CYAA_SALTY
ID CYAA_SALTY Reviewed; 848 AA.
AC P0A1A7; Q05878;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 74.
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; Synonyms=cya; OrderedLocusNames=STM3939; ORFNames=STMD1.50;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-419.
RX PubMed=3049583; DOI=10.1016/s0021-9258(18)68088-3;
RA Holland M.M., Leib T.K., Gerlt J.A.;
RT "Isolation and characterization of a small catalytic domain released from
RT the adenylate cyclase from Escherichia coli by digestion with trypsin.";
RL J. Biol. Chem. 263:14661-14668(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
RC STRAIN=AZ3409;
RX PubMed=2204578; DOI=10.1093/genetics/125.4.709;
RA Thorner L., Fandl J., Artz S.;
RT "Analysis of sequence elements important for expression and regulation of
RT the adenylate cyclase gene (cya) of Salmonella typhimurium.";
RL Genetics 125:709-717(1990).
RN [4]
RP REVIEW.
RX PubMed=8418825;
RA Danchin A.;
RT "Phylogeny of adenylyl cyclases.";
RL Adv. Second Messenger Phosphoprotein Res. 27:109-162(1993).
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 -!- ACTIVITY REGULATION: The regulatory domain is involved in the
CC regulation of cyclase activity by the carbon source. Activated by the
CC PTS system, glucose-specific IIA component (CRR).
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-1 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF233324; AAF33452.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL22784.1; -; Genomic_DNA.
DR EMBL; X55783; CAA39304.1; -; Genomic_DNA.
DR PIR; B31974; B31974.
DR RefSeq; NP_462825.1; NC_003197.2.
DR RefSeq; WP_000281718.1; NC_003197.2.
DR AlphaFoldDB; P0A1A7; -.
DR STRING; 99287.STM3939; -.
DR PaxDb; P0A1A7; -.
DR EnsemblBacteria; AAL22784; AAL22784; STM3939.
DR GeneID; 1255465; -.
DR KEGG; stm:STM3939; -.
DR PATRIC; fig|99287.12.peg.4156; -.
DR HOGENOM; CLU_013280_0_0_6; -.
DR OMA; YDDYVMS; -.
DR PhylomeDB; P0A1A7; -.
DR BioCyc; SENT99287:STM3939-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004016; F:adenylate cyclase activity; IBA:GO_Central.
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; Reference proteome.
FT CHAIN 1..848
FT /note="Adenylate cyclase"
FT /id="PRO_0000195673"
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"
FT CONFLICT 247
FT /note="S -> T (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="R -> G (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 398
FT /note="I -> N (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 848 AA; 97359 MW; EBA1E01E1AD60641 CRC64;
MYLYIETLKQ RLDAINQLRV DRALAAMGPA FQQVYSLLPT LLHYHHPLMP GYLDGNVPSG
ICFYTPDETQ RHYLNELELY RGMTPQDPPK GELPITGVYT MGSTSSVGQS CSSDLDIWVC
HQSWLDGEER QLLQRKCSLL ESWAASLGVE VSFFLIDENR FRHNESGSLG GEDCGSTQHI
LLLDEFYRTA VRLAGKRILW SMVPCDEEEH YDDYVMTLYA QGVLTPNEWL DLGGLSSLSA
EEYFGASLWQ LYKSIDSPYK AVLKTLLLEA YSWEYPNPRL LAKDIKQRLH DGEIVSFGLD
PYCMMLERVT EYLTAIEDPT RLDLVRRCFY LKVCEKLSRE RACVGWRREV LSQLVSEWGW
DDARLTMLDN RANWKIDQVR EAHNELLDAM MQSYRNLIRF ARRNNLSVSA SPQDIGVLTR
KLYAAFEALP GKVTLVNPQI SPDLSEPNLT FIHVPPGRAN RSGWYLYNRA PNMDSIISHQ
PLEYNRYLNK LVAWAWFNGL LTSRTHLFIK GNGIVDLPKL QEMVADVSHH FPLRLPAPTP
KALYSPCEIR HLAIIVNLEY DPTAAFRNKV VHFDFRKLDV FSFGEEQNCL IGSIDLLYRN
SWNEVRTLHF NGEQAMIEAL KTILGKMHQD AAPPDSVEVF CYSQHLRGLI RTRVQQLVSE
CIELRLSSTR QETGRFKALR VSGQTWGLFF ERLNVSVQKL ENAIEFYGAI SHNKLHGLSV
QVETNQVKLP SVVDGFASEG IIQFFFEETG DEKGFNIYIL DESNRAEVYH HCEGSKEELV
RDVSRFYSSS HDRFTYGSSF INFNLPQFYQ IVKTDGRAQV IPFRTQPINT VPPANQDHDA
PLLQQYFS
