CYAA_ECOL6
ID CYAA_ECOL6 Reviewed; 848 AA.
AC Q8FBP0;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Adenylate cyclase;
DE EC=4.6.1.1;
DE AltName: Full=ATP pyrophosphate-lyase;
DE AltName: Full=Adenylyl cyclase;
GN Name=cyaA; OrderedLocusNames=c4725;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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 class-1 family.
CC {ECO:0000305}.
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DR EMBL; AE014075; AAN83158.1; -; Genomic_DNA.
DR RefSeq; WP_000281692.1; NC_004431.1.
DR AlphaFoldDB; Q8FBP0; -.
DR STRING; 199310.c4725; -.
DR EnsemblBacteria; AAN83158; AAN83158; c4725.
DR KEGG; ecc:c4725; -.
DR eggNOG; COG3072; Bacteria.
DR HOGENOM; CLU_013280_0_0_6; -.
DR OMA; YDDYVMS; -.
DR BioCyc; ECOL199310:C4725-MON; -.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0005737; C:cytoplasm; 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:0006171; P:cAMP biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR000274; Adenylate_cyclase_1.
DR InterPro; IPR024686; Adenylate_cyclase_1_CS.
DR InterPro; IPR024685; Adenylate_cyclase_1_N.
DR PANTHER; PTHR38760; PTHR38760; 1.
DR Pfam; PF12633; Adenyl_cycl_N; 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; Cytoplasm; Lyase; Nucleotide-binding;
KW Phosphoprotein.
FT CHAIN 1..848
FT /note="Adenylate cyclase"
FT /id="PRO_0000195670"
FT REGION 1..535
FT /note="Catalytic"
FT REGION 541..848
FT /note="Regulatory"
FT MOD_RES 609
FT /note="Phosphohistidine; by CRR"
FT /evidence="ECO:0000255"
SQ SEQUENCE 848 AA; 97686 MW; 9D74F9E51221727D CRC64;
MYLYIETLKQ RLDAINQLRV DRALAAMGPA FQQVYSLLPT LLHYHHPLMP GYLDGNVPKG
ICLYTPDETQ RHYLNELELY RGMSVQDPPK GELPITGVYT MGSTSSVGQS CSSDLDIWVC
HQSWLDSEER QLLQRKCSLL ESWAASLGVE VSFFLIDENR FRHNESGSLG GEDCGSTQHI
LLLDEFYRTA VRLAGKRILW NMVPCDEEEH YDDYVMTLYA QGVLTPNEWL DLGGLSSLSA
EEYFGASLWQ LYKSIDSPYK AVLKTLLLEA YSWEYPNPRL LAKDIKQRLH DGEIVSFGLD
PYCMMLERVT EYLTAIEDFT RLDLVRRCFY LKVCEKLSRE RACVGWRREV LSQLVKEWEW
DDARLAMLDN RANWKIDQVR EAHNELLDAM MQSYRNLIRF ARRNNLSVSA SPQDIGVLTR
KLYAAFEALP GKVTLVNPQI SPDLSEPNLT FIYVPPGRAN RSGWYLYNRA PNIESIISHQ
PLEYNRYLNK LVAWAWFNGL LTSRTRLYIK GNGVVDLPKL QEMVADVSHH FPLRLPAPTP
KALYSPCEIR HLAIIVNLEY DPTAAFRNQV VHFDFRKLDV FSFGENQNCL VGSVDLLYRN
SWNEVRTLHF NGEQSMIEAL KTILGKMHQD AAPPDSVEVF CYSQHLRGLI RTRVQQLVSE
CIELRLSSTR QETGRFKALR VSGQTWGLFF ERLNVSVQKL ENAIEFYGAI SHNKLHGLSV
QVETNHVKLP AVVDGFASEG IIQFFFEETQ DENGFNIYIL DESNRVEVYH HCEGSKEELV
RDVSRFYSSS HDRFTYGSSF INFNLPQFYQ IVKVDGREQV IPFRTKSIGN MPPANQEHDA
PLLQQYFS