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Haemophilus ducreyi Search Results

Record: 1 of 1  
MiniMap IGR1359 IGR1356 IGR1363 IGR1357 IGR1360 IGR1358 IGR1361 IGR1362 HD1852 nagB, - HD1847 nanA, - HD1850 HD1856 wecA,rfe, - HD1844 wecB,rffE, - HD1843 nagA, - HD1845 HD1854 menD, - HD1853 HD1852 nagB, - HD1847 nanA, - HD1850 HD1856 wecA,rfe, - HD1844 wecB,rffE, - HD1843 nagA, - HD1845 HD1854 menD, - HD1853 HD1852 nagB, - HD1847 nanA, - HD1850 HD1856 wecA,rfe, - HD1844 wecB,rffE, - HD1843 nagA, - HD1845 nanA, - HD1849 nanA, - HD1849 HD1854 menD, - HD1853
* Calculated from Protein Sequence

Gene ID: HD1850

DNA Molecule Name:
1  

Genbank ID:
0

Gene Name:
nanA  

Definition:
N-acetylneuraminate lyase

Gene Start:
1554817

Gene Stop:
1554008

Gene Length:
810

Molecular Weight*:
29684

pI*:
5.30

Net Charge*:
-4.32

EC:
4.1.3.3  

Functional Class:
Energy metabolism; Sugars  

Pathway: pathway table
Aminosugars metabolism

Secondary Evidence:
Kruger D, Schauer R, Traving C.
Characterization and mutagenesis of the recombinant N-acetylneuraminate lyase from Clostridium perfringens: insights into the reaction mechanism.
Eur J Biochem. 2001 Jul;268(13):3831-9.
PMID: 11432751

Barbosa JA, Smith BJ, DeGori R, Ooi HC, Marcuccio SM, Campi EM, Jackson WR, Brossmer R, Sommer M, Lawrence MC.
Active site modulation in the N-acetylneuraminate lyase sub-family as revealed by the structure of the inhibitor-complexed Haemophilus influenzae enzyme.
J Mol Biol. 2000 Oct 27;303(3):405-21.
PMID: 11031117

Comment:


Blast Summary:  PSI-Blast Search
Numerous significant hits in gapped BLAST to nanA proteins; e.g., residues 1-266 are 86% similar to residues 1-266 of HPL_HAEIN; residues 2-266 are 75% similar to residues 27-291 of the N-acetylneuraminate lyase protein in Trichomonas vaginalis; residues 4-266 are 69% similar to residues 1-263 of sialic acid lyase (N-acetylneuraminate lyase) in Clostridium perfringens; and residues 3-258 are 38% similar to residues 3-259 of HPL_ECOLI. There are also significant hits (though not as strong as those listed above) to dihydrodipicolinate synthase proteins (EC 4.2.1.52); e.g., residues 4-266 are 27% similar to residues 3-269 of DAPA_METTH and residues 2-266 are 26% similar to residues 2-266 of DAPA_BACSU (vegetative protein 81).

COGS Summary:  COGS Search
BeTs to 13 clades of COG0329
COG name: Dihydrodipicolinate synthetase/N-acetylneuraminate lyase
Functional Class: E,M
The phylogenetic pattern of COG0329 is amtk-qvcEBrHuj----inx
Number of proteins in this genome belonging to this COG is 2

Blocks Summary:  Blocks Search
***** IPB002220 (Dihydrodipicolinate synthetase) with a combined E-value of 2.5e-51.
    IPB002220A    10-22
    IPB002220B    38-59
    IPB002220C    78-125
    IPB002220D    132-143
    IPB002220E    181-195
    IPB002220F    200-213
    IPB002220G    238-262


ProDom Summary:  Protein Domain Search
Residues 19-99 are 88% similar to a (SYNTHASE DIHYDRODIPICOLINATE LYASE BIOSYNTHESIS) protein domain (PD001859) which is seen in Q9CKB0_PASMU.

Residues 106-266 are 87% similar to a (SYNTHASE DIHYDRODIPICOLINATE LYASE) protein domain (PD213669) which is seen in NPL_HAEIN.

Residues 2-37 are 80% similar to a (LYASE N-ACETYLNEURAMINIC ACID) protein domain (PD385694) which is seen in Q27818_TRIVA.



Paralogs:  Local Blast Search
HD1850 is paralogously related to HD1107 (2e-19).


Pfam Summary:  Pfam Search
Residues 3 to 269 (E-value = 3.2e-117) place HD1850 in the DHDPS family which is described as Dihydrodipicolinate synthetase family (PF00701)

PDB Hit:
pdb|1F6P|A Chain A, Crystal Structure Analysis Of N-Acetylneura... 479 2e-136
pdb|1FDZ|A Chain A, N-Acetylneuraminate Lyase In Complex With P... 197 1e-051
pdb|1NAL|1 Chain 1, Mol_id: 1; Molecule: N-Acetylneuraminate Ly... 197 1e-051

Gene Protein Sequence:
MKNLTGIFSALLVAFNEDGSINERGLRQIVRYNIDKMKVDGLYVGGSTGE
NFMLSTSEKKEIFRIVKDEVRDQIALIAQVGSVNVQEAVELGKYSTELGY
DCLSAVTPFYYKFSFPEIKHYYDTIIAETGNKMIVYSIPFLTGVNIGVEQ
FGALYQNPNIIGVKFTAGDFYLLERIKKAYPNHLIWAGFDEMMVPAVALG
VDGAIGSTFNVNGLRARQIFDAVKSGKLAQALQIQHVTNDLIEGILANGL
YLTIKELLKLEGVEAGVLS$

Gene Nucleotide Sequence:  Sequence Viewer
ATGAAAAATTTAACCGGTATTTTCAGTGCGTTATTGGTTGCTTTTAATGA
AGATGGTTCGATTAATGAACGCGGGTTACGCCAAATCGTACGTTATAATA
TTGATAAAATGAAAGTAGATGGTTTATATGTTGGCGGTTCAACGGGTGAA
AATTTTATGCTTTCAACTTCGGAGAAAAAAGAAATTTTCCGTATTGTTAA
AGATGAGGTTAGAGATCAAATTGCGTTAATTGCTCAAGTGGGAAGCGTGA
ATGTACAAGAAGCGGTTGAATTAGGTAAATATTCGACTGAATTGGGTTAT
GATTGCCTTTCTGCCGTCACACCGTTTTACTATAAATTTAGTTTCCCTGA
GATTAAACATTACTATGATACCATTATTGCTGAAACCGGTAATAAAATGA
TTGTTTATTCCATTCCCTTTTTAACCGGAGTAAATATTGGGGTGGAGCAA
TTTGGTGCGCTTTATCAAAATCCTAATATTATCGGCGTCAAATTTACAGC
CGGTGATTTTTATTTACTTGAGCGGATTAAAAAAGCTTATCCAAATCATT
TAATTTGGGCAGGTTTTGATGAAATGATGGTGCCTGCGGTTGCTTTAGGG
GTAGATGGTGCAATTGGTTCAACATTTAATGTGAATGGGCTTCGTGCGCG
TCAGATCTTTGACGCCGTTAAATCAGGTAAATTAGCGCAGGCGCTACAAA
TTCAACACGTGACCAATGATTTAATTGAGGGTATTTTAGCAAATGGTTTA
TACCTCACTATTAAAGAATTACTCAAACTTGAGGGCGTTGAGGCGGGGGT
ATTGTCGTGA


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