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

Neisseria gonorrhoeae Search Results

Record: 1 of 1  
MiniMap tRNA-Phe-1 IGR1308 IGR1312 IGR1313.1 IGR1311 IGR1316 IGR1310 IGR1314 IGR1315 IGR1317 IGR1313 IGR1309 NG1614 NG1608 NG1607 yhbG, - NG1605 NG1612 kpsF, - NG1609 NG1615 NG1604 NG1610.1 mtgA, - NG1603 yadB, - NG1611 tal, - NG1610 NG1613 NG1614 NG1608 NG1607 yhbG, - NG1605 NG1612 kpsF, - NG1609 NG1615 NG1604 NG1610.1 mtgA, - NG1603 yadB, - NG1611 tal, - NG1610 NG1613 yhbG, - NG1605 NG1612 kpsF, - NG1609 NG1615 NG1606 NG1607 NG1614 NG1606 NG1608 NG1610.1 mtgA, - NG1603 yadB, - NG1611 tal, - NG1610 NG1613 NG1604
* Calculated from Protein Sequence

Gene ID: NG1610

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
tal  

Definition:
transaldolase

Gene Start:
1579426

Gene Stop:
1580478

Gene Length:
1053

Molecular Weight*:
37489

pI*:
5.30

Net Charge*:
-5.92

EC:
2.2.1.2  

Functional Class:
Energy metabolism; Pentose phosphate pathway  

Pathway: pathway table
Pentose phosphate cycle

Secondary Evidence:
Jia,J., Huang,W., Schorken,U., Sahm,H., Sprenger,G.A., Lindqvist,Y.and Schneider,G.
Crystal structure of transaldolase B from Escherichia coli suggests a circular permutation of the alpha/beta barrel within the class I aldolase family
Structure 4 (6), 715-724 (1996)
Medline: 96399717

Sprenger,G.A., Schorken,U., Sprenger,G. and Sahm,H.
Transaldolase B of Escherichia coli K-12: cloning of its gene,
talB, and characterization of the enzyme from recombinant strains
J. Bacteriol. 177 (20), 5930-5936 (1995)
Medline: 96011384


Comment:
Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.

Oklahoma ID: NGO.1610

Blast Summary:  PSI-Blast Search
Residues 1-351 are 95% similar to transaldolase in Neisseria
meningitidis group A strain Z2491 (11354184|).

Numerous hits in gapped BLAST to transaldolase sequences, e.g.residues 4-350 are 40% similar to transaldolase in Nostoc sp. PCC 7120 (988292|).Residues 23-169 are 31% similar to transaldolase in Escherichia coli (7433626|).

COGS Summary:  COGS Search
BeTs to 10 clades of COG0176
COG name: Transaldolase
Functional Class:  G
The phylogenetic pattern of COG0176 is -m--YqvcEbrhuj----in-
Number of proteins in this genome belonging to this COG is 1

Blocks Summary:  Blocks Search
***** IPB001585 (Transaldolase) with a combined E-value of 2.5e-29.
    IPB001585A    32-47
    IPB001585B    101-123
    IPB001585C    135-148
    IPB001585D    155-190
    IPB001585E    254-282
    IPB001585F    323-346


ProDom Summary:  Protein Domain Search
Residues 4-148 are 41% similar to a (TRANSALDOLASE TRANSFERASE PENTOSE SHUNT MULTIGENE FAMILY) protein domain (PD003490) which is seen in TAL_ANASP.

Residues 149-347 are 41% similar to a (TRANSALDOLASE TRANSFERASE PENTOSE SHUNT DIHYDROXYACETONE) protein domain (PD009632) which is seen in O04894_SOLTU.



Paralogs:  Local Blast Search


NG1610 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.


Pfam Summary:  Pfam Search
Residues 13 to 350 (E-value = 4.2e-73) place NG1610 in the Transaldolase family which is described as Transaldolase (PF00923)

Structural Feature(s):
Feature Type  Start  Stop
coil-coil  
300  
351

PDB Hit:
pdb|1I2P|1I2P-A CRYSTAL STRUCTURE OF ESCHERICHIA COLI 50.0 6e-07
pdb|1ONR|1ONR-A STRUCTURE OF TRANSALDOLASE B 50.0 6e-07
pdb|1I2R|1I2R-A CRYSTAL STRUCTURE OF ESCHERICHIA COLI 50.0 6e-07
pdb|1I2N|1I2N-A CRYS

Gene Protein Sequence:
MTILSDVKALGQQIWLDNLSRSLVQSGELAQMLKQGVCGVTSNPAIFQKA
FAGDALYADEVAALKRQNLSPKQRYETMAVADVRAACDVCLAEHESTGGK
TGFVSLEVSPELAKDAQGTVEEARRLHAAIARKNAMIKVPATDAGIDALE
TLVSDGISVNLTLLFSRAQTLKAYAAYARGIAKRLAAGQSVAHIQVVASF
FISRVDSALDATLPDRLKGKTAIALAKAAYQDWEQYFTAPEFAALEAQGA
NRVQLLWASTGVKNPAYPDTLYVDSLIGVHTVNTVPDATLKAFIDHGTAK
ATLTESADEARARLAEIAALGIDVETLAARLQEDGLKQFEEAFEKLLAPL
V

Gene Nucleotide Sequence:  Sequence Viewer
ATGACTATTTTATCGGACGTTAAAGCATTAGGACAACAAATCTGGCTGGA
CAACCTTTCCCGCTCGCTCGTGCAAAGCGGCGAATTGGCGCAAATGCTCA
AACAAGGCGTGTGCGGCGTAACTTCCAATCCCGCCATTTTCCAAAAAGCC
TTCGCCGGCGACGCGCTTTATGCCGACGAGGTCGCCGCCCTCAAGCGGCA
AAACCTCAGCCCCAAACAACGCTACGAAACCATGGCGGTTGCCGACGTAC
GGGCAGCCTGCGACGTTTGCCTTGCCGAACACGAATCCACCGGCGGCAAA
ACCGGTTTCGTCAGTCTCGAAGTTTCTCCCGAACTTGCCAAAGACGCTCA
AGGCACGGTAGAAGAAGCCCGCCGCCTCCATGCCGCCATCGCGCGTAAAA
ACGCCATGATTAAAGTGCCTGCCACCGACGCAGGCATCGATGCGCTCGAA
ACCCTCGTTTCAGACGGCATCAGCGTGAACCTGACCCTGCTGTTCTCACG
CGCCCAAACCCTCAAAGCCTACGCCGCCTACGCGCGCGGCATTGCCAAAC
GCTTGGCAGCCGGACAAAGCGTTGCCCATATCCAAGTTGTCGCCAGCTTC
TTCATCTCGCGCGTGGACAGTGCGCTGGATGCAACGCTGCCCGACCGGCT
CAAAGGCAAAACCGCCATCGCCCTTGCCAAAGCCGCCTATCAAGATTGGG
AACAATATTTCACCGCCCCCGAATTTGCCGCACTGGAAGCCCAAGGCGCA
AACCGCGTGCAGCTTTTATGGGCATCTACCGGCGTGAAAAACCCAGCCTA
TCCCGACACGCTCTACGTTGACAGCCTGATCGGCGTGCACACCGTCAACA
CCGTCCCCGATGCCACGCTCAAAGCCTTTATCGACCACGGCACGGCGAAA
GCGACGCTGACCGAAAGCGCGGACGAAGCACGGGCGCGGCTCGCCGAAAT
TGCCGCGCTCGGCATCGATGTCGAAACCTTGGCGGCGCGTTTGCAGGAAG
ACGGTTTGAAACAGTTTGAAGAAGCCTTTGAAAAACTGCTCGCGCCTTTG
GTT


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