ID   CYAA_AERHY              Reviewed;         843 AA.
AC   Q59119;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 64.
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   Aeromonas hydrophila.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=644;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=218;
RX   PubMed=8874804; DOI=10.1016/0300-9084(96)82192-4;
RA   Trotot P., Sismeiro O., Vivares C., Glaser P., Bresson-Roy A., Danchin A.;
RT   "Comparative analysis of the cya locus in enterobacteria and related Gram-
RT   negative facultative anaerobes.";
RL   Biochimie 78:277-287(1996).
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   -!- ACTIVITY REGULATION: The regulatory domain is involved in the
CC       regulation of cyclase activity by the carbon source.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-1 family.
CC       {ECO:0000305}.
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DR   EMBL; X95881; CAA65130.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q59119; -.
DR   STRING; 1448139.AI20_17035; -.
DR   eggNOG; COG3072; Bacteria.
DR   BRENDA; 4.6.1.1; 164.
DR   GO; GO:0005737; C:cytoplasm; 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:0006171; P:cAMP biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR000274; Adenylate_cyclase_1.
DR   InterPro; IPR024686; Adenylate_cyclase_1_CS.
DR   InterPro; IPR024685; Adenylate_cyclase_1_N.
DR   PANTHER; PTHR38760; PTHR38760; 1.
DR   Pfam; PF12633; Adenyl_cycl_N; 1.
DR   Pfam; PF01295; Adenylate_cycl; 1.
DR   PIRSF; PIRSF001444; Adenylate_cycl; 1.
DR   PROSITE; PS01092; ADENYLATE_CYCLASE_1_1; 1.
DR   PROSITE; PS01093; ADENYLATE_CYCLASE_1_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; cAMP biosynthesis; Cytoplasm; Lyase; Nucleotide-binding.
FT   CHAIN           1..843
FT                   /note="Adenylate cyclase"
FT                   /id="PRO_0000195668"
FT   REGION          1..537
FT                   /note="Catalytic"
FT   REGION          543..843
FT                   /note="Regulatory"
SQ   SEQUENCE   843 AA;  96853 MW;  8DE267A02ABE8C77 CRC64;
     MLVKLDTLVA RYDELNRLKT QRALGLMSRY GQQVFQLLPV MLHFNHPLLP GYVAGDVPHG
     IWSFTANEAQ QAFIQDLCQN ANCQNGLTTH DKSIQGLYSM GSTSSIGQCC HSDLDIWVCH
     VAGLSQERLE LLDLKCQQLS KWAEQRGVDL NFFLIPEDKF RQRNDAQMQG ESCGSAQHLL
     LLDEFYRSAM LIAGKRLLWY LVPAEYDDRY DEYVNGLFAH GKLSQDDWLD LGGFDRIPAE
     EYFGSALWQL YKGIDSPYKA VLKSVLMEAY SHEYPNTRLL SVTSRDWFQH NEGMHYRLDN
     YCLMLDKVTN YLKSIGDMQR LDLVRRCFYL KVCDGLSHPK EDHSPAWRRE QMTQLVAYWG
     WSPERLHHLD HRQEWKVEDV KVAHAELLEA LMQSYRNLIQ FARRNNISES INPEDIGILS
     RKLYAAFESL PGKVQRINLT IAPDLSEPDL SLVQVPHGRL NRAGWYLYKH SLEPADIIGR
     APLEYNGYIS KLVSWAYFNG LLTPQSRVHL FNQGSDLHID NLHQFCRDLS GTFPVKYPRA
     TNLALSRPCE IRQLSIFLNL ETDPTSHWVG QVIEFDANAA DVFSFGRNLE CLVGSVDLVY
     RNSWSEIRTL HFQGDEAVVD ALTTILGKMH QDAAAPEMIE VFCYSQHFRS LVRTRFQQLV
     AECIELRLAR DKQQLVKTLA LGKEKYGIFF ERRGVSVKKL ENAIDFYRHI SHNKLDHLPL
     RLDKTHSQHL PGIVDSYASE GLVQFFFDTR DAGTNIYILD EANRVEIYQH FAGNKDELVQ
     GVNRFYTSSH ERFSDAGQFS NFNLPPYYEI VQVNGELEVI PYRSQGPLRD GAGQARELGS
     ATG