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Search term: Rv1264

General annotation | Coordinates | Sequence | Structural information | Orthologs/Cross-references | Interacting Drugs/Compounds | Bibliography
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General annotation
Gene nameRv1264
Rv numberRv1264
FunctionPossibly involved in cAMP synthesis [catalytic activity: ATP = 3',5'-cyclic AMP + diphosphate]. Activity is PH-dependent. Inhibited by polyphosphates.
ProductAdenylyl cyclase (ATP pyrophosphate-lyase) (adenylate cyclase)
CommentsRv1264, (MTCY50.18c), len: 397 aa. Adenylate cyclase (function proven experimentally: see Linder et al., 2002), showing some similarity to other adenylate cyclases e.g. CYAA_BRELI|P27580 (403 aa), FASTA scores, opt: 270, E(): 1.3e-10, (29.3% identity in 317 aa overlap); etc. Similar to other putative cyclases in M. tuberculosis e.g. Rv2212, Rv1647. The C terminus seems to code for a catalytic domain belonging to a subfamily of adenylyl cyclase isozymes (mostly found in Gram-positive bacteria). The N terminus seems to be a potential novel regulator of adenylyl cyclase activity (autoinhibitory domain). Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.
Molecular mass (Da)42200
Isoelectric point4.6985
Gene length (bp)1194
Protein length397
Location (kb)1411.89

Functional categoryintermediary metabolism and respiration

ProteomicsIdentified by mass spectrometry in M. tuberculosis H37Rv-infected guinea pig lungs at 30 days but not 90 days (See Kruh et al., 2010). Identified by mass spectrometry in whole cell lysates of M. tuberculosis H37Rv but not the culture filtrate or membrane protein fraction (See de Souza et al., 2011).
TranscriptomemRNA identified by DNA microarray analysis (gene induced by hypoxia) (see Sherman et al., 2001).
Mutationnon essential gene by Himar1-based transposon mutagenesis in H37Rv strain (see Sassetti et al., 2003). Non-essential gene for in vitro growth of H37Rv, by sequencing of Himar1-based transposon mutagenesis (See Griffin et al., 2011). M. tuberculosis H37Rv (streptomycin-resistant strain 1424) Rv1264 mutant is not attenuated in C57BL/6 (See Dittrich et al., 2006). Check for mutants available at TARGET website


Protein sequence in FASTA format
>M. tuberculosis H37Rv|Rv1264|Rv1264
Blastp: Pre-computed results
TransMembrane prediction using Hidden Markov Models: TMHMM
Genomic sequence

Add extra bases upstream (5') and downstream (3')

Structural information
Protein Data Bank1Y10 1Y11 2EV1 2EV2 2EV3 2EV4

Enzyme Classification4.6.1.1
Gene Ontologyadenylate cyclase activity
ATP binding
cAMP biosynthetic process
lipid binding
negative regulation of cAMP biosynthetic process
protein homodimerization activity
metal ion binding
M. bovisMb1295
M. lepraeML1111
M. marinumMMAR_4173
M. smegmatisMSMEG_5018
Multiple Sequences Alignment: between orthologs

Interacting Drugs/Compounds
TDR TargetsRv1264

Expression Data

Sherman DR, Voskuil M, Schnappinger D, Liao R, Harrell MI, Schoolnik GK,
Regulation of the Mycobacterium tuberculosis hypoxic response gene encoding alpha -crystallin
Proc Natl Acad Sci U S A (2001) 98(13):7534-9
Cited for: Transcriptome
Linder JU, Schultz A, Schultz JE,
Adenylyl cyclase Rv1264 from Mycobacterium tuberculosis has an autoinhibitory N-terminal domain
J Biol Chem (2002) 277(18):15271-6
Cited for: Product/Biochemistry
Sassetti CM, Boyd DH, Rubin EJ,
Genes required for mycobacterial growth defined by high density mutagenesis.
Mol Microbiol (2003) 48(1):77-84
Cited for: Mutant
Tews I, Findeisen F, Sinning I, Schultz A, Schultz JE, Linder JU,
The structure of a pH-sensing mycobacterial adenylyl cyclase holoenzyme.
Science (2005) 308(5724):1020-3
Cited for: Structure
Dittrich D, Keller C, Ehlers S, Schultz JE, Sander P,
Characterization of a Mycobacterium tuberculosis mutant deficient in pH-sensing adenylate cyclase Rv1264.
Int J Med Microbiol (2006) 296(8):563-6
Cited for: Mutant
Findeisen F, Linder JU, Schultz A, Schultz JE, Brugger B, Wieland F, Sinning I, Tews I,
The structure of the regulatory domain of the adenylyl cyclase Rv1264 from Mycobacterium tuberculosis with bound oleic acid.
J Mol Biol (2007) 369(5):1282-95
Cited for: Structure
Guo YL, Mayer H, Vollmer W, Dittrich D, Sander P, Schultz A, Schultz JE,
Polyphosphates from Mycobacterium bovis--potent inhibitors of class III adenylate cyclases.
FEBS J (2009) 276(4):1094-103
Cited for: Biochemistry
Kruh NA, Troudt J, Izzo A, Prenni J, Dobos KM,
Portrait of a pathogen: the Mycobacterium tuberculosis proteome in vivo.
PLoS One (2010) 5(11):e13938
Cited for: Proteomics
de Souza GA, Leversen NA, Malen H, Wiker HG,
Bacterial proteins with cleaved or uncleaved signal peptides of the general secretory pathway.
J Proteomics (2011) 75(2):502-10
Cited for: Proteomics
Griffin JE, Gawronski JD, Dejesus MA, Ioerger TR, Akerley BJ, Sassetti CM,
High-resolution phenotypic profiling defines genes essential for mycobacterial growth and cholesterol catabolism.
PLoS Pathog (2011) 7(9):e1002251
Cited for: Mutant