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Database: UniProt
Entry: Q9Z3Q0
LinkDB: Q9Z3Q0
Original site: Q9Z3Q0 
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};
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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
//
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