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Neisseria gonorrhoeae Search Results

Record: 1 of 1  
MiniMap IGR0533 IGR0531 IGR0534 IGR0528 IGR0530 IGR0527 IGR0535 IGR0536 IGR0532 IGR0529 NG0635 hesB, - NG0632 hscB, - NG0630 nifU, - NG0633 NG0637 iscS,nifS, - NG0636 gyrA, - NG0629 res, - NG0640 NG0631 NG0638 NG0634 lldD, - NG0639 NG0635 hesB, - NG0632 hscB, - NG0630 nifU, - NG0633 NG0637 iscS,nifS, - NG0636 gyrA, - NG0629 res, - NG0640 NG0631 NG0638 NG0634 lldD, - NG0639 NG0635 hesB, - NG0632 hscB, - NG0630 nifU, - NG0633 NG0637 iscS,nifS, - NG0636 gyrA, - NG0629 res, - NG0640 NG0631 NG0638 NG0634 lldD, - NG0639
* Calculated from Protein Sequence

Gene ID: NG0636

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
iscS  nifS  

Definition:
cysteine desulferase (aminotranferase NifS) (THII transerpersulfidase)

Gene Start:
625163

Gene Stop:
623952

Gene Length:
1212

Molecular Weight*:
44566

pI*:
6.00

Net Charge*:
-7.21

EC:
4.4.1.-  

Functional Class:
Central intermediary metabolism; Sulfur metabolism  
Other categories; Other  

Pathway: pathway table

Secondary Evidence:
Flint,D.H. Escherichia coli contains a protein that is homologous in function and N-terminal sequence to the protein encoded by the nifS gene ofAzotobacter vinelandii and that can participate in the synthesis ofthe Fe-S cluster of dihydroxy-acid dehydratase. J. Biol. Chem. 271 (27): 16068-16074 (1996) [Medline: 96279148].

Kambampati,R. and Lauhon,C.T. IscS is a sulfurtransferase for the in vitro biosynthesis of 4-thiouridine in Escherichia coli tRNA. Biochemistry 38 (50): 16561-16568 (1999) [Medline: 20068850].

Mihara,H., Kurihara,T., Yoshimura,T. and Esaki,N. Kinetic and mutational studies of three NifS homologs from Escherichia coli: mechanistic difference between L-cysteinedesulfurase and L-selenocysteine lyase reactions. J. Biochem. 127 (4): 559-567 (2000) [Medline: 20206733].

Takahashi,Y. and Nakamura,M. Functional assignment of the ORF2-iscS-iscU-iscA-hscB-hscA-fdx-ORF3 gene cluster involved in the assembly of Fe-S clusters inEscherichia coli. J. Biochem. 126 (5): 917-926 (1999) [Medline: 20013001].

Kiyasu,T., Asakura,A., Nagahashi,Y. and Hoshino,T. Contribution of cysteine desulfurase (NifS protein) to the biotin synthase reaction of Escherichia coli. J. Bacteriol. 182 (10): 2879-2885 (2000) [Medline: 20245547].

Lauhon,C.T. and Kambampati,R. The iscS gene in Escherichia coli is required for the biosynthesis of 4-thiouridine, thiamin, and NAD. J. Biol. Chem. 275 (26): 20096-20103 (2000) [Medline: 20347927].

Comment:
From GenBANK (gi:2506181): In E. coli, cysteine desulferase catalyzes the removal of elemental sulfur from cysteine to produce alanine, requiring a cofactor, pyridoxal phosphate. It functions as a sulfur delivery protein for NAD, Biotin, and Fe-S cluster synthesis. It also functions as a selenium delivery protein in the pathway for the biosynthesis of selenophosphate. It belongs to class-V of pyridoxal-phosphate-dependent aminotransferases, NIFS/ISCS subfamily.

Oklahoma ID: NGO.636c

Blast Summary:  PSI-Blast Search
Numerous significant hits in gapped BLAST to cysteine desulferase /aminotranferase NifS; e.g. residues 3-404 are 74% similar to AE004160 of Vibrio cholerae.

Residues 1-404 are 97% similar to NMA1594 and are 97% similar to AE002486, both nifS proteins of N.meningitidis (13431593, 13431594).

COGS Summary:  COGS Search
BeTs to 12 clades of COG1104
COG name: Cysteine sulfinate desulfinase/cysteine desulfurase and related enzymes (NifS family)
Functional Class:  E
The phylogenetic pattern of COG1104 is A--kYQvCeBRHuj---lINX
Number of proteins in this genome belonging to this COG is 1

Blocks Summary:  Blocks Search
***** IPB000192 (Aminotransferase class-V) with a combined E-value of 5.6e-11.
    IPB000192A    7-15
    IPB000192B    205-214


ProDom Summary:  Protein Domain Search
Residues 96-383 are 22% similar to a (NIFS-RELATED PROTEIN AMINOTRANSFERASE TRANSFERASE) protein domain (PD167853) which is seen in O84726_CHLTR.

Residues 6-288 are 72% similar to a (PYRIDOXAL PHOSPHATE AMINOTRANSFERASE TRANSFERASE PROTEIN) protein domain (PD000087) which is seen in NIFS_ECOLI.

Residues 289-373 are 78% similar to a (PROTEIN NIFS PYRIDOXAL PHOSPHATE) protein domain (PD002061) which is seen in NIFS_ECOLI.

Residues 377-404 are 78% similar to a (PROTEIN PYRIDOXAL PHOSPHATE NIFS) protein domain (PD013123) which is seen in NIFS_ECOLI.

Residues 231-287 are 57% similar to a (PROTEIN NIFS PYRIDOXAL PHOSPHATE) protein domain (PD001054) which is seen in O51886_BUCAP.



Paralogs:  Local Blast Search


NG0636 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.


Pfam Summary:  Pfam Search
Residues 16 to 308 (E-value = 9.8e-05) place NG0636 in the Pyridoxal_deC family which is described as Pyridoxal-dependent decarboxylase conserved domain (PF00282)
Residues 17 to 369 (E-value = 3e-116) place NG0636 in the Aminotran_5 family which is described as Aminotransferase class-V (PF00266)

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

PDB Hit:
pdb|1EG5|1EG5-A NIFS-LIKE263.0 3e-71
pdb|1JF9|1JF9-A CRYSTAL STRUCTURE OF SELENOCYSTEINE LYASE 96.7 6e-21
pdb|1KMJ|1KMJ-A E. COLI NIFS/CSDB PROTEIN AT 2.0A WITH THE 96.7 6e-21
pdb|1C0N|1C0N-A CSDB PROTEIN, NIFS HOMOLOGUE

Gene Protein Sequence:
MTVKTPVYLDYAATTPVDKRVAEKMIPYLTETFGNPASNSHAFGWTAEEA
VEKARADIAALINADPKEIVFTSGATESDNLAIKGAANFYKTKGKHLITV
KTEHKAVLDTMRELERQGFEVTYLGVQENGLIDLEELKAAIRDDTILISI
MWVNNEIGVVQNIPAIGEICRERKIAFHVDAAQACGKVPVDVEAAKIDLL
SMSAHKVYGPKGIGALYVRRKPRVRLEAQMHGGGHERGFRSGTLPTHQIV
GMGEAFRIAKEELAQDTAHYLKLRDIFLKGIEGIEEVYINGDLEHRAPNN
LNVSFNFVEGESLIMAVKELAVSSGSACTSASLEPSYVLRALGRNDELAH
SSLRITFGRMTTEEEVQFAAELIKSKIGKLRELSPLWEMFKDGIDLNSIE
WAAH

Gene Nucleotide Sequence:  Sequence Viewer
ATGACCGTCAAAACCCCCGTTTACCTCGACTACGCCGCCACCACACCCGT
TGACAAACGCGTTGCCGAAAAAATGATTCCCTATCTGACTGAAACCTTCG
GCAACCCCGCCTCCAACAGCCACGCATTCGGCTGGACGGCAGAAGAAGCC
GTCGAAAAAGCCCGCGCCGACATCGCCGCCCTGATTAACGCCGACCCCAA
AGAAATCGTCTTCACCAGCGGCGCGACCGAGTCCGACAACCTCGCCATCA
AAGGTGCGGCAAACTTCTACAAAACCAAAGGCAAACACCTCATCACCGTC
AAAACCGAACACAAAGCCGTGCTCGACACGATGCGCGAACTCGAACGCCA
AGGCTTTGAAGTTACCTACCTCGGCGTGCAGGAAAACGGTTTGATTGATT
TGGAAGAACTCAAAGCCGCCATCCGCGACGACACCATCCTGATTTCCATA
ATGTGGGTGAACAACGAAATCGGCGTGGTGCAAAACATTCCCGCCATCGG
CGAAATCTGCCGCGAACGCAAAATCGCCTTCCACGTCGATGCCGCCCAAG
CCTGCGGCAAAGTGCCTGTCGATGTCGAAGCCGCCAAAATCGACTTGCTC
TCGATGTCCGCGCACAAAGTGTACGGCCCCAAAGGCATCGGCGCGCTGTA
CGTCCGCCGCAAACCGCGCGTCCGCCTCGAAGCCCAAATGCACGGTGGCG
GTCACGAGCGCGGTTTCCGTTCCGGCACATTGCCGACCCATCAAATCGTC
GGCATGGGCGAGGCCTTCCGCATCGCCAAAGAAGAATTGGCACAAGACAC
AGCGCACTACCTGAAACTGCGCGACATCTTCCTCAAAGGCATCGAAGGCA
TCGAAGAAGTCTATATCAACGGCGACCTCGAACACCGCGCCCCGAACAAC
CTGAACGTCAGCTTCAACTTCGTCGAAGGCGAAAGCCTGATTATGGCGGT
GAAAGAACTCGCCGTATCCAGCGGATCCGCCTGCACCTCCGCCTCGCTCG
AACCCAGCTACGTCCTGCGCGCGCTTGGCCGCAACGACGAACTGGCGCAC
TCATCCCTGCGCATCACCTTCGGCCGCATGACCACCGAAGAAGAAGTGCA
ATTCGCGGCAGAACTGATCAAATCCAAAATCGGCAAACTGCGCGAACTGT
CGCCGCTGTGGGAAATGTTCAAAGACGGTATTGATCTGAACTCGATTGAA
TGGGCGGCGCAT


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