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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 //