UniProt functional annotation for P9WMU9



	UniProt functional annotation for P9WMU9

UniProt code: P9WMU9.

Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).

Taxonomy: Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium tuberculosis complex.

Function: Catalyzes the formation of the second messenger cAMP.

Catalytic activity: Reaction=ATP = 3',5'-cyclic AMP + diphosphate; Xref=Rhea:RHEA:15389, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58165; EC=4.6.1.1; Evidence={ECO:0000269|PubMed:11839758};

Cofactor: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:11839758}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:11839758}; Note=The isolated catalytic domain prefers Mn(2+) over Mg(2+) as a cofactor. {ECO:0000269|PubMed:11839758};

Biophysicochemical properties: Kinetic parameters: Vmax=420 nmol/min/mg enzyme {ECO:0000269|PubMed:15890882}; Note=At pH 6.0.; pH dependence: Optimum pH is 6.0. {ECO:0000269|PubMed:15890882};

Subunit: Homodimer. {ECO:0000269|PubMed:11839758, ECO:0000269|PubMed:15890882}.

Induction: A possible member of the dormancy regulon. Induced in response to reduced oxygen tension (hypoxia). It is hoped that this regulon will give insight into the latent, or dormant phase of infection. {ECO:0000269|PubMed:11416222}.

Domain: Consists of 3 structural domains. The pH-responsive N-terminus inhibits the adenylyl cyclase (AC) activity of the C-terminal catalytic domain. The length of the linker segment (aa 192-206) is decisive for regulation.

Disruption phenotype: No visible phenotype following infection of SPF C57BL/6 mice. {ECO:0000269|PubMed:17005450}.

Miscellaneous: Was identified as a high-confidence drug target.

Miscellaneous: Binds 1 C18:1 fatty acid per monomer.

Similarity: Belongs to the adenylyl cyclase class-4/guanylyl cyclase family. {ECO:0000255|PROSITE-ProRule:PRU00099}.

Annotations taken from UniProtKB at the EBI.


Organism:		Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Taxonomy:		Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; Mycobacterium; Mycobacterium tuberculosis complex.



Function:		Catalyzes the formation of the second messenger cAMP.


Catalytic activity:		Reaction=ATP = 3',5'-cyclic AMP + diphosphate; Xref=Rhea:RHEA:15389, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58165; EC=4.6.1.1; Evidence={ECO:0000269\|PubMed:11839758};
Cofactor:		Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269\|PubMed:11839758}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269\|PubMed:11839758}; Note=The isolated catalytic domain prefers Mn(2+) over Mg(2+) as a cofactor. {ECO:0000269\|PubMed:11839758};
Biophysicochemical properties:		Kinetic parameters: Vmax=420 nmol/min/mg enzyme {ECO:0000269\|PubMed:15890882}; Note=At pH 6.0.; pH dependence: Optimum pH is 6.0. {ECO:0000269\|PubMed:15890882};
Subunit:		Homodimer. {ECO:0000269\|PubMed:11839758, ECO:0000269\|PubMed:15890882}.
Induction:		A possible member of the dormancy regulon. Induced in response to reduced oxygen tension (hypoxia). It is hoped that this regulon will give insight into the latent, or dormant phase of infection. {ECO:0000269\|PubMed:11416222}.
Domain:		Consists of 3 structural domains. The pH-responsive N-terminus inhibits the adenylyl cyclase (AC) activity of the C-terminal catalytic domain. The length of the linker segment (aa 192-206) is decisive for regulation.
Disruption phenotype:		No visible phenotype following infection of SPF C57BL/6 mice. {ECO:0000269\|PubMed:17005450}.
Miscellaneous:		Was identified as a high-confidence drug target.
Miscellaneous:		Binds 1 C18:1 fatty acid per monomer.
Similarity:		Belongs to the adenylyl cyclase class-4/guanylyl cyclase family. {ECO:0000255\|PROSITE-ProRule:PRU00099}.