ID   CYAA_YERIN              Reviewed;         848 AA.
AC   P30528;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   25-MAY-2022, entry version 63.
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   Yersinia intermedia.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Glaser P., Sismeiro O., Danchin A.;
RL   Submitted (JUN-1992) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   REVIEW.
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   -!- 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; X66781; CAA47277.1; ALT_SEQ; Genomic_DNA.
DR   PIR; S24981; S24981.
DR   AlphaFoldDB; P30528; -.
DR   STRING; 631.CH53_1993; -.
DR   PRIDE; P30528; -.
DR   eggNOG; COG3072; Bacteria.
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..848
FT                   /note="Adenylate cyclase"
FT                   /id="PRO_0000195679"
FT   REGION          1..535
FT                   /note="Catalytic"
FT                   /evidence="ECO:0000255"
FT   REGION          541..848
FT                   /note="Regulatory"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   848 AA;  96879 MW;  1D9AB11F0D282FAD CRC64;
     MYLYIETLKQ RLDAINQLRV DRALAAMGPT FQKVYSLLPT LLHCHHPLMP GYLDGNVPHG
     VCLFTPNETQ QDYLSEVEAK WGEPLQQSVG GELPITGVYS MGSTSSIGQC HTSDLDVWVC
     HQAWLDSEER NRLQEKCSLL EKWAASMGVE VSFFLIDENR FRHNASGSLG GEDCGSTQHI
     LLLDEFYRSA VRLAGKRILW NMVPVEEENN YDDYVLSLYA QGVLTPNEWL DLGGLSTLSA
     EEYFGASLWQ LYKSIDSPYK AVLKTLLLEA YSWEYPNSQL LAMEIKQRLH AGEIVAFGLD
     AYCMMLDRVT RYLTQINDTT RLNLVRRCFY LKVCEKLSRS PASVGWRREI LSQLVSEWGW
     SDESLAVLDN RANWKIERVR EAHNELLDAM MQSYRNLIRF ARRNNLSVSA SPQDIGVLTR
     KLYAAFEALP GKVTLVNPQI SPDLSEEHLT FIHVPAGRAN RAGWYLYNQA PSMDAIVSHQ
     PLEYNRYLNK LVSWAYFNGL LTSKTRLHIK SANLCDTVKL QELVTDISHH FPLRLPAPTP
     KALYSPCEIR HLAIIVNLEH DPTAAFRNQV VHFDFRKLDV FSFGEQQQCL VGSIDLLYRN
     SWNEVRTLHF SGEQAVLEAL KTILGKMHQD AAPPESVDVF CYSQHLRGLI RTRIQQLVSE
     CIELRLSSTR QEPGRFKAVR VSGHTWGLFF ERLSVSVQKL ENAVEFYGAI SNNKLHGLSI
     QVETDQIHLP PVVDGFASEG IIQFFFEGTA DEKGFNIYIL DESNRVEVYH HCEGSKEALV
     RDVSRFYSSS HDRFTYGSSF INFNLPQFYQ IVQLDGRTQV IPFRSNTLSH LYIVDREPSQ
     PAQQFQLH