ID   CYAA_STRCO              Reviewed;         381 AA.
AC   P40135;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 123.
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; OrderedLocusNames=SCO4928; ORFNames=SCK13.20;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8282183; DOI=10.1111/j.1574-6968.1993.tb06565.x;
RA   Danchin A., Pidoux J., Krin E., Thompson C.J., Ullmann A.;
RT   "The adenylate cyclase catalytic domain of Streptomyces coelicolor is
RT   carboxy-terminal.";
RL   FEMS Microbiol. Lett. 114:145-152(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
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   -!- SIMILARITY: Belongs to the adenylyl cyclase class-3 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA52780.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X74768; CAA52780.2; ALT_INIT; Genomic_DNA.
DR   EMBL; AL939121; CAD30918.1; -; Genomic_DNA.
DR   PIR; S42625; S42625.
DR   RefSeq; NP_629081.1; NC_003888.3.
DR   RefSeq; WP_011029954.1; NZ_VNID01000027.1.
DR   AlphaFoldDB; P40135; -.
DR   SMR; P40135; -.
DR   STRING; 100226.SCO4928; -.
DR   PRIDE; P40135; -.
DR   GeneID; 1100369; -.
DR   KEGG; sco:SCO4928; -.
DR   PATRIC; fig|100226.15.peg.5007; -.
DR   eggNOG; COG2114; Bacteria.
DR   HOGENOM; CLU_043761_0_0_11; -.
DR   InParanoid; P40135; -.
DR   OMA; LQPMWQR; -.
DR   PhylomeDB; P40135; -.
DR   Proteomes; UP000001973; Chromosome.
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; IPR032026; Ad_Cy_reg.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   Pfam; PF16701; Ad_Cy_reg; 1.
DR   Pfam; PF00211; Guanylate_cyc; 1.
DR   SMART; SM00044; CYCc; 1.
DR   SUPFAM; SSF55073; SSF55073; 1.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; cAMP biosynthesis; Lyase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..381
FT                   /note="Adenylate cyclase"
FT                   /id="PRO_0000195749"
FT   DOMAIN          191..300
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         196
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         240
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   381 AA;  40903 MW;  F9356425011A6D02 CRC64;
     MTVDDTGSGA DGDGRVDPEP APDSADPGED PLALRLEGLI LGAERRYTPF QAARSAGVSM
     ELASRFWRAM GFADIGQAKA LTEADVLALR RLAGLVEAGL LSEAMAVQVA RSTGQTTARL
     AEWQIDSFLE GLTEPPEPGM TRTEVTYPIV ELLLPELQEF LVYVWRRQLA ASAGRVIQAG
     DDEEMVDRRL AVGFADLVGF TRLTRRMEEE ELGELVEAFE TTSADLVAAR GGRLVKTLGD
     EVLYAADDAG TAAEIALLLV ETMAHDETMP ELRVGIAFGT VTTRMGDVFG TTVNLASRLT
     SIAPKDAVLV DTAFAEELIR TRDAPASEAA AAEEAAAAEK EGEEPPVYRF ALQPMWQRPV
     RGLGVVEPWL LTRRDGGGGE A