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P0A1A7 (CYAA_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Adenylate cyclase

EC=4.6.1.1
Alternative name(s):
ATP pyrophosphate-lyase
Adenylyl cyclase
Gene names
Name:cyaA
Synonyms:cya
Ordered Locus Names:STM3939
ORF Names:STMD1.50
OrganismSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]
Taxonomic identifier99287 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length848 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP = 3',5'-cyclic AMP + diphosphate.

Enzyme regulation

The regulatory domain is involved in the regulation of cyclase activity by the carbon source. Activated by the PTS system, glucose-specific IIA component (CRR).

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the adenylyl cyclase class-1 family.

Ontologies

Keywords
   Biological processcAMP biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionLyase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

adenylate cyclase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 848848Adenylate cyclase
PRO_0000195673

Regions

Region1 – 535535Catalytic
Region541 – 848308Regulatory

Amino acid modifications

Modified residue6091Phosphohistidine; by CRR Potential

Experimental info

Sequence conflict2471S → T no nucleotide entry Ref.2
Sequence conflict3211R → G no nucleotide entry Ref.2
Sequence conflict3981I → N no nucleotide entry Ref.2

Sequences

Sequence LengthMass (Da)Tools
P0A1A7 [UniParc].

Last modified March 1, 2005. Version 1.
Checksum: EBA1E01E1AD60641

FASTA84897,359
        10         20         30         40         50         60 
MYLYIETLKQ RLDAINQLRV DRALAAMGPA FQQVYSLLPT LLHYHHPLMP GYLDGNVPSG 

        70         80         90        100        110        120 
ICFYTPDETQ RHYLNELELY RGMTPQDPPK GELPITGVYT MGSTSSVGQS CSSDLDIWVC 

       130        140        150        160        170        180 
HQSWLDGEER QLLQRKCSLL ESWAASLGVE VSFFLIDENR FRHNESGSLG GEDCGSTQHI 

       190        200        210        220        230        240 
LLLDEFYRTA VRLAGKRILW SMVPCDEEEH YDDYVMTLYA QGVLTPNEWL DLGGLSSLSA 

       250        260        270        280        290        300 
EEYFGASLWQ LYKSIDSPYK AVLKTLLLEA YSWEYPNPRL LAKDIKQRLH DGEIVSFGLD 

       310        320        330        340        350        360 
PYCMMLERVT EYLTAIEDPT RLDLVRRCFY LKVCEKLSRE RACVGWRREV LSQLVSEWGW 

       370        380        390        400        410        420 
DDARLTMLDN RANWKIDQVR EAHNELLDAM MQSYRNLIRF ARRNNLSVSA SPQDIGVLTR 

       430        440        450        460        470        480 
KLYAAFEALP GKVTLVNPQI SPDLSEPNLT FIHVPPGRAN RSGWYLYNRA PNMDSIISHQ 

       490        500        510        520        530        540 
PLEYNRYLNK LVAWAWFNGL LTSRTHLFIK GNGIVDLPKL QEMVADVSHH FPLRLPAPTP 

       550        560        570        580        590        600 
KALYSPCEIR HLAIIVNLEY DPTAAFRNKV VHFDFRKLDV FSFGEEQNCL IGSIDLLYRN 

       610        620        630        640        650        660 
SWNEVRTLHF NGEQAMIEAL KTILGKMHQD AAPPDSVEVF CYSQHLRGLI RTRVQQLVSE 

       670        680        690        700        710        720 
CIELRLSSTR QETGRFKALR VSGQTWGLFF ERLNVSVQKL ENAIEFYGAI SHNKLHGLSV 

       730        740        750        760        770        780 
QVETNQVKLP SVVDGFASEG IIQFFFEETG DEKGFNIYIL DESNRAEVYH HCEGSKEELV 

       790        800        810        820        830        840 
RDVSRFYSSS HDRFTYGSSF INFNLPQFYQ IVKTDGRAQV IPFRTQPINT VPPANQDHDA 


PLLQQYFS 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LT2 / SGSC1412 / ATCC 700720.
[2]"Isolation and characterization of a small catalytic domain released from the adenylate cyclase from Escherichia coli by digestion with trypsin."
Holland M.M., Leib T.K., Gerlt J.A.
J. Biol. Chem. 263:14661-14668(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-419.
[3]"Analysis of sequence elements important for expression and regulation of the adenylate cyclase gene (cya) of Salmonella typhimurium."
Thorner L., Fandl J., Artz S.
Genetics 125:709-717(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
Strain: AZ3409.
[4]"Phylogeny of adenylyl cyclases."
Danchin A.
Adv. Second Messenger Phosphoprotein Res. 27:109-162(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF233324 Genomic DNA. Translation: AAF33452.1.
AE006468 Genomic DNA. Translation: AAL22784.1.
X55783 Genomic DNA. Translation: CAA39304.1.
PIRB31974.
RefSeqNP_462825.1. NC_003197.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING99287.STM3939.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL22784; AAL22784; STM3939.
GeneID1255465.
KEGGstm:STM3939.
PATRIC32386741. VBISalEnt20916_4156.

Phylogenomic databases

eggNOGCOG3072.
HOGENOMHOG000270910.
KOK05851.
OMASEGFLQF.
OrthoDBEOG63JR9H.
ProtClustDBPRK09450.

Enzyme and pathway databases

BioCycSENT99287:GCTI-3968-MONOMER.

Family and domain databases

InterProIPR000274. Adenylate_cyclase_1.
IPR024686. Adenylate_cyclase_1_CS.
IPR024685. Adenylate_cyclase_1_N.
[Graphical view]
PfamPF12633. Adenyl_cycl_N. 1 hit.
PF01295. Adenylate_cycl. 1 hit.
[Graphical view]
PIRSFPIRSF001444. Adenylate_cycl. 1 hit.
PROSITEPS01092. ADENYLATE_CYCLASE_1_1. 1 hit.
PS01093. ADENYLATE_CYCLASE_1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCYAA_SALTY
AccessionPrimary (citable) accession number: P0A1A7
Secondary accession number(s): Q05878
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: March 1, 2005
Last modified: November 13, 2013
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families