ID   CYAA_DICCH              Reviewed;         851 AA.
AC   P40130;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   25-MAY-2022, entry version 60.
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   Dickeya chrysanthemi (Pectobacterium chrysanthemi) (Erwinia chrysanthemi).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Dickeya.
OX   NCBI_TaxID=556;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=B374;
RX   PubMed=3057176;
RA   Danchin A., Lenzen G.;
RT   "Structure and evolution of bacterial adenylate cyclase: comparison between
RT   Escherichia coli and Erwinia chrysanthemi.";
RL   Second Messengers Phosphoproteins 12:7-28(1988).
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   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-1 family.
CC       {ECO:0000305}.
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DR   EMBL; X63207; CAA44891.1; -; Genomic_DNA.
DR   PIR; S23699; S23699.
DR   AlphaFoldDB; P40130; -.
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..851
FT                   /note="Adenylate cyclase"
FT                   /id="PRO_0000195675"
FT   REGION          1..534
FT                   /note="Catalytic"
FT                   /evidence="ECO:0000255"
FT   REGION          540..851
FT                   /note="Regulatory"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   851 AA;  97560 MW;  0EA8AE944F302AD2 CRC64;
     MYFYIETLKQ RLDAINQLRV DRALEAMKPA FQQVYSLLPV LLHHHHPLMP GYLEGKVPHG
     ICLFSPDEKQ QHYLDSVELR WGELSAPDRK GELPITGVYS MGSTSSIGQS CSSDLDIWVC
     HQSWLDNEER QLQQKCSLLE KWAAGQGVDV SFFLMDENRF RHNESGSLGG EDCGSTQHIL
     LLDEFYRTAV RMAGKRILWN MVPVEEEAHY DEFVLSLYAR GALAPNEWLD LGGLSALSAE
     EYFGASLWQL YKSIDSPYKA VLKTLLLEAY SWEYPNTRLL SSEIKARLHK GEIVSFGLDP
     YCMMLERVTQ YLDAINDQTR LDLVRRCFYL KVCEKLSRER ACTAWRRQIL TQMVQAWGWS
     DERLVMLDNR ANWKIGQVRE AHNELLDAMM QSYRNLIRFA RRNNLSVSAS PQDIGVLTRK
     LYAAFEALPG KVTLVNPQIS PDLSETNLTF IYVPAGRANR SGWYLYNQAP SMDAIISHQP
     LEYNRYLNKL VAWAYFNGLL TSSTRLHIKG HELCDIARLQ ELVSDVSSHF PLRVAAPTPK
     ALYSPCEIRH LAIIVNLEHD PTAAFRNQVV HFDFRQLDVF SFGQQQQCLV GSIDLLYRNS
     WNEVRTLHFS GEQAMLEALK TILGKMHQDA ALPESLEVFC YSQHLRGLIR TRVQQLVSEC
     IELRLSSTRQ EPGRFKAVKV AGETWGLFFE RLSVSAQKLE NAVEFYGAIS NNKLQGLPVQ
     VETNHIHLPP VVDGVASEGI IQFFFEDQHD NQGFNIYILD ESNRVEVYHH CEGSKEELVR
     DVSRFYSSSH DRFTYGSSFI NFNLPQFYQI VQLDGRTQVI PFRSSALSHL CVTPSSEDKK
     NLVLSQRLQM L