DB code: M00201

CATH domain -.-.-.- :
-.-.-.- :
3.30.70.1230 : Alpha-Beta Plaits Catalytic domain
-.-.-.- :
E.C. 4.6.1.1
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
3.30.70.1230 : Alpha-Beta Plaits M00200

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Pfam
Q99279 Receptor-type adenylate cyclase GRESAG 4.1
EC 4.6.1.1
ATP pyrophosphate-lyase
Adenylyl cyclase
PF00211 (Guanylate_cyc)
[Graphical View]
Q99280 Receptor-type adenylate cyclase GRESAG 4.3
EC 4.6.1.1
ATP pyrophosphate-lyase
Adenylyl cyclase
PF00211 (Guanylate_cyc)
[Graphical View]

KEGG enzyme name
adenylate cyclase
adenylylcyclase
adenyl cyclase
3',5'-cyclic AMP synthetase
ATP diphosphate-lyase (cyclizing)

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
Q99279 CY41_TRYBB ATP = 3'',5''-cyclic AMP + diphosphate. Membrane, Multi-pass membrane protein (Potential). Binds 1 magnesium ion per subunit.
Q99280 CY43_TRYBB ATP = 3'',5''-cyclic AMP + diphosphate. Membrane, Multi-pass membrane protein (Potential). Binds 1 magnesium ion per subunit.

KEGG Pathways
Map code Pathways E.C.
MAP00230 Purine metabolism

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00305 C00002 C00131 C00575 C00968 C00013
E.C.
Compound Magnesium ATP dATP 3',5'-Cyclic AMP 3',5'-Cyclic dAMP Pyrophosphate
Type divalent metal (Ca2+, Mg2+) amine group,nucleotide amine group,nucleotide amine group,nucleotide amine group,nucleotide phosphate group/phosphate ion
ChEBI 18420
 18420
 		15422
 15422
 		16284
 16284
 		17489
 17489
 		28074
 28074
 		29888
 29888
PubChem 888
 888
 		5957
 5957
 		15993
 15993
 		6076
 6076
 		188955
 188955
 		1023
 21961011
 1023
 21961011
1fx2A Unbound Unbound Unbound Unbound Unbound Analogue:SO4
1fx4A Bound:_MG Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
literature [5]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1fx2A ARG 1022;ARG 1053;ARG 1115 ASP 906;ASP 949(Magnesium binding)
1fx4A ARG 1010;ARG 1041;ARG 1103 ASP 894;ASP 937(Magnesium binding)

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[3]
p.33
[5]
p.437-440

References
[1]
Resource
Comments
Medline ID
PubMed ID 1525824
Journal Cell
Year 1992
Volume 70
Pages 869-72
Authors Tang WJ, Gilman AG
Title Adenylyl cyclases.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 8418825
Journal Adv Second Messenger Phosphoprotein Res
Year 1993
Volume 27
Pages 109-62
Authors Danchin A
Title Phylogeny of adenylyl cyclases.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 9214499
Journal Nature
Year 1997
Volume 388
Pages 33-4
Authors Artymiuk PJ, Poirrette AR, Rice DW, Willett P
Title A polymerase I palm in adenylyl cyclase?
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 10593176
Journal Mol Biochem Parasitol
Year 1999
Volume 104
Pages 205-17
Authors Taylor MC, Muhia DK, Baker DA, Mondragon A, Schaap PB, Kelly JM
Title Trypanosoma cruzi adenylyl cyclase is encoded by a complex multigene family.
Related PDB
Related UniProtKB
[5]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 11157750
Journal EMBO J
Year 2001
Volume 20
Pages 433-45
Authors Bieger B, Essen LO
Title Structural analysis of adenylate cyclases from Trypanosoma brucei in their monomeric state.
Related PDB 1fx2 1fx4
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 11166383
Journal Mol Biochem Parasitol
Year 2001
Volume 112
Pages 19-28
Authors Naula C, Schaub R, Leech V, Melville S, Seebeck T
Title Spontaneous dimerization and leucine-zipper induced activation of the recombinant catalytic domain of a new adenylyl cyclase of Trypanosoma brucei, GRESAG4.4B.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 12121994
Journal J Biol Chem
Year 2002
Volume 277
Pages 35025-34
Authors D'Angelo MA, Montagna AE, Sanguineti S, Torres HN, Flawia MM
Title A novel calcium-stimulated adenylyl cyclase from Trypanosoma cruzi, which interacts with the structural flagellar protein paraflagellar rod.
Related PDB
Related UniProtKB

Comments
There is a variety of adenylyl cyclase enzymes. This enzyme belongs to Class-III adenylyl cylcase family, whose catalytic domain is homologous to the catalytic domains of the class-IV family (M00200 in EzCatDB).
This enzyme has got two transmembrane regions, which provide the N-terminal cytoplasmic region, the extracelluar region, and the C-terminal cytoplasmic region with a catalytic domain. Only the catalytic domain has been determined by X-ray crystallography.
According to the literature [5], the catalytic activity of these enzymes depends on the dimerization of the catalytic domains, the C1A and C2A domains, in the case of the Class-III family enzymes (M00200 in EzCatDB). However, the catalytic domain of this enzyme is in a monomeric state, which is inactive, instead of a dimeric state. By the dimerization of these catalytic domains, this enzyme can be active.
Moreover, by the dimerization of the two molecules of this enzyme, the two catalytic sites can be formed along the 2-fold symmetrical dimer interface, whereas only one site is formed in the heterodimer of C1A/C2A domain complex of the homologous enzymes (see [5]).
According to the literature [5], the catalytic mechanism of this enzyme must be similar to that of its homologue (M00200 in EzCatDB).

Created Updated
2004-04-12 2009-02-26