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Neisseria gonorrhoeae Search Results

Record: 1 of 1  
MiniMap IGR0987 IGR0981 IGR0982 IGR0986 IGR0985 IGR0980 IGR0983 IGR0988 IGR0984 IGR0989 dagK, - NG1216 NG1215 gntR,mdcY, - NG1221 glpR,deoR, - NG1219 NG1220 gshB,gsh-II, - NG1217 trmU, - NG1214 pyrG, - NG1212 fadD,lfcA, - NG1213 glnS,glnRS, - NG1218 dagK, - NG1216 NG1215 gntR,mdcY, - NG1221 glpR,deoR, - NG1219 NG1220 gshB,gsh-II, - NG1217 trmU, - NG1214 pyrG, - NG1212 fadD,lfcA, - NG1213 glnS,glnRS, - NG1218 dagK, - NG1216 NG1215 gntR,mdcY, - NG1221 glpR,deoR, - NG1219 NG1220 gshB,gsh-II, - NG1217 trmU, - NG1214 pyrG, - NG1212 fadD,lfcA, - NG1213 glnS,glnRS, - NG1218
* Calculated from Protein Sequence

Gene ID: NG1217

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
gshB  gsh-II  

Definition:
glutathione synthetase

Gene Start:
1167779

Gene Stop:
1166823

Gene Length:
957

Molecular Weight*:
35275

pI*:
6.60

Net Charge*:
-1.02

EC:
6.3.2.3  

Functional Class:
Biosynthesis of cofactors, prosthetic groups, and carriers; Thioredoxin, glutaredoxin, and glutathione  

Pathway: pathway table
Glutamate metabolism
Glutathione metabolism

Secondary Evidence:
Gushima,H., Yasuda,S., Soeda,E., Yokota,M., Kondo,M. and Kimura,A.
Complete nucleotide sequence of the E. coli glutathione synthetase
gsh-II.
Nucleic Acids Res. 12 (24), 9299-9307 (1984)
M:85087938

Yamaguchi,H., Kato,H., Hata,Y., Nishioka,T., Kimura,A., Oda,J. and
Katsube,Y.
Three-dimensional structure of the glutathione synthetase from
Escherichia coli B at 2.0 A resolution.
J. Mol. Biol. 229 (4), 1083-1100 (1993)
M:93188002



Comment:
Oklahoma ID: NGO.1217c

Blast Summary:  PSI-Blast Search
Several matches in gapped BLAST to glutathione synthase sequences, e.g. residues 7-297 are 50% similar to the enzyme from P.aeruginosa (gb|AAG03796).

Residues 1-319 are virtually identical to NMB1559 in N.meningitidis (gb|AAF41913).

COGS Summary:  COGS Search
BeTs to 3 clades of COG0189
COG name: Glutathione synthase/Ribosomal protein S6 modification enzyme (glutaminyl transferase)
Functional Class:  H,J
The phylogenetic pattern of COG0189 is aM-k---cE--h--gp-----
Number of proteins in this genome belonging to this COG is 1

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

ProDom Summary:  Protein Domain Search
Residues 110-280 are 53% similar to a (GLUTATHIONE SYNTHETASE SYNTHASE GSH) protein domain (PD014092) which is seen in GSHB_ECOLI.

Residues 81-289 are 27% similar to a (LIGASE SYNTHETASE CARBOXYLASE CARBAMOYL-PHOSPHATE) protein domain (PD000180) which is seen in RIMK_ECOLI.

Residues 2-106 are 30% similar to a (GLUTATHIONE SYNTHETASE SYNTHASE GSH GSH-S BIOSYNTHESIS) protein domain (PD187037) which is seen in GSHB_ECOLI.



Paralogs:  Local Blast Search


NG1217 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.


Pfam Summary:  Pfam Search
Residues 2 to 124 (E-value = 5.8e-24) place NG1217 in the GSH-S_N family which is described as Prokaryotic glutathione synthetase, N-terminal domain (PF02951)
Residues 127 to 304 (E-value = 2.9e-39) place NG1217 in the GSH-S_ATP family which is described as Prokaryotic glutathione synthetase, ATP-binding domain (PF02955)

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

PDB Hit:
pdb|1GSA|1GSA STRUCTURE OF GLUTATHIONE SYNTHETASE COMPLEXED 271.0 1e-73
pdb|1GLV|1GLV GLUTATHIONE SYNTHASE (E.C.6.3.2.3) LOOPLESS 235.0 7e-63
pdb|1GSA|1GSA STRUCTURE OF GLUTATHIONE SYNTHETASE COMPLEXED 535.0 0e+00
pdb|1GLV|1GLV GLUTA

Gene Protein Sequence:
MMKVLFIADPMASFKTYKDTTYAMMREMAKRGWRLFHTLSGELSVNGGLV
TAQASAFEFSGAKNDDDHEWFKAADKVQTALKEFDAVIMRTDPPFDMQYL
YSTQLLTLAEQQGAKVFNSGRAMRDFNEKLAILNFSRFTAPTLVTTRSAD
VRAFLKEHGDIIVKPLDGMGGMGIFRLTEKDPNIGSILETLMRFDSRTIM
AQRYIPEIVHGDKRILIIGGEVVPYALARIPQNGETRGNLAAGGRGVAQE
LDGRDREIAETLAPELKRSGILLAGLDVIGSNLTEVNVTSPTGFQEIMKQ
KSFDVAAMFADAVAAWSVR

Gene Nucleotide Sequence:  Sequence Viewer
ATGATGAAAGTCCTCTTTATCGCCGACCCGATGGCAAGTTTCAAAACCTA
CAAAGACACCACCTACGCGATGATGCGGGAAATGGCAAAACGCGGCTGGC
GGCTGTTTCATACCTTGAGCGGGGAATTGTCTGTAAACGGCGGTTTGGTA
ACGGCACAGGCATCGGCATTTGAATTTTCGGGTGCAAAAAACGATGATGA
CCATGAATGGTTTAAAGCGGCGGACAAAGTTCAGACGGCATTAAAAGAAT
TTGATGCCGTGATTATGCGTACCGATCCGCCGTTCGATATGCAATACCTT
TACTCCACCCAATTACTGACGCTGGCGGAACAGCAGGGCGCGAAAGTGTT
CAACAGCGGACGGGCGATGCGCGACTTTAACGAAAAACTGGCGATTTTGA
ATTTCAGCCGCTTTACCGCGCCCACGCTGGTAACGACCCGTTCCGCCGAT
GTCCGCGCATTTTTGAAAGAACACGGCGACATCATCGTCAAACCGCTCGA
CGGCATGGGCGGCATGGGCATCTTCCGCCTGACCGAAAAAGACCCCAACA
TCGGCAGCATCCTCGAAACCCTGATGCGGTTTGATTCCCGCACCATTATG
GCGCAACGCTACATTCCCGAAATCGTACACGGTGACAAACGCATCTTGAT
TATCGGCGGCGAAGTCGTCCCCTATGCTTTGGCGCGTATCCCGCAAAACG
GCGAAACACGCGGCAATCTGGCGGCAGGCGGGCGCGGTGTGGCGCAGGAA
TTGGACGGACGCGACCGGGAAATTGCAGAGACTCTGGCTCCCGAGCTTAA
ACGGAGCGGCATCCTGCTGGCCGGTTTGGACGTTATCGGCAGCAACCTGA
CCGAAGTCAACGTAACCAGCCCGACCGGATTCCAAGAAATTATGAAACAA
AAAAGTTTCGACGTGGCGGCAATGTTTGCCGATGCCGTTGCCGCGTGGTC
GGTACGT


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