ID   CYAB_STIAU              Reviewed;         352 AA.
AC   P40138; O54080;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 3.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Adenylate cyclase 2;
DE            EC=4.6.1.1;
DE   AltName: Full=ATP pyrophosphate-lyase 2;
DE   AltName: Full=Adenylyl cyclase 2;
DE            Short=AC2;
GN   Name=cyaB;
OS   Stigmatella aurantiaca.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Archangiaceae; Stigmatella.
OX   NCBI_TaxID=41;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION, AND MUTANT GLN-58.
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   SEQUENCE REVISION TO 163.
RA   Danchin A.;
RL   Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 149-350.
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 and GTP.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the adenylyl cyclase
CC       class-3 family. {ECO:0000305}.
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DR   EMBL; AJ223795; CAA11548.1; -; Genomic_DNA.
DR   PIR; T10905; T10905.
DR   AlphaFoldDB; P40138; -.
DR   SMR; P40138; -.
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:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR   CDD; cd07302; CHD; 1.
DR   Gene3D; 3.30.70.1230; -; 1.
DR   InterPro; IPR001054; A/G_cyclase.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   Pfam; PF00211; Guanylate_cyc; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   SMART; SM00044; CYCc; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF52172; SSF52172; 1.
DR   SUPFAM; SSF55073; SSF55073; 1.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; cAMP biosynthesis; Lyase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Phosphoprotein.
FT   CHAIN           1..352
FT                   /note="Adenylate cyclase 2"
FT                   /id="PRO_0000195748"
FT   DOMAIN          7..124
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   DOMAIN          166..306
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT   BINDING         171
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         215
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         58
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   MUTAGEN         58
FT                   /note="D->Q: Decrease in activity."
SQ   SEQUENCE   352 AA;  38238 MW;  5DDB4C67B11ABCA6 CRC64;
     MLQGHHRVMV VDDSPLACDF VKEGLEALGL GYEVMCFQDP YEALEQVGKV QPAIVLSDLD
     MPGIDGLELC WRLKESPSRQ VPVIILTAND SEAERVKGLR AGADDYVNKS ASMAELSARI
     ESVMRRTSET ERMRKLFARY TSDAVVEEIL KSPDTVVLTG EKPEVTVLFA DIRNFTGLAE
     SLPPEQVVGV LNQVLGRLSD AVLTCGGTLD KFLGDGLMAV WGAPVHRTDD ALRALQAAKM
     MMTAMVELRQ AAQAEWAANE RLGRPLVLEL GIGINSGLAV AGNIGGSMRT EYTCIGDAVN
     VAARLCALAG PGEILAGERT RELVSHREMP FEDLPPVRLK GKQQPVPLYR VL