ID   CYAA_PASMU              Reviewed;         838 AA.
AC   Q05766;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 2.
DT   16-JUN-2009, entry version 58.
DE   RecName: Full=Adenylate cyclase;
DE            EC=4.6.1.1;
DE   AltName: Full=ATP pyrophosphate-lyase;
DE   AltName: Full=Adenylyl cyclase;
GN   Name=cya; OrderedLocusNames=PM1811;
OS   Pasteurella multocida.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=747;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 43137 / LMG 2851 / NCTC 10322 / W-9217;
RX   MEDLINE=92011391; PubMed=1917858;
RA   Mock M., Crasnier M., Duflot E., Dumay V., Danchin A.;
RT   "Structural and functional relationships between Pasteurella multocida
RT   and enterobacterial adenylate cyclases.";
RL   J. Bacteriol. 173:6265-6269(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   MEDLINE=21145866; PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
RN   [3]
RP   REVIEW.
RX   MEDLINE=93119764; PubMed=8418825;
RA   Danchin A.;
RT   "Phylogeny of adenylyl cyclases.";
RL   Adv. Second Messenger Phosphoprotein Res. 27:109-162(1993).
CC   -!- CATALYTIC ACTIVITY: ATP = 3',5'-cyclic AMP + diphosphate.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-1 family.
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DR   EMBL; M68901; AAA25532.1; -; Genomic_DNA.
DR   EMBL; AE004439; AAK03895.1; -; Genomic_DNA.
DR   PIR; A38172; A38172.
DR   RefSeq; NP_246750.1; -.
DR   GeneID; 1245158; -.
DR   GenomeReviews; AE004439_GR; PM1811.
DR   KEGG; pmu:PM1811; -.
DR   NMPDR; fig|272843.1.peg.1812; -.
DR   HOGENOM; Q05766; -.
DR   OMA; Q05766; LWQLYKG.
DR   BRENDA; 4.6.1.1; 258935.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004016; F:adenylate cyclase activity; IEA:EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006171; P:cAMP biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR000274; Adenylt_cyclse_1.
DR   Pfam; PF01295; Adenylate_cycl; 1.
DR   PIRSF; PIRSF001444; Adenylate_cycl; 1.
DR   PROSITE; PS01092; ADENYLATE_CYCLASE_1_1; 1.
DR   PROSITE; PS01093; ADENYLATE_CYCLASE_1_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; cAMP biosynthesis; Complete proteome; Cytoplasm; Lyase;
KW   Nucleotide-binding.
FT   CHAIN         1    838       Adenylate cyclase.
FT                                /FTId=PRO_0000195677.
FT   REGION        1    541       Catalytic (Potential).
FT   REGION      547    838       Regulatory (Potential).
FT   CONFLICT    469    469       D -> A (in Ref. 1; AAA25532).
FT   CONFLICT    659    660       TA -> PH (in Ref. 1; AAA25532).
SQ   SEQUENCE   838 AA;  96799 MW;  08D64CA7B0A30E62 CRC64;
     MNYDLFSAQK KVEYLDKLRI ERALSGSSGE FQHVFQLLTL LLHINHPNLP GYVADAPVGI
     ADFVISPYQK QYLLTTVPSL EANQSLLPSF SYRSTNAILG VYVMGSIASI SQTPKSDLDT
     WVCHRDDLST KEKEALQRKT HLLKNWAKQF NIEINFYLMD QKRFRCFRYA EPLTAENCGS
     AQYMLLLDEF YRSAIRLAGK PLLWLHLLIE QEENYESEVE RLVRTQQICL DDWVDFGGLG
     QLSANEYFGA SLWQLYKGID APYKSVIKIL LLETYSSEYP NTYLIARQFK EELLTGKLNP
     SHHFDPYLAM LQRATRYLTK HNELKRLGFV RRSVYLKATE GMCWQDPNAT NNWRLQHLQK
     LIQEWDWSDA LIEELNQRAN WKIKQVKKAH NSLIKFLMLS YRNLVAFARK HKVNSSIMPQ
     DISVLTRKLY TAFEELPGKI TLLNPQISLN LSEKNLLFFE VKGSKTFKDG WYVVNQTPSV
     AGFVQKRYTE YSESLNKLVA WAYFNRILTA NTDLHIISPN VSLTTLRHFV TDLRLSFPVT
     VSSVTNEDLT HACEIRSLIV AVNLTVDPTK KITQVKSRIQ ASDLFSFGPK EESLVGSIDI
     TYRNLWNEIR TLHFEGPNAI LLALKVLSNK IHRGAPSPKL IQVFSYSHRY RRTLSNIVTA
     LINRCISIQI GDALPPQNNL LRVAGKNWQF FFEERGISLQ EIHSNEELEA TGFDTALQTE
     VEEKESALPD TSRTYPPEID HFASEGFLQF FFEDNSDGSF NVYILDEANR IEIYRNCDGQ
     KEKKILEINH IYQSSGLDEN NNPYKIVQRD FNYPQFYQLL LQENGVKIVP FHSRLAMS
//