ID CYA2_RHIME Reviewed; 363 AA.
AC Q52915;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 27-MAR-2024, entry version 122.
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;
GN Name=cya2; OrderedLocusNames=R01190; ORFNames=SMc00621;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=F34;
RX PubMed=7750735; DOI=10.1111/j.1574-6968.1995.tb07519.x;
RA Archdeacon J., Talty J., Boesten B., Danchin A., O'Gara F.;
RT "Cloning of the second adenylate cyclase gene (cya2) from Rhizobium
RT meliloti F34: sequence similarity to eukaryotic cyclases.";
RL FEMS Microbiol. Lett. 128:177-184(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481430; DOI=10.1073/pnas.161294398;
RA Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT meliloti strain 1021.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
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 -!- SIMILARITY: Belongs to the adenylyl cyclase class-3 family.
CC {ECO:0000305}.
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DR EMBL; X80991; CAA56916.1; -; Genomic_DNA.
DR EMBL; AL591688; CAC45769.1; -; Genomic_DNA.
DR PIR; S60684; S60684.
DR RefSeq; NP_385296.1; NC_003047.1.
DR RefSeq; WP_010969098.1; NC_003047.1.
DR AlphaFoldDB; Q52915; -.
DR SMR; Q52915; -.
DR EnsemblBacteria; CAC45769; CAC45769; SMc00621.
DR GeneID; 61602648; -.
DR KEGG; sme:SMc00621; -.
DR PATRIC; fig|266834.11.peg.2601; -.
DR eggNOG; COG2114; Bacteria.
DR HOGENOM; CLU_055425_0_0_5; -.
DR OrthoDB; 9768499at2; -.
DR Proteomes; UP000001976; 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; Nucleotide cyclase; 1.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR PANTHER; PTHR43081; ADENYLATE CYCLASE, TERMINAL-DIFFERENTIATION SPECIFIC-RELATED; 1.
DR PANTHER; PTHR43081:SF1; PH-SENSITIVE ADENYLATE CYCLASE RV1264; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR SMART; SM00044; CYCc; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 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..363
FT /note="Adenylate cyclase 2"
FT /id="PRO_0000195745"
FT DOMAIN 157..286
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT REGION 341..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 162
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 206
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT CONFLICT 179
FT /note="Q -> H (in Ref. 1; CAA56916)"
FT /evidence="ECO:0000305"
FT CONFLICT 302
FT /note="L -> R (in Ref. 1; CAA56916)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 363 AA; 39902 MW; 486A0B0C43378E37 CRC64;
MRWRFSTLEI ILLLLVVAGS GMAYAWVVYG GGGLIGATYA LFMCMPILAF ERHIIFRRLY
RRIHGSPTPA FLLSSLAVYF IFVNVGYAAA GLLLHVAGVM RESRTDAMLP SLNVLVYALA
TSGPIIFVLR VRELLGRDVF LSLLTGRYRK PVQEERVFLF IDLAGSTSLA ERFGDLRMQE
YLGKLFAAMA DPVLRYGGSI DDYVGDAAVI TWPYDRAVAD AACIRCVFDI LEQIEADAHR
WQKDYGEVPR LRAALHGGTI VAAEIGVDKH KITYFGDTVN TTARLEGLCR TLNRQVLISA
DLLRRLRPPV FVRAEDLGEH EVKGRGQKLA VLSLTAGSLS GDGATEPAGE TVRSPAAEAF
TSL
//
