)
Medline: 94155856

Meinnel,T., Guillon,J.M., Mechulam,Y. and Blanquet,S.
The Escherichia coli fmt gene, encoding methionyl-tRNA(fMet)
formyltransferase, escapes metabolic control
J. Bacteriol. 175 (4), 993-1000 (1993)
Medline: 93163064

Guillon,J.M., Mechulam,Y., Schmitter,J.M., Blanquet,S. and Fayat,G.
Disruption of the gene for Met-tRNA(fMet) formyltransferase
severely impairs growth of Escherichia coli
J. Bacteriol. 174 (13), 4294-4301 (1992)
Medline: 92325012



Comment:
Oklahoma ID: NGO.1871c

Blast Summary:  PSI-Blast Search
Numerous significant hits in gapped BLAST; e.g. residues 15-178 are 58% similar to gb|AAG03409.1|AE004441_10 (AE004441) polypeptide deformylase of Pseudomonas aeruginosa.

Residues 15-181 are 98% similar to emb|CAB83478.1| (AL162752) polypeptide deformylase of Neisseria meningitidis Z2491.




COGS Summary:  COGS Search
BeTs to 12 clades of COG0242
COG name: N-formylmethionyl-tRNA deformylase
Functional Class:  J
The phylogenetic pattern of COG0242 is -----qvceBrhujgpolinx
Number of proteins in this genome belonging to this COG is 1

Blocks Summary:  Blocks Search
***** IPB000181 (Formylmethionine deformylase) with a combined E-value of 5.6e-59.
    IPB000181A    35-75
    IPB000181B    87-102
    IPB000181C    115-161


ProDom Summary:  Protein Domain Search
Residues 20-157 are 60% similar to a (DEFORMYLASE PROTEIN POLYPEPTIDE PDF) protein domain (PD003844) which is seen in DEF_ECOLI.



Paralogs:  Local Blast Search


NG1871 is paralogously related to NG1872 (hypothetical protein) (3e-06).


Pfam Summary:  Pfam Search
Residues 17 to 167 (E-value = 1.4e-75) place NG1871 in the Pep_deformylase family which is described as Polypeptide deformylase (PF01327)

Structural Feature(s):
Feature Type  Start  Stop
uncleavable N-terminal sequence N-terminal sequence  
1  
32

PDB Hit:
pdb|1LRY|1LRY-A CRYSTAL STRUCTURE OF P. AERUGINOSA PEPTIDE 199.0 2e-52
pdb|1BS4|1BS4-A PEPTIDE DEFORMYLASE AS ZN2+ CONTAINING FORM 195.0 4e-51
pdb|1DFF|1DFF PEPTIDE DEFORMYLASE 195.0 4e-51
pdb|2DEF|2DEF PEPTI

Gene Protein Sequence:
MKNRRRIRRRKEKIMALLNILQYPDERLHTVAKPVEQVDERIRKLVADMF
ETMYESRGIGLAATQVDVHERVVVMDLTEDRSEPRVFINPVIVEKDGETT
YEEGCLSVPGIYDAVTRAERVKVEALNEKGEKFTLEADGLLAICVQHELD
HLMGIVFVERLSQLKQGRIKTKLKKRQKHTI

Gene Nucleotide Sequence:  Sequence Viewer
ATGAAAAACAGGCGGCGTATCCGCCGAAGGAAAGAGAAAATTATGGCTTT
ACTGAATATCTTGCAATATCCCGACGAGCGTCTGCACACGGTGGCAAAGC
CTGTCGAACAAGTTGACGAGCGCATCCGGAAGCTGGTTGCCGATATGTTT
GAAACGATGTACGAATCGCGCGGCATCGGGCTGGCGGCGACGCAGGTCGA
TGTGCACGAACGCGTGGTCGTGATGGATTTGACCGAAGACCGCAGCGAAC
CGCGCGTGTTCATCAACCCCGTCATCGTTGAAAAAGACGGCGAAACCACT
TACGAAGAGGGCTGCCTGTCCGTACCGGGCATTTACGACGCCGTTACCCG
CGCCGAACGCGTCAAGGTCGAGGCTTTGAACGAAAAAGGCGAAAAATTCA
CGCTGGAGGCGGACGGGCTGCTGGCGATTTGCGTGCAGCACGAGTTAGAT
CACCTGATGGGCATCGTGTTTGTCGAACGCCTTTCCCAACTCAAGCAGGG
GCGGATTAAGACCAAACTGAAAAAACGTCAGAAACATACGATT


Los Alamos National Laboratory     
Operated by the University of California for the National Nuclear Security Administration,
of the US Department of Energy.     Copyright © 2001 UC | Disclaimer/Privacy