TB Genome Annotation Portal

Rv1625c (cya)

• Current annotations:
  • TBCAP: (community-based annotations - see table at bottom of page)
  • TBDB: adenylate cyclase
  • REFSEQ: membrane-anchored adenylyl cyclase Cya (ATP pyrophosphate-lyase) (adenylate cyclase)
  • PATRIC: Adenylate cyclase (EC 4.6.1.1)
  • TUBERCULIST: Membrane-anchored adenylyl cyclase Cya (ATP pyrophosphate-lyase) (adenylate cyclase)
  • NCBI: Membrane-anchored adenylyl cyclase Cya (ATP pyrophosphate-lyase) (adenylate cyclase)
  • updated information (H37Rv4):
    • gene name: cya
    • function:
    • reference:
• Type: Not Target
• Start: 1826614
• End: 1827945
• Operon:


• Trans-membrane region:
  
• Role: IV.J - Cyclases
• GO terms:
  • GO:0046872 - metal ion binding (Uniprot)
  • GO:0035556 - intracellular signal transduction (Uniprot)
  • GO:0030145 - manganese ion binding (Uniprot)
  • GO:0016849 - phosphorus-oxygen lyase activity (Uniprot)
  • GO:0016829 - lyase activity (Uniprot)
  • GO:0016021 - integral component of membrane (Uniprot)
  • GO:0016020 - membrane (Uniprot)
  • GO:0009190 - cyclic nucleotide biosynthetic process (Uniprot)
  • GO:0007165 - signal transduction (Uniprot)
  • GO:0006171 - cAMP biosynthetic process (Uniprot)
  • GO:0005886 - plasma membrane (Uniprot)
  • GO:0005622 - intracellular (Uniprot)
  • GO:0005524 - ATP binding (Uniprot)
  • GO:0005515 - protein binding (Uniprot)
  • GO:0004016 - adenylate cyclase activity (Uniprot)
  • GO:0000287 - magnesium ion binding (Uniprot)
  • GO:0000166 - nucleotide binding (Uniprot)
• Reaction(s) (based on iSM810 metabolic model):
  • ATP[c] -> PPI[c] + cAMP[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: 1yk9
• Search for Homologs in PDB
• Top 10 Homologs in PDB (as of Nov 2020):
  

  PDB	aa ident	species	PDB title
  4P2M	100%	Mycobacterium tuberculosis	Swapped Dimer of Mycobacterial Adenylyl cyclase Rv1625c: Form 1
  4P2X	98%	Mycobacterium tuberculosis	Swapped Dimer of Mycobacterial Adenylyl cyclase Rv1625c: Form 2
  1YK9	98%	Mycobacterium tuberculosis	Crystal structure of a mutant form of the mycobacterial adenylyl cyclase Rv1625c
  4P2F	98%	Mycobacterium tuberculosis	Monomeric form of a single mutant (F363R) of Mycobacterial Adenylyl cyclase Rv1625c
  5O5L	84%	Mycobacterium intracellulare 1956	X-ray structure of a bacterial adenylyl cyclase soluble domain, solved at cryogenic temperature
  5O5K	84%	Mycobacterium intracellulare 1956	X-ray structure of a bacterial adenylyl cyclase soluble domain
  3ET6	47%	Chlamydomonas reinhardtii	The crystal structure of the catalytic domain of a eukaryotic guanylate cyclase
  3ET6	47%	Chlamydomonas reinhardtii	The crystal structure of the catalytic domain of a eukaryotic guanylate cyclase
  5OYH	38%	Catenaria anguillulae PL171	crystal structure of the catalytic core of a rhodopsin-guanylyl cyclase with converted specificity in complex with ATPalphaS
  6AOA	37%	Blastocladiella emersonii	Monomeric crystal structure of the E497/C566D double mutant of the guanylyl cyclase domain of the RhoGC fusion protein from the aquatic fungus Blastocladiella emersonii

• Links to additional information on cya:
  • TBDB (updated)
  • Phyre2 structure prediction, model: final.casp.pdb (from Mao et al, 2013)
  • UniProt
  • AlphaFold model
  • Vulnerability = 0.496 (from Jeremy Rock's lab)
  • KEGG - nucleotide and amino acid sequences of gene
  • Mycobrowser
  • PATRIC
  • BioCyc
  • Systems Biology

Amino Acid Sequence

VAARKCGAPPIAADGSTRRPDCVTAVRTQARAPTQHYAESVARRQRVLTITAWLAVVVTGSFALMQLATGAGGWYIALINVFTAVTFAIVPLLHRFGGLV
APLTFIGTAYVAIFAIGWDVGTDAGAQFFFLVAAALVVLLVGIEHTALAVGLAAVAAGLVIALEFLVPPDTGLQPPWAMSVSFVLTTVSACGVAVATVWF
ALRDTARAEAVMEAEHDRSEALLANMLPASIAERLKEPERNIIADKYDEASVLFADIVGFTERASSTAPADLVRFLDRLYSAFDELVDQHGLEKIKVSGD
SYMVVSGVPRPRPDHTQALADFALDMTNVAAQLKDPRGNPVPLRVGLATGPVVAGVVGSRRFFYDVWGDAVNVASRMESTDSVGQIQVPDEVYERLKDDF
VLRERGHINVKGKGVMRTWYLIGRKVAADPGEVRGAEPRTAGV

Additional Information