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Neisseria gonorrhoeae Search Results

Record: 1 of 1  
MiniMap IGR0309 IGR0313 IGR0315 IGR0310 IGR0307 IGR0312 IGR0311 IGR0314 IGR0308 NG0378 NG0381 ppiB, - NG0376 pth, - NG0379 NG0371 pgm, - NG0375 NG0377 recB, - NG0370 glnQ, - NG0374 NG0372 NG0378 NG0381 ppiB, - NG0376 pth, - NG0379 NG0371 pgm, - NG0375 NG0377 recB, - NG0370 glnQ, - NG0374 NG0372 NG0378 ppiB, - NG0376 pth, - NG0379 NG0371 pgm, - NG0375 NG0377 recB, - NG0370 NG0380 NG0381 NG0380 glnQ, - NG0374 NG0372 NG0373 NG0373
* Calculated from Protein Sequence

Gene ID: NG0375

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
pgm  

Definition:
phosphoglucomutase (glucose phosphomutase)

Gene Start:
370091

Gene Stop:
368712

Gene Length:
1380

Molecular Weight*:
49425

pI*:
5.00

Net Charge*:
-15.16

EC:
2.7.5.1  5.4.2.2  

Functional Class:
Cell envelope; Surface polysaccharides, lipopolysaccharides and antigens  
Energy metabolism; Sugars  

Pathway: pathway table
Aminosugars metabolism
Erythromycin biosynthesis
Galactose metabolism
Glycolysis / Gluconeogenesis
Pentose phosphate cycle
Starch and sucrose metabolism
Streptomycin biosynthesis

Primary Evidence:
Zhou,D., Stephens,D.S., Gibson,B.W., Engstrom,J.J., McAllister,C.F., Lee,F.K. and Apicella,M.A. 1994. Lipooligosaccharide biosynthesis in pathogenic Neisseria. Cloning,
identification, and characterization of the phosphoglucomutase gene.
J. Biol. Chem. 269 (15): 11162-11169.
Medline: 94209286.

Sandlin,R.C. and Stein,D.C. 1994.
Role of phosphoglucomutase in lipooligosaccharide biosynthesis in Neisseria gonorrhoeae.
J. Bacteriol. 176 (10): 2930-2937.
Medline: 94245620.



Secondary Evidence:
Ward CK, Lumbley SR, Latimer JL, Cope LD, Hansen EJ:
Haemophilus ducreyi secretes a filamentous
hemagglutinin-like protein.
J Bacteriol 1998 Nov;180(22):6013-22
Medline: 99030326

Regni C, Tipton PA, Beamer LJ.
Crystal structure of PMM/PGM: an enzyme in the biosynthetic pathway of P.aeruginosa virulence factors.
Structure (Camb). 2002 Feb;10(2):269-79.
PMID: 11839312

Comment:
Oklahoma ID: NGO.375c

Blast Summary:  PSI-Blast Search
NG0375 is 99% identical to a previously sequenced N.gonhorroeae protein, phosphoglucomutase (glucose phosphomutase), in GenBank, 452116.

NG0375 is orthologously related to AL162754, Neisseria meningitidis, strain Z2491, a phosphoglucomutase protein: residues 1-460 are 94% similar to residues 1-460 of NG0375.

Numerous sigmficant hits in gapped BLAST; e.g. residues 3-454 are 57% similar to gb|AAG08707.1|AE004945_1 phosphomannomutase of Pseudomonas aeruginosa, residues 69-447 are 55% similar to 5714739 phosphoglucomutase of Bordetella bronchiseptica, residues 2-452 are 43% similar to gb|AAF82964.1|AE003869_1 phosphomannomutase of Xylella fastidiosa.

COGS Summary:  COGS Search
BeTs to 17 clades of COG1109
COG name: Phosphomannomutase
Functional Class:  G
The phylogenetic pattern of COG1109 is aMTKYQVCEBRHUJgpOLINx
Number of proteins in this genome belonging to this COG is 2

Blocks Summary:  Blocks Search
No significant hits to the Blocks database.

ProDom Summary:  Protein Domain Search
Residues 325-452 are identical to a (PHOSPHOMANNOMUTASE PROTEIN ISOMERASE PHOSPHORYLATION PMM) protein domain (PD001709) which is seen in PGMU_NEIGO.

Residues 19-125 are 71% similar to a (ISOMERASE PHOSPHOMANNOMUTASE PHOSPHORYLATION) protein domain (PD000667) which is seen in PGMU_NEIME.

Residues 141-324 are 90% similar to a (ISOMERASE PHOSPHORYLATION PHOSPHOMANNOMUTASE) protein domain (PD000778) which is seen in PGMU_NEIME.

Residues 119-167 are identical to a (PHOSPHOGLUCOMUTASE EC 5.4.2.2 GLUCOSE) protein domain (PD038265) which is seen in PGMU_NEIGO.



Paralogs:  Local Blast Search


NG0375 is paralogously related to NG1341 (phosphoglucomutase/phosphomannomutase family) (9e-27).


Pfam Summary:  Pfam Search
Residues 6 to 140 (E-value = 7.5e-45) place NG0375 in the PGM_PMM_I family which is described as Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I (PF02878)
Residues 154 to 254 (E-value = 6.7e-52) place NG0375 in the PGM_PMM_II family which is described as Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II (PF02879)
Residues 256 to 366 (E-value = 1e-48) place NG0375 in the PGM_PMM_III family which is described as Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III (PF02880)
Residues 371 to 454 (E-value = 9.3e-30) place NG0375 in the PGM_PMM_IV family which is described as Phosphoglucomutase/phosphomannomutase, C-terminal domain (PF00408)

Structural Feature(s):
Feature Type  Start  Stop
non-globular  
1  
53
coil-coil  
432  
460

PDB Hit:
pdb|1K2Y|1K2Y-X CRYSTAL STRUCTURE OF 474.0 0e+00
pdb|1K35|1K35-A CRYSTAL STRUCTURE OF 473.0 0e+00
pdb|1C47|1C47-A BINDING DRIVEN STRUCTURAL CHANGES IN CRYSTALINE 63.2 9e-11
pdb|1JDY|1JDY-A RABB

Gene Protein Sequence:
MASITRDIFKAYDIRGIVGKTLTDDAAYFIGRAIAAKAAEKGIARIAIGR
DGRLSGPELMEHIQRGLTDSGIGVLNVGMVTTPMLYFAAVNECGGSGVMI
TGSHNPPDYNGFKMMLGGDTLAGEAIQELLAIVEKDGFVAADKQGSVTEK
DISGAYHDHIVGHVKLKRPINIAIDAGNGVGGAFAGKLYKGLGNEVTELF
CEVDGNFPNHHPDPSKPENLQDLIAALKNGDAEIGLAFDGDADRLGVVTK
DGNIIYPDRQLMLFAQDVLNRNPGAKVIFDVKSTRLLAPWIKEHGGEAIM
EKTGHSFIKSAMKKTGALVAGEMSGHVFFKERWFGFDDGLYAGARLLEIL
SASDNPSEVLDNLPQSISTPELNISLPEGSNGHQVIEELAAKAEFEGATE
IITIDGLRVEFPDGFGLMRASNTTPILVLRFEADTQAAIERIQNRFKAVI
ESNPHLIWPL

Gene Nucleotide Sequence:  Sequence Viewer
ATGGCAAGCATCACCCGCGACATCTTCAAAGCCTACGACATCCGTGGCAT
CGTCGGCAAAACCCTGACCGACGATGCCGCTTATTTCATCGGCAGGGCCA
TCGCCGCCAAAGCCGCCGAAAAAGGTATCGCCCGCATCGCGATCGGACGC
GACGGACGCTTGAGCGGCCCCGAACTGATGGAGCACATCCAACGCGGCCT
GACCGACAGCGGTATCGGCGTACTCAATGTCGGCATGGTTACCACTCCTA
TGCTCTACTTCGCAGCCGTCAACGAATGCGGCGGCAGCGGAGTGATGATT
ACCGGCAGCCACAATCCGCCCGATTACAACGGTTTCAAAATGATGCTCGG
CGGCGACACGCTCGCAGGCGAAGCCATTCAAGAACTTTTAGCTATTGTTG
AGAAAGACGGTTTTGTTGCCGCCGACAAACAAGGCAGCGTAACCGAAAAA
GACATCTCCGGCGCATACCACGACCACATCGTCGGACACGTCAAACTCAA
ACGCCCGATAAACATCGCCATCGACGCGGGCAACGGCGTGGGCGGCGCGT
TTGCCGGCAAACTCTACAAAGGTTTGGGCAACGAAGTGACCGAACTTTTC
TGCGAAGTGGACGGCAATTTCCCTAATCACCACCCTGATCCTTCCAAACC
GGAAAACCTGCAAGATTTGATTGCCGCGCTGAAAAACGGCGATGCCGAAA
TCGGCTTGGCGTTTGACGGCGATGCCGACCGCTTGGGCGTGGTTACCAAA
GACGGCAACATTATTTATCCCGACCGCCAACTGATGCTGTTCGCCCAAGA
CGTTTTGAACCGCAATCCCGGCGCGAAAGTCATTTTCGATGTCAAATCCA
CACGCCTGCTTGCCCCGTGGATTAAAGAACACGGCGGAGAAGCCATAATG
GAAAAAACCGGCCACAGCTTCATCAAATCCGCTATGAAAAAAACCGGTGC
ACTGGTTGCCGGCGAAATGAGCGGACACGTTTTCTTTAAAGAACGCTGGT
TCGGCTTCGACGACGGCCTGTATGCCGGCGCACGCCTCTTGGAAATCCTG
TCCGCCTCCGACAATCCGTCCGAAGTGTTGGACAACCTGCCGCAAAGCAT
TTCCACGCCCGAACTCAACATCTCCCTGCCCGAAGGCAGCAACGGGCATC
AAGTTATCGAAGAACTCGCCGCCAAAGCCGAATTTGAAGGCGCAACCGAA
ATCATCACCATCGACGGCCTGCGCGTTGAATTTCCCGACGGCTTCGGTCT
GATGCGTGCTTCCAATACCACGCCGATTTTGGTGTTGCGTTTTGAAGCGG
ATACGCAAGCAGCCATCGAGCGCATTCAAAACCGATTCAAAGCCGTCATC
GAAAGCAATCCGCATTTAATCTGGCCTCTG


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