CYA1_RHIME
ID CYA1_RHIME Reviewed; 665 AA.
AC P19485;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Adenylate cyclase 1;
DE EC=4.6.1.1;
DE AltName: Full=ATP pyrophosphate-lyase 1;
DE AltName: Full=Adenylyl cyclase 1;
GN Name=cya1; Synonyms=cyaA; OrderedLocusNames=R00259; ORFNames=SMc00339;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
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 [2]
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 473-665.
RX PubMed=1970565; DOI=10.1128/jb.172.5.2614-2621.1990;
RA Beuve A., Boesten B., Crasnier M., Danchin A., O'Gara F.;
RT "Rhizobium meliloti adenylate cyclase is related to eucaryotic adenylate
RT and guanylate cyclases.";
RL J. Bacteriol. 172:2614-2621(1990).
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-3 family.
CC {ECO:0000305}.
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DR EMBL; AL591688; CAC41696.1; -; Genomic_DNA.
DR EMBL; M35096; AAA26247.1; -; Genomic_DNA.
DR PIR; A35266; A35266.
DR PIR; B35266; B35266.
DR RefSeq; NP_384365.1; NC_003047.1.
DR RefSeq; WP_010968455.1; NC_003047.1.
DR AlphaFoldDB; P19485; -.
DR SMR; P19485; -.
DR STRING; 266834.SMc00339; -.
DR EnsemblBacteria; CAC41696; CAC41696; SMc00339.
DR GeneID; 61601740; -.
DR KEGG; sme:SMc00339; -.
DR PATRIC; fig|266834.11.peg.1626; -.
DR eggNOG; COG2114; Bacteria.
DR HOGENOM; CLU_021956_0_0_5; -.
DR OMA; SMERDDQ; -.
DR Proteomes; UP000001976; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; 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; IPR033479; dCache_1.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR029151; Sensor-like_sf.
DR Pfam; PF02743; dCache_1; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF00672; HAMP; 1.
DR SMART; SM00044; CYCc; 1.
DR SMART; SM00304; HAMP; 1.
DR SUPFAM; SSF103190; SSF103190; 1.
DR SUPFAM; SSF55073; SSF55073; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR PROSITE; PS50885; HAMP; 1.
PE 3: Inferred from homology;
KW ATP-binding; cAMP biosynthesis; Cell membrane; Lyase; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..665
FT /note="Adenylate cyclase 1"
FT /id="PRO_0000195744"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 373..393
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 394..444
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 471..603
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 476
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 520
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 665 AA; 71325 MW; E6E553FE5FF77A1B CRC64;
MLQRSESGFK DIESMQDSNA DKPSRTWTSS LRSLLGLVMV AMLIVVSATL VGLDYRRARS
AAIAGAEDNM DAFVGRLVDR LGALSGDTSA LVSLVASVAN SFLVPPPERM NDKVAVLREG
IARSPHIDGV YVGYPSGAFF HVVDLDSAAW RMALDAPRGA AIAVRSMERN DQGKPFDRIL
FLDASGLQFA ERHAASNGFD PRTRPWYRAA VNGKAPVAIG PYEMATTGNL GMTISQAHRG
NPQIVIGADV VLDTITDFLS RERLTDDSVS FVLDAVGRPI IHSDSTMMRR IMASKGRDRP
VATPQEDGLI ESIRRNPPPA GKATLVEVGN RTYLVTVAPL ESALLLSGHR VVVAAPLDEL
LAAANETLVQ GLAVSGAVVV VAVLLALVLA HLITKSLNQL TDSANRLQDL DFATPIDVSS
HVAEISTLNG AMNRARDAIF TFALYVPKEL VRKGIESGHF GGRAAWRQEV TAMFTDIYDF
TTISEGRSPE EVVAMLSEYF DLFSEVVAAH DGTIIQFHGD SVFAMWNAPV ADTRHAEHAC
RCALAVEERL EAFNSAQRAS GLPEFRTRFG IHTGTAVVGS VGAKERLQYT AMGDTVNVAS
RLEGMNKDYG TSVLASGAVV AQCKDMVKFR PLGTAKAKGR STALDIYEVV GVVRAVNTTE
AGTAA
