ID   Y240_METJA              Reviewed;         175 AA.
AC   Q57692;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=Putative adenylate cyclase MJ0240;
DE            EC=4.6.1.1;
DE   AltName: Full=ATP pyrophosphate-lyase;
DE   AltName: Full=Adenylyl cyclase;
GN   OrderedLocusNames=MJ0240;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
CC   -!- FUNCTION: Could catalyze the biosynthesis of cyclic AMP (cAMP) from
CC       ATP. {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase CyaB family. {ECO:0000305}.
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DR   EMBL; L77117; AAB98225.1; -; Genomic_DNA.
DR   PIR; A64330; A64330.
DR   RefSeq; WP_010869738.1; NC_000909.1.
DR   AlphaFoldDB; Q57692; -.
DR   SMR; Q57692; -.
DR   STRING; 243232.MJ_0240; -.
DR   EnsemblBacteria; AAB98225; AAB98225; MJ_0240.
DR   GeneID; 1451094; -.
DR   KEGG; mja:MJ_0240; -.
DR   eggNOG; arCOG01723; Archaea.
DR   HOGENOM; CLU_105244_2_0_2; -.
DR   InParanoid; Q57692; -.
DR   OMA; QHPCRDF; -.
DR   OrthoDB; 123503at2157; -.
DR   PhylomeDB; Q57692; -.
DR   Proteomes; UP000000805; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004016; F:adenylate cyclase activity; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006171; P:cAMP biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd07890; CYTH-like_AC_IV-like; 1.
DR   InterPro; IPR008173; Adenylyl_cyclase_CyaB.
DR   InterPro; IPR033469; CYTH-like_dom_sf.
DR   InterPro; IPR023577; CYTH_domain.
DR   PANTHER; PTHR21028; PTHR21028; 1.
DR   Pfam; PF01928; CYTH; 1.
DR   SMART; SM01118; CYTH; 1.
DR   SUPFAM; SSF55154; SSF55154; 1.
DR   TIGRFAMs; TIGR00318; cyaB; 1.
DR   PROSITE; PS51707; CYTH; 1.
PE   3: Inferred from homology;
KW   ATP-binding; cAMP biosynthesis; Cytoplasm; Lyase; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..175
FT                   /note="Putative adenylate cyclase MJ0240"
FT                   /id="PRO_0000106757"
FT   DOMAIN          1..175
FT                   /note="CYTH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01044"
FT   ACT_SITE        37
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   175 AA;  20821 MW;  7A85A90FD46F97F9 CRC64;
     MIEVEIKVKI DDKNKVVEQL KKLGFKFIKK KFQEDIYFNG IDRDFRETDE ALRIRDEDGN
     FFVTYKGPKI DKISKTREEI EVKIEDKEKM RQIFKKLGFK EVPPIRKIRE IYKKEDIEAS
     IDDVEGLGLF LELEKSISDI NEKDKVLEEM MEILKALNIS KDNIIRKSYL ELRGL