ID   CYAA_STIAU              Reviewed;         424 AA.
AC   P40137;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 3.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Adenylate cyclase 1;
DE            EC=4.6.1.1;
DE   AltName: Full=ATP pyrophosphate-lyase 1;
DE   AltName: Full=Adenylyl cyclase 1;
DE            Short=AC 1;
GN   Name=cyaA;
OS   Stigmatella aurantiaca.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Archangiaceae; Stigmatella.
OX   NCBI_TaxID=41;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC   STRAIN=B17R20;
RX   PubMed=9523018; DOI=10.1016/s0300-9084(97)86934-9;
RA   Coudart-Cavalli M.-P., Sismeiro O., Danchin A.;
RT   "Bifunctional structure of two adenylyl cyclases from the myxobacterium
RT   Stigmatella aurantiaca.";
RL   Biochimie 79:757-767(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 213-424.
RX   PubMed=8418825;
RA   Danchin A.;
RT   "Phylogeny of adenylyl cyclases.";
RL   Adv. Second Messenger Phosphoprotein Res. 27:109-162(1993).
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   -!- ACTIVITY REGULATION: Inhibited by adenosine. Activated by GTP.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-3 family.
CC       {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-2 is the initiator.
CC       {ECO:0000305}.
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DR   EMBL; AJ223796; CAA11549.1; -; Genomic_DNA.
DR   AlphaFoldDB; P40137; -.
DR   SMR; P40137; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma 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; 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   1: Evidence at protein level;
KW   ATP-binding; cAMP biosynthesis; Cell membrane; Lyase; Magnesium; Membrane;
KW   Metal-binding; Nucleotide-binding; Transmembrane; Transmembrane helix.
FT   CHAIN           1..424
FT                   /note="Adenylate cyclase 1"
FT                   /id="PRO_0000195747"
FT   TRANSMEM        26..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        57..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        88..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        163..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          230..363
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT   REGION          1..223
FT                   /note="Ion channel"
FT                   /evidence="ECO:0000255"
FT   BINDING         235
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         279
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   424 AA;  46048 MW;  C41C6841D7237EE3 CRC64;
     MMDAAGRTTQ ETLARTLESE QGHNALNLSW VRLLATSAVL IVSLYFGRVR GMTDWDVYTP
     PFAAYWSVTA LTLVALYRFE RLRRWAGLSL ALVDVPAIYW LQHIALPLSP SPGGVAGFTL
     GLYATLILLS ALSLRRTMTL VVTACAAVGE VALQREAHIS LGAQLTAVVV LGACAAGACH
     LLLRIRTLLT TATQQELKRA RLGRYFSPAV AERLQDLDRS ETSPELREVT LLFADIRDFT
     SLSERLRPEQ VVTLLNEYYG RMVEVVFRHG GTLDKFIGDA LMVYFGAPIA DPAHARRGVQ
     CALDMVQELE TVNALRSARG EPCLRIGVGV HTGPAVLGNI GSATRRLEYT AIGDTVNLAS
     RIESLTKTRD VPILASRATR EQAGDTFLWN EMAPASVPGK SQPVAIFTPR NRTPAQQAGA
     PAAA