EzCatDB: M00201
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DB codeM00201
CATH domainDomain 1-.-.-.-
Domain 2-.-.-.-
Domain 33.30.70.1230 : Alpha-Beta PlaitsCatalytic domain
Domain 4-.-.-.-
E.C.4.6.1.1

CATH domainRelated DB codes (homologues)
3.30.70.1230 : Alpha-Beta PlaitsM00200

Enzyme Name
UniProtKBKEGG

Q99279Q99280
Protein nameReceptor-type adenylate cyclase GRESAG 4.1Receptor-type adenylate cyclase GRESAG 4.3adenylate cyclase
adenylylcyclase
adenyl cyclase
3',5'-cyclic AMP synthetase
ATP diphosphate-lyase (cyclizing)
SynonymsEC 4.6.1.1
ATP pyrophosphate-lyase
Adenylyl cyclase
EC 4.6.1.1
ATP pyrophosphate-lyase
Adenylyl cyclase
PfamPF00211 (Guanylate_cyc)
[Graphical view]
PF00211 (Guanylate_cyc)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00230Purine metabolism

UniProtKB:Accession NumberQ99279Q99280
Entry nameCY41_TRYBBCY43_TRYBB
ActivityATP = 3'',5''-cyclic AMP + diphosphate.ATP = 3'',5''-cyclic AMP + diphosphate.
Subunit

Subcellular locationMembrane, Multi-pass membrane protein (Potential).Membrane, Multi-pass membrane protein (Potential).
CofactorBinds 1 magnesium ion per subunit.Binds 1 magnesium ion per subunit.

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProducts
KEGG-idC00305C00002C00131C00575C00968C00013
CompoundMagnesiumATPdATP3',5'-Cyclic AMP3',5'-Cyclic dAMPPyrophosphate
Typedivalent metal (Ca2+, Mg2+)amine group,nucleotideamine group,nucleotideamine group,nucleotideamine group,nucleotidephosphate group/phosphate ion
ChEBI18420
15422
16284
17489
28074
29888
PubChem888
5957
15993
6076
188955
21961011
1023
              
1fx2AUnboundUnboundUnboundUnboundUnboundAnalogue:SO4
1fx4ABound:_MGUnboundUnboundUnboundUnboundUnbound

Active-site residues
resource
literature [5]
pdbCatalytic residuesCofactor-binding residues
          
1fx2AARG 1022;ARG 1053;ARG 1115
ASP 906;ASP  949(Magnesium binding)
1fx4AARG 1010;ARG 1041;ARG 1103
ASP 894;ASP  937(Magnesium binding)

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[3]p.33
[5]p.437-440

references
[1]
PubMed ID1525824
JournalCell
Year1992
Volume70
Pages869-72
AuthorsTang WJ, Gilman AG
TitleAdenylyl cyclases.
[2]
PubMed ID8418825
JournalAdv Second Messenger Phosphoprotein Res
Year1993
Volume27
Pages109-62
AuthorsDanchin A
TitlePhylogeny of adenylyl cyclases.
[3]
PubMed ID9214499
JournalNature
Year1997
Volume388
Pages33-4
AuthorsArtymiuk PJ, Poirrette AR, Rice DW, Willett P
TitleA polymerase I palm in adenylyl cyclase?
[4]
PubMed ID10593176
JournalMol Biochem Parasitol
Year1999
Volume104
Pages205-17
AuthorsTaylor MC, Muhia DK, Baker DA, Mondragon A, Schaap PB, Kelly JM
TitleTrypanosoma cruzi adenylyl cyclase is encoded by a complex multigene family.
[5]
CommentsX-ray crystallography
PubMed ID11157750
JournalEMBO J
Year2001
Volume20
Pages433-45
AuthorsBieger B, Essen LO
TitleStructural analysis of adenylate cyclases from Trypanosoma brucei in their monomeric state.
Related PDB1fx2,1fx4
[6]
PubMed ID11166383
JournalMol Biochem Parasitol
Year2001
Volume112
Pages19-28
AuthorsNaula C, Schaub R, Leech V, Melville S, Seebeck T
TitleSpontaneous dimerization and leucine-zipper induced activation of the recombinant catalytic domain of a new adenylyl cyclase of Trypanosoma brucei, GRESAG4.4B.
[7]
PubMed ID12121994
JournalJ Biol Chem
Year2002
Volume277
Pages35025-34
AuthorsD'Angelo MA, Montagna AE, Sanguineti S, Torres HN, Flawia MM
TitleA novel calcium-stimulated adenylyl cyclase from Trypanosoma cruzi, which interacts with the structural flagellar protein paraflagellar rod.

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).

createdupdated
2004-04-122009-02-26


Copyright: Nozomi Nagano, JST & CBRC-AIST
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Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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