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

Neisseria gonorrhoeae Search Results

Record: 1 of 1  
MiniMap IGR1234 IGR1235 IGR1231 IGR1233 IGR1232 IGR1236 IGR1237.1 IGR1237 IGR1238 dpj, - NG1507 recO, - NG1509 pdxJ, - NG1508 mutT, - NG1506 NG1512 NG1504 bcr, - NG1511 pilS, - NG1512.1 opa,P.II, - NG1513 dpj, - NG1507 recO, - NG1509 pdxJ, - NG1508 mutT, - NG1506 NG1512 NG1504 bcr, - NG1511 pilS, - NG1512.1 opa,P.II, - NG1513 Type: tandem, Name:  - 70 Type: inverse, Name:  - 168 Type: inverse, Name:  - 180 dpj, - NG1507 recO, - NG1509 pdxJ, - NG1508 mutT, - NG1506 NG1512 NG1504 bcr, - NG1511 NG1505 pheA, - NG1510 NG1505 pheA, - NG1510 pilS, - NG1512.1 opa,P.II, - NG1513
* Calculated from Protein Sequence

Gene ID: NG1510

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
pheA  

Definition:
bifunctional P-protein:chorismate mutase; prephenate dehydratase

Gene Start:
1478178

Gene Stop:
1477054

Gene Length:
1125

Molecular Weight*:
40810

pI*:
5.80

Net Charge*:
-8.41

EC:
4.2.1.51  5.4.99.5  

Functional Class:
Amino acid biosynthesis; Aromatic amino acid family  

Pathway: pathway table
Phenylalanine, tyrosine and tryptophan biosynthesis

Primary Evidence:
Mehr,I.J. and Seifert,H.S.,
Differential roles of homologous recombination pathways in
Neisseria gonorrhoeae pilin antigenic variation, DNA
transformation and DNA repair,
Mol. Microbiol. 30 (4), 697-710 (1998)

Secondary Evidence:
Gavini,N. and Davidson,B.E.
pheAo mutants of Escherichia coli have a defective pheA attenuator
The journal of biological chemistry. 265 (35), 21532-21535 (1990)
M:91072346

Zurawski,G., Brown,K., Killingly,D. and Yanofsky,C.
Nucleotide sequence of the leader region of the phenylalanine
operon of Escherichia coli
Proceedings of the National Academy of Sciences of the United
States of America. 75 (9), 4271-4275 (1978)
M: 79033820

Lee,A.Y., Karplus,P.A., Ganem,B. and Clardy,J.
Atomic structure of the buried catalytic pocket of Escherichia
coli chorismate mutase
J. Am. Chem. Soc. 117, 3627-3628 (1995)

Zhang,S., Pohnert,G., Kongsaeree,P., Wilson,D.B., Clardy,J. and
Ganem,B.
Chorismate mutase-prephenate dehydratase from Escherichia coli.
Study of catalytic and regulatory domains using genetically engineered proteins
The Journal of biological chemistry. 273 (11), 6248-6253 (1998)
M:98165805

Husain A, Chen S, Wilson DB, Ganem B.
A selective inhibitor of Escherichia coli prephenate dehydratase.
Bioorg Med Chem Lett. 2001 Sep;11(18):2485-8.
PMID: 11549452

Zhang S, Wilson DB, Ganem B.
Probing the catalytic mechanism of prephenate dehydratase by site-directed mutagenesis of the Escherichia coli P-protein dehydratase domain.
Biochemistry. 2000 Apr;39(16):4722-8.
PMID: 10769128

Pohnert G, Zhang S, Husain A, Wilson DB, Ganem B.
Regulation of phenylalanine biosynthesis. Studies on the mechanism of phenylalanine binding and feedback inhibition in the Escherichia coli P-protein.
Biochemistry. 1999 Sep;38(38):12212-7.
PMID: 10493788

Baldwin GS, Davidson BE.
Kinetic studies on the mechanism of chorismate mutase/prephenate dehydratase from Escherichia coli K12.
Biochim Biophys Acta. 1983 Jan;742(2):374-83.
PMID: 6337635

Comment:
Oklahoma ID: NGO.1510c

For other 'phe' genes, see NG0299 (pheS) and NG0304 (pheT).

Blast Summary:  PSI-Blast Search
NG1510 is 100% identical to a previously sequenced N.gonorrhoeae protein in GenBank, 4105530. See also 8134631.

Residues 1-375 in NG1510 have 98% similarity to residues 1-375 in AL162757, N. meningitidis Z2491 chorismate mutase.

Residues 26-375 in NG1510 have 49% similarity to residues 11-365 in AF038578, P. stutzeri chorismate mutase/prephenate dehydratase.

COGS Summary:  COGS Search
BeTs to 10 clades of COG0077
COG name: Prephenate dehydratase
Functional Class:  E
The phylogenetic pattern of COG0077 is amt-yqvcebrh---------
Number of proteins in this genome belonging to this COG is 1

Blocks Summary:  Blocks Search
***** IPB001086 (Prephenate dehydratase (PDT)) with a combined E-value of 1.2e-92.
    IPB001086A    105-117
    IPB001086B    148-169
    IPB001086C    178-189
    IPB001086D    199-216
    IPB001086E    247-280
    IPB001086F    292-344
***** IPB002701 (Chorismate mutase) with a combined E-value of 9.3e-15.
    IPB002701    22-54


ProDom Summary:  Protein Domain Search
Residues 26-103 are identical to a (CHORISMATE INCLUDES: MUTASE CM) protein domain (PD005194) which is seen in Q9ZHY3_NEIGO.

Residues 105-375 are identical to a (PHENYLALANINE BIOSYNTHESIS DEHYDRATASE PREPHENATE) protein domain (PD002231) which is seen in Q9ZHY3_NEIGO.

Residues 1-25 are identical to a (PHEA) protein domain (PD198108) which is seen in Q9ZHY3_NEIGO.



Paralogs:  Local Blast Search


NG1510 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.


Pfam Summary:  Pfam Search
Residues 18 to 101 (E-value = 3.9e-13) place NG1510 in the Chorismate_mut family which is described as Chorismate mutase (PF01817)
Residues 105 to 285 (E-value = 7.3e-71) place NG1510 in the PDT family which is described as Prephenate dehydratase (PF00800)
Residues 293 to 369 (E-value = 1.1e-11) place NG1510 in the ACT family which is described as ACT domain (PF01842)

Structural Feature(s):
Feature Type  Start  Stop
transmembrane  
166  
182

PDB Hit:
No hits to the PDB database.

Gene Protein Sequence:
MLECTANYRSGEIMSQTIDELLIPHRNAIDTIDAEILRLLNERAQHAHAI
GELKGTGAVYRPEREVAVLRRIQDLNKGPLPDESVARLFREVMSECLAVE
RPLTIAYLGPQGTFTQQAAIKHFGHAAHTMACPTIDDCFKQVETRQADYL
VAPVENSTEGSVGRTLDLLAVTALQACGEVVLRIHHNLLRKNNGSTEGIA
KVFSHAQALAQCNDWLGRRLPNAERIAVSSNAEAARLVAESDDGTVAAIA
GRTAAEIYGLDMVAECIEDEPNNTTRFLVMGHHETGASGSDKTSLAVSAP
NRAGAVASLLQPLTESGISMTKFESRPSKSVLWEYLFFIDIEGHRRDAQI
QTALERLGERASFVKAIGSYPTAVL

Gene Nucleotide Sequence:  Sequence Viewer
ATGTTAGAATGCACGGCAAATTACCGTTCAGGCGAAATTATGTCCCAAAC
TATCGACGAACTCCTCATCCCGCACCGCAACGCCATCGACACCATCGATG
CCGAAATTCTGCGCCTGCTCAACGAACGCGCGCAACATGCCCACGCCATC
GGCGAGCTGAAAGGCACGGGCGCGGTGTACCGCCCCGAACGCGAGGTTGC
CGTGTTGCGCCGCATTCAGGATTTGAACAAAGGCCCGCTGCCCGACGAAT
CGGTAGCACGCCTGTTTCGGGAAGTGATGAGCGAGTGCCTCGCCGTCGAA
CGTCCGCTGACCATCGCCTATCTGGGGCCGCAGGGCACGTTTACCCAACA
GGCGGCAATCAAGCATTTCGGACACGCCGCGCATACAATGGCGTGTCCGA
CCATAGACGACTGCTTCAAACAGGTTGAAACCCGTCAGGCGGATTATCTG
GTCGCGCCCGTGGAAAACTCGACCGAAGGCTCGGTCGGGCGCACATTGGA
TTTGCTTGCCGTTACCGCGTTGCAGGCGTGCGGCGAAGTCGTTTTGCGCA
TCCACCACAACCTGTTGCGCAAAAACAACGGCAGCACCGAGGGTATCGCC
AAAGTATTTTCGCACGCGCAGGCGTTGGCGCAGTGCAACGACTGGTTGGG
CAGGCGTCTGCCCAATGCCGAACGGATTGCCGTGTCCAGCAATGCCGAAG
CCGCAAGGCTGGTTGCCGAATCGGACGACGGTACGGTTGCCGCCATCGCC
GGACGCACGGCGGCGGAAATTTACGGACTCGATATGGTTGCCGAGTGCAT
CGAAGACGAACCGAACAACACCACGCGCTTTCTGGTCATGGGACATCACG
AAACCGGTGCAAGCGGCAGCGACAAAACCTCGCTGGCCGTTTCCGCGCCC
AACCGCGCCGGCGCGGTTGCCTCGCTGCTGCAACCGCTGACCGAATCGGG
TATTTCCATGACCAAGTTTGAGAGCCGTCCGAGCAAATCCGTTTTGTGGG
AATACCTGTTCTTCATCGACATCGAAGGACACCGCCGGGACGCGCAGATT
CAGACGGCATTGGAACGCTTGGGCGAACGCGCTTCGTTTGTCAAAGCCAT
CGGTTCGTATCCGACTGCCGTTTTG


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