ID   CYAA_ANACY              Reviewed;         502 AA.
AC   P43524;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 96.
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;
OS   Anabaena cylindrica.
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena.
OX   NCBI_TaxID=1165;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=IAM M-1;
RX   PubMed=7601856; DOI=10.1128/jb.177.13.3873-3878.1995;
RA   Katayama M., Wada Y., Ohmori M.;
RT   "Molecular cloning of the cyanobacterial adenylate cyclase gene from the
RT   filamentous cyanobacterium Anabaena cylindrica.";
RL   J. Bacteriol. 177:3873-3878(1995).
CC   -!- FUNCTION: May function as a membrane-localized receptor protein.
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   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane; Multi-pass membrane
CC       protein.
CC   -!- DOMAIN: The N-terminal half could sense signals such as pH or a change
CC       in membrane potential and regulates the catalytic activity of the C-
CC       terminal half.
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-3 family.
CC       {ECO:0000305}.
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DR   EMBL; D55650; BAA09511.1; -; Genomic_DNA.
DR   PIR; I39600; I39600.
DR   AlphaFoldDB; P43524; -.
DR   SMR; P43524; -.
DR   PRIDE; P43524; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
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; IPR003660; HAMP_dom.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   Pfam; PF00211; Guanylate_cyc; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   SMART; SM00044; CYCc; 1.
DR   SMART; SM00304; HAMP; 1.
DR   SUPFAM; SSF55073; SSF55073; 1.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR   PROSITE; PS50885; HAMP; 1.
PE   3: Inferred from homology;
KW   ATP-binding; cAMP biosynthesis; Lyase; Magnesium; Membrane; Metal-binding;
KW   Nucleotide-binding; Thylakoid; Transmembrane; Transmembrane helix.
FT   CHAIN           1..502
FT                   /note="Adenylate cyclase"
FT                   /id="PRO_0000195742"
FT   TOPO_DOM        1..25
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        26..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        47..203
FT                   /note="Lumenal, thylakoid"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        204..226
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        227..502
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          227..280
FT                   /note="HAMP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT   DOMAIN          320..451
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT   BINDING         325
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         369
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   502 AA;  55294 MW;  C61023B37CD8C4E9 CRC64;
     MGDFCRRVDC KAMKFFALRS SIRTQIMAST TLLILALIGA IVTVWAKSES TLYHQEKLND
     AKILSKVLSS TYANEVSEEN WSQIRLNIDL LLRENEDFLY ALVSDSNQKN QIAASSPDEF
     QNNYIPDIVS LSVTNAAINS SEKTHVVETF ILRDIYFADK LRAKRGEKVM EVSSDIQTLS
     GRKLGKLRIG ISLRKVNLAV TNAVNQALVV GFAGLNIGWI CAYFLAQHLS DPVRRLQISV
     AKIAGGDLQH RADIHSRADE IGALATSVNE MSAALQISFN KLKKTLDSFE RFVPNKFISV
     IAPQGIENIE VGAASTRRMT ILFCDIRGYT SMSEAMEPIE IFRFLNDYLA CMGKAIDEAG
     GFIDKYIGDA IMALFDDGNT DCALHAAILM QQALDKFNDE RSMQTGKTGL PRISVGIGIH
     RGTVVMGTVG FTSRIDSTVI GDAVNVASRI EGLTKQYGCN ILITESVVRN LSCPESFSLR
     LIDKSVKVKG KDEAISIYEV KA