ID CYA3_RHIME Reviewed; 587 AA. AC Q9Z3Q0; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 02-NOV-2001, sequence version 2. DT 27-MAR-2024, entry version 138. DE RecName: Full=Putative adenylate cyclase 3; DE EC=4.6.1.1; DE AltName: Full=ATP pyrophosphate-lyase 3; DE AltName: Full=Adenylyl cyclase 3; GN Name=cya3; Synonyms=cyaF5; OrderedLocusNames=RA0861; ORFNames=SMa1583; OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium OS meliloti). OG Plasmid pSymA (megaplasmid 1). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=266834; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=CXM1-105; RX PubMed=10485295; DOI=10.1007/s004380051052; RA Sharypova L.A., Yurgel S.N., Keller M., Simarov B.V., Puehler A., RA Becker A.; RT "The eff-482 locus of Sinorhizobium meliloti CXM1-105 that influences RT symbiotic effectiveness consists of three genes encoding an endoglycanase, RT a transcriptional regulator and an adenylate cyclase."; RL Mol. Gen. Genet. 261:1032-1044(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1021; RX PubMed=11481432; DOI=10.1073/pnas.161294798; RA Barnett M.J., Fisher R.F., Jones T., Komp C., Abola A.P., Barloy-Hubler F., RA Bowser L., Capela D., Galibert F., Gouzy J., Gurjal M., Hong A., Huizar L., RA Hyman R.W., Kahn D., Kahn M.L., Kalman S., Keating D.H., Palm C., RA Peck M.C., Surzycki R., Wells D.H., Yeh K.-C., Davis R.W., Federspiel N.A., RA Long S.R.; RT "Nucleotide sequence and predicted functions of the entire Sinorhizobium RT meliloti pSymA megaplasmid."; RL Proc. Natl. Acad. Sci. U.S.A. 98:9883-9888(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 -!- 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 -!- SIMILARITY: Belongs to the adenylyl cyclase class-3 family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAK65519.2; Type=Erroneous initiation; Evidence={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; AJ225896; CAB38103.1; -; Genomic_DNA. DR EMBL; AE006469; AAK65519.2; ALT_INIT; Genomic_DNA. DR PIR; E95369; E95369. DR RefSeq; NP_436107.2; NC_003037.1. DR RefSeq; WP_015242161.1; NC_003037.1. DR AlphaFoldDB; Q9Z3Q0; -. DR SMR; Q9Z3Q0; -. DR EnsemblBacteria; AAK65519; AAK65519; SMa1583. DR GeneID; 61599632; -. DR KEGG; sme:SMa1583; -. DR PATRIC; fig|266834.11.peg.895; -. DR HOGENOM; CLU_019981_0_0_5; -. DR OrthoDB; 9807521at2; -. DR Proteomes; UP000001976; Plasmid pSymA. DR GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProtKB-EC. DR GO; GO:0005524; F:ATP 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 Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1. DR Gene3D; 3.40.50.10070; TolB, N-terminal domain; 1. DR InterPro; IPR001054; A/G_cyclase. DR InterPro; IPR029787; Nucleotide_cyclase. DR InterPro; IPR011990; TPR-like_helical_dom_sf. DR InterPro; IPR019734; TPR_repeat. DR PANTHER; PTHR44366; UDP-N-ACETYLGLUCOSAMINE--PEPTIDE N-ACETYLGLUCOSAMINYLTRANSFERASE 110 KDA SUBUNIT; 1. DR PANTHER; PTHR44366:SF1; UDP-N-ACETYLGLUCOSAMINE--PEPTIDE N-ACETYLGLUCOSAMINYLTRANSFERASE 110 KDA SUBUNIT; 1. DR Pfam; PF00211; Guanylate_cyc; 1. DR Pfam; PF13424; TPR_12; 1. DR Pfam; PF13432; TPR_16; 1. DR SMART; SM00028; TPR; 4. DR SUPFAM; SSF55073; Nucleotide cyclase; 1. DR SUPFAM; SSF48452; TPR-like; 1. DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1. DR PROSITE; PS50005; TPR; 4. DR PROSITE; PS50293; TPR_REGION; 1. PE 3: Inferred from homology; KW ATP-binding; cAMP biosynthesis; Lyase; Nucleotide-binding; Plasmid; KW Reference proteome; Repeat; TPR repeat. FT CHAIN 1..587 FT /note="Putative adenylate cyclase 3" FT /id="PRO_0000195746" FT DOMAIN 12..127 FT /note="Guanylate cyclase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099" FT REPEAT 343..376 FT /note="TPR 1" FT REPEAT 421..454 FT /note="TPR 2" FT REPEAT 455..488 FT /note="TPR 3" FT REPEAT 490..522 FT /note="TPR 4" FT REPEAT 524..556 FT /note="TPR 5" FT CONFLICT 18 FT /note="A -> T (in Ref. 1; CAB38103)" FT /evidence="ECO:0000305" FT CONFLICT 178 FT /note="R -> H (in Ref. 1; CAB38103)" FT /evidence="ECO:0000305" FT CONFLICT 183 FT /note="P -> L (in Ref. 1; CAB38103)" FT /evidence="ECO:0000305" FT CONFLICT 196..197 FT /note="KP -> S (in Ref. 1; CAB38103)" FT /evidence="ECO:0000305" FT CONFLICT 251 FT /note="D -> N (in Ref. 1; CAB38103)" FT /evidence="ECO:0000305" FT CONFLICT 553 FT /note="N -> D (in Ref. 1; CAB38103)" FT /evidence="ECO:0000305" SQ SEQUENCE 587 AA; 65307 MW; 4630AC9816FB615D CRC64; MAKESIRRRL AAILAADAVG YSRLMERDEK STHTLLMARW KEVLEPLVGI HQGRVFKRTG DGVLVEFGSA VNAVECAAAL QQAMAAANRD LPEDRAIVLR VGVNLGDIMV EDSDLFGDGV NVAARIEALA DPGGVAISDG IHEYVHGRTD IDFVDSGYHE VKNIERPVHI WTWSPKDRAR EPPNIAAEPP PQLPAKPSIA VLPFDNMSGD PEQGYFADGI TEDIITDLSK VSGLFVIARN SSFAYKGKTP DIRKVSRELG VRYVLEGSVR RAANRIRINA QMIDGTTGGH LWAERYDRGL EDIFAVQDEV TRTIVNALRV KLTAGEEERR ESRGKVDPEA YDLLVRSRQA ILQFNALSSM EARRMLHRVL EIDPGMAAAH ASLSIIALTD FINQWNGATP DNLTQALGLA QEAIDTDGSE PQGHYTLALA LSWMRRLDEA EHAAERAIEL DPNSANAYTA LGTIRDFQGR HEEALALYTR AHRLDPQFDL SLHFQGRALL NLGRFDEAEV AFKRRLLLAP RSDMTRFYLA CLYGRTGRHE EARGYWREVL GVNPSFSVDH LRRSLPYQDP HLMDRLVEGL REAGVSI //