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Neisseria gonorrhoeae Search Results

Record: 1 of 1  
MiniMap IGR0518 IGR0519 IGR0521 IGR0515.1 IGR0517 IGR0523 IGR0522 IGR0515 IGR0520 IGR0516 IGR0514 NG0622 NG0616 NG0621 panD, - NG0620 NG0618 kdsA, - NG0619 eno, - NG0617 mfd, - NG0623 NG0615.1 rir2,nrdB, - NG0615 acdV, - NG0624 NG0622 NG0616 NG0621 panD, - NG0620 NG0618 kdsA, - NG0619 eno, - NG0617 mfd, - NG0623 NG0615.1 rir2,nrdB, - NG0615 acdV, - NG0624 NG0616 NG0621 panD, - NG0620 NG0618 kdsA, - NG0619 eno, - NG0617 mfd, - NG0623 NG0622 NG0615.1 rir2,nrdB, - NG0615 acdV, - NG0624
* Calculated from Protein Sequence

Gene ID: NG0620

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
panD  

Definition:
aspartate 1-decarboxylase (aspartate alpha-decarboxylase)

Gene Start:
607967

Gene Stop:
607587

Gene Length:
381

Molecular Weight*:
13728

pI*:
5.70

Net Charge*:
-2.38

EC:
4.1.1.11  

Functional Class:
Biosynthesis of cofactors, prosthetic groups, and carriers; Pantothenate  

Pathway: pathway table
Alanine and aspartate metabolism
beta-Alanine metabolism

Secondary Evidence:
Ramjee,M.K., Genschel,U., Abell,C. and Smith,A.G.
Escherichia coli L-aspartate-alpha-decarboxylase: preprotein processing and observation of reaction intermediates by electrospray mass spectrometry.
Biochem. J. 323 (Pt 3): 661-669 (1997)
[Medline: 97270610].

Albert,A., Dhanaraj,V., Genschel,U., Khan,G., Ramjee,M.K., Pulido,R., Sibanda,B.L., von Delft,F., Witty,M., Blundell,T.L., Smith,A.G. and Abell,C.
Crystal structure of aspartate decarboxylase at 2.2 A resolution provides evidence for an ester in protein self-processing.
Nat. Struct. Biol. 5 (4): 289-293 (1998)
[Medline: 98206295].

Comment:
For other 'pan' genes, see NG0437 (panC), NG0436 (panB).

From GenBANK (gi:1709570): Catalytic activity: L-aspartate = beta-alanine + CO(2), requiring a cofactor, a pyruvoyl group; this reaction is involved in pantothenate biosynthesis.

Oklahoma ID: NGO.620c

Blast Summary:  PSI-Blast Search
Numerous significant hits in gapped BLAST to aspartate 1-decarboxylases; e.g. residues 1-127 are 66% similar to Z99115 of Bacillus subtilis.

Residues 1-127 are 97% similar to NMB1282, and are 96% similar to NMA1492, both aspartate 1-decarboxylases of N.meningitidis (11280004, 11280003).

COGS Summary:  COGS Search
BeTs to 7 clades of COG0853
COG name: Aspartate 1-decarboxylase
Functional Class:  H
The phylogenetic pattern of COG0853 is -----qvcebr-uj-------
Number of proteins in this genome belonging to this COG is 1

Blocks Summary:  Blocks Search
***** IPB003190 (Aspartate decarboxylase) with a combined E-value of 1.6e-72.
    IPB003190A    5-37
    IPB003190B    51-105


ProDom Summary:  Protein Domain Search
Residues 1-117 are 69% similar to a (ASPARTATE 1-DECARBOXYLASE PRECURSOR) protein domain (PD009294) which is seen in PAND_BACSU.



Paralogs:  Local Blast Search


NG0620 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.


Pfam Summary:  Pfam Search
Residues 1 to 116 (E-value = 9.3e-78) place NG0620 in the Asp_decarbox family which is described as Aspartate decarboxylase (PF02261)

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

PDB Hit:
pdb|1AW8|1AW8-B PYRUVOYL DEPENDENT ASPARTATE DECARBOXYLASE 87.8 8e-19
pdb|1AW8|1AW8-A PYRUVOYL DEPENDENT ASPARTATE DECARBOXYLASE 49.3 3e-07

Gene Protein Sequence:
MFRTILGGKIHRATVTEADLNYVGSITVDQDLLDAAGICPNEKVAIVNNN
NGERFETYTIAGKRGSGVICLNGAAARLVQKGDIVIIMSYIQLSEPEIAA
HEPKVVLVDGNNKIRDIISYEPPHTVL

Gene Nucleotide Sequence:  Sequence Viewer
ATGTTCCGTACTATACTTGGCGGAAAAATCCACCGCGCCACCGTAACCGA
AGCCGATTTAAACTACGTCGGCAGCATTACCGTCGATCAAGACCTGTTAG
ACGCGGCAGGCATCTGCCCCAACGAAAAAGTCGCCATCGTCAACAACAAC
AACGGCGAACGTTTTGAAACCTATACCATTGCAGGGAAACGCGGCAGCGG
CGTGATTTGCCTGAACGGTGCTGCAGCCAGGCTGGTACAGAAAGGCGACA
TCGTCATCATTATGTCTTATATCCAACTTTCCGAACCGGAAATCGCCGCA
CACGAACCCAAAGTCGTCTTAGTGGACGGAAACAATAAAATCCGCGACAT
CATCTCCTACGAGCCGCCGCACACCGTACTG


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