TB Genome Annotation Portal

Rv1652 (argC)

• Current annotations:
  • TBCAP: (community-based annotations - see table at bottom of page)
  • TBDB: N-acetyl-gamma-glutamyl-phosphate reductase
  • REFSEQ: N-acetyl-gamma-glutamyl-phosphate reductase
  • PATRIC: N-acetyl-gamma-glutamyl-phosphate reductase (EC 1.2.1.38)
  • TUBERCULIST: Probable N-acetyl-gamma-glutamyl-phoshate reductase ArgC
  • NCBI: Probable N-acetyl-gamma-glutamyl-phoshate reductase ArgC
  • updated information (H37Rv4):
    • gene name: argC
    • function:
    • reference:
• Type: Not Target
• Start: 1865576
• End: 1866634
• Operon:


• Trans-membrane region:
  
• Role: I.D.1 - Glutamate family
• GO terms:
  • GO:0070401 - NADP+ binding (Uniprot)
  • GO:0055114 - oxidation-reduction process (Uniprot)
  • GO:0051287 - NAD binding (Uniprot)
  • GO:0046983 - protein dimerization activity (Uniprot)
  • GO:0040007 - growth (Uniprot)
  • GO:0016620 - oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor (Uniprot)
  • GO:0016491 - oxidoreductase activity (Uniprot)
  • GO:0008652 - cellular amino acid biosynthetic process (Uniprot)
  • GO:0006526 - arginine biosynthetic process (Uniprot)
  • GO:0005737 - cytoplasm (Uniprot)
  • GO:0005515 - protein binding (Uniprot)
  • GO:0003942 - N-acetyl-gamma-glutamyl-phosphate reductase activity (Uniprot)
• Reaction(s) (based on iSM810 metabolic model):
  • NADPH[c] + NAGLUP[c] -> PI[c] + NADP[c] + NAGLUS[c]
• Gene Expression Profile (Transcriptional Responses to Drugs; Boshoff et al, 2004)
• Gene Modules extracted from cluster analysis of 249 transcriptomic datasets using ICA
• Orthologs among selected mycobacteria
• Protein structure: 2i3a, 2nqt, 2i3g
• Search for Homologs in PDB
• Top 10 Homologs in PDB (as of Nov 2020):
  

  PDB	aa ident	species	PDB title
  2NQT	100%	Mycobacterium tuberculosis	Crystal structure of N-Acetyl-gamma-Glutamyl-Phosphate Reductase (Rv1652) from Mycobacterium tuberculosis at 1.58 A resolution
  2I3G	100%	Mycobacterium tuberculosis	Crystal structure of N-Acetyl-gamma-Glutamyl-Phosphate Reductase (Rv1652) from Mycobacterium tuberculosis in complex with NADP+.
  2I3A	100%	Mycobacterium tuberculosis	Crystal structure of N-Acetyl-gamma-Glutamyl-Phosphate Reductase (Rv1652) from Mycobacterium tuberculosis
  1VKN	39%	Thermotoga maritima	Crystal structure of N-acetyl-gamma-glutamyl-phosphate reductase (TM1782) from Thermotoga maritima at 1.80 A resolution
  2Q49	38%	Arabidopsis thaliana	Ensemble refinement of the protein crystal structure of gene product from Arabidopsis thaliana At2g19940
  1XYG	38%	Arabidopsis thaliana	X-RAY STRUCTURE OF GENE PRODUCT FROM ARABIDOPSIS THALIANA AT2G19940
  2CVO	38%	Oryza sativa	Crystal structure of putative N-acetyl-gamma-glutamyl-phosphate reductase (AK071544) from rice (Oryza sativa)
  5EIO	37%	Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)	Crystal structure of LysY from Thermus thermophilus complexed with NADP+ and LysW-gamma-aminoadipic semialdehyde
  5EIN	37%	Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)	Crystal structure of C148A mutant of LysY from Thermus thermophilus in complex with NADP+ and LysW-gamma-aminoadipic acid
  2OZP	37%	Thermus thermophilus	Crystal structure of N-acetyl-gamma-glutamyl-phosphate reductase (TTHA1904) from Thermus thermophilus

• Links to additional information on argC:
  • TBDB (updated)
  • Phyre2 structure prediction, model: final.casp.pdb (from Mao et al, 2013)
  • UniProt
  • AlphaFold model
  • Vulnerability = -5.758 (from Jeremy Rock's lab)
  • KEGG - nucleotide and amino acid sequences of gene
  • Mycobrowser
  • PATRIC
  • BioCyc
  • Systems Biology

Amino Acid Sequence

MQNRQVANATKVAVAGASGYAGGEILRLLLGHPAYADGRLRIGALTAATSAGSTLGEHHPHLTPLAHRVVEPTEAAVLGGHDAVFLALPHGHSAVLAQQL
SPETLIIDCGADFRLTDAAVWERFYGSSHAGSWPYGLPELPGARDQLRGTRRIAVPGCYPTAALLALFPALAADLIEPAVTVVAVSGTSGAGRAATTDLL
GAEVIGSARAYNIAGVHRHTPEIAQGLRAVTDRDVSVSFTPVLIPASRGILATCTARTRSPLSQLRAAYEKAYHAEPFIYLMPEGQLPRTGAVIGSNAAH
IAVAVDEDAQTFVAIAAIDNLVKGTAGAAVQSMNLALGWPETDGLSVVGVAP

Additional Information