CYAA_GLUNI
ID CYAA_GLUNI Reviewed; 403 AA.
AC P27580;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 92.
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 Glutamicibacter nicotianae (Arthrobacter nicotianae).
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Glutamicibacter.
OX NCBI_TaxID=37929;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 74929;
RX PubMed=1683468; DOI=10.1111/j.1365-2958.1991.tb01890.x;
RA Peters E.P., Wilderspin A.F., Wood S.P., Zvelebil M.J.J.M., Sezer O.,
RA Danchin A.;
RT "A pyruvate-stimulated adenylate cyclase has a sequence related to the
RT fes/fps oncogenes and to eukaryotic cyclases.";
RL Mol. Microbiol. 5:1175-1181(1991).
CC -!- FUNCTION: Plays essential roles in regulation of cellular metabolism by
CC catalyzing the synthesis of a second messenger, cAMP.
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: Pyruvate-stimulated.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-3 family.
CC {ECO:0000305}.
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DR EMBL; X57541; CAA40760.1; -; Genomic_DNA.
DR PIR; S15273; OYFKQ.
DR AlphaFoldDB; P27580; -.
DR SMR; P27580; -.
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: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 SUPFAM; SSF55073; SSF55073; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; cAMP biosynthesis; Cytoplasm; Lyase; Magnesium; Metal-binding;
KW Nucleotide-binding.
FT CHAIN 1..403
FT /note="Adenylate cyclase"
FT /id="PRO_0000195743"
FT DOMAIN 238..347
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 31..60
FT /note="Pyruvate binding"
FT /evidence="ECO:0000255"
FT BINDING 243
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 287
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 403 AA; 43899 MW; 90293F790E9AAF19 CRC64;
MSTEHTNTPR ADSPQSAAEA VRGARQHAPA ATPAESDPIL ELAEAMEGPL RIPAHTPEAV
RDTVASLEKR LIGGQREFRR REVASEAGVS LHSARKLWRA IGFPELSDDE VFFTEADKKA
LGTMVGMVRE GALTEETAIS LMRSVGQMTD RMVVWQIEAL VEDMIANQNL SDRQARRQLF
SLLPEIIPAI EDLLLYSWRR QLNSAVHRMA LRVETGVAAY NQDRGEDDGG TPLPLARAVG
FADLVSYTSL SRRMNERTLA QLVQRFEAKC AEIISVGGGR LVKTIGDEVL YVAETPQAGA
QIALSLSREL AKDELFPQTR GAVVWGRLLS RLGDIYGPTV NMAARLTSLA EPGTVLTDAI
TANTLRNDAR FVLTAQEITA VRGFGDIQPY ELSAGEGAGL VID
