ID   CYAA_STRGR              Reviewed;         399 AA.
AC   Q9WXC3;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Adenylate cyclase;
DE            EC=4.6.1.1;
DE   AltName: Full=ATP pyrophosphate-lyase;
DE   AltName: Full=Adenylyl cyclase;
GN   Name=cya; Synonyms=cyaA;
OS   Streptomyces griseus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10376832; DOI=10.1099/13500872-145-5-1161;
RA   Kang D.K., Li X.M., Ochi K., Horinouchi S.;
RT   "Possible involvement of cAMP in aerial mycelium formation and secondary
RT   metabolism in Streptomyces griseus.";
RL   Microbiology 145:1161-1172(1999).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP = 3',5'-cyclic AMP + diphosphate; Xref=Rhea:RHEA:15389,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58165; EC=4.6.1.1;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-3 family.
CC       {ECO:0000305}.
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DR   EMBL; AB018557; BAA76599.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9WXC3; -.
DR   SMR; Q9WXC3; -.
DR   GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006171; P:cAMP biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   CDD; cd07302; CHD; 1.
DR   Gene3D; 3.30.70.1230; -; 1.
DR   InterPro; IPR001054; A/G_cyclase.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   Pfam; PF00211; Guanylate_cyc; 1.
DR   SMART; SM00044; CYCc; 1.
DR   SUPFAM; SSF55073; SSF55073; 1.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; cAMP biosynthesis; Lyase; Magnesium; Metal-binding;
KW   Nucleotide-binding.
FT   CHAIN           1..399
FT                   /note="Adenylate cyclase"
FT                   /id="PRO_0000195750"
FT   DOMAIN          198..307
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..35
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         203
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         247
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   399 AA;  43164 MW;  C38C6A015F9E7685 CRC64;
     MTVGDTTSGS GEEPAADSSV HATPHHEVDH TVEPTDDPLA IRLEALILGA DRRYTPFQAA
     RTAGVSMDLA SRFWRAMAFA DIGQAKALTE ADVLALRRLA GLVEAGLLSE PMAIQVARST
     GQTTARLAEW QIDSFLEGLT EPPEPGMTRT EVTYPLVELL LPELQEFLVY VWRRQLAAAT
     GRVVQAADDE EMVDRRPRVR FADLVGFTRL TRRLEEEELG ELVESFETTA ADLVAPTAAG
     LVKTLGDEVL FAADDAGTAA EIALRLIEAM SQDETMPALR VGIAFGTVTT RMGDVFGTTV
     NLASRLTSIA PKDAVLVDGA FAKELVRHGE APESEAQAAE AVAAAAERVR LAEKEGREPD
     DEPPLPTYRF GLQPMWQRPV RGLGVVEPWL LARRGKTGS