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 27-MAR-2024, entry version 101. 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; Cyanobacteriota; Cyanophyceae; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D55650; BAA09511.1; -; Genomic_DNA. DR PIR; I39600; I39600. DR AlphaFoldDB; P43524; -. DR SMR; P43524; -. 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 CDD; cd06225; HAMP; 1. DR Gene3D; 6.10.340.10; -; 1. DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 1. DR InterPro; IPR001054; A/G_cyclase. DR InterPro; IPR003660; HAMP_dom. DR InterPro; IPR029787; Nucleotide_cyclase. DR PANTHER; PTHR43081:SF16; ADENYLATE CYCLASE, TERMINAL-DIFFERENTIATION SPECIFIC; 1. DR PANTHER; PTHR43081; ADENYLATE CYCLASE, TERMINAL-DIFFERENTIATION SPECIFIC-RELATED; 1. DR Pfam; PF00211; Guanylate_cyc; 1. DR Pfam; PF00672; HAMP; 1. DR SMART; SM00044; CYCc; 1. DR SMART; SM00304; HAMP; 1. DR SUPFAM; SSF158472; HAMP domain-like; 1. DR SUPFAM; SSF55073; Nucleotide cyclase; 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 //