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Protein

Adenylate cyclase

Gene

cyaA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the formation of the second messenger cAMP from ATP. Its transcript is probably degraded by endoribonuclease LS (rnlA), decreasing cAMP levels and the negative regulator Crp-cAMP, which then induces its own transcription again.

Catalytic activityi

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

Activity regulationi

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).

GO - Molecular functioni

  • adenylate cyclase activity Source: EcoCyc
  • ATP binding Source: UniProtKB-KW

GO - Biological processi

  • cAMP biosynthetic process Source: EcoCyc

Keywordsi

Molecular functionLyase
Biological processcAMP biosynthesis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:ADENYLATECYC-MONOMER
MetaCyc:ADENYLATECYC-MONOMER
BRENDAi4.6.1.1 2026

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylate cyclase (EC:4.6.1.1)
Alternative name(s):
ATP pyrophosphate-lyase
Adenylyl cyclase
Gene namesi
Name:cyaA
Synonyms:cya
Ordered Locus Names:b3806, JW3778
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10170 cyaA

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Not essential, eliminates the NaCl sensitivity of an rnlA deletion mutant.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001956691 – 848Adenylate cyclaseAdd BLAST848

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei609Phosphohistidine; by CRRSequence analysis1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP00936
PRIDEiP00936

Expressioni

Inductioni

Repressed by the Crp-cAMP complex. Expression increases during growth, decreasing again in stationary phase; more strongly induced in an rnlA deletion mutant, levels remain high even in stationary phase (at protein level).2 Publications

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
helDP150383EBI-1116685,EBI-551473

Protein-protein interaction databases

BioGridi4262610, 11 interactors
IntActiP00936, 23 interactors
STRINGi316407.85676245

Structurei

3D structure databases

ProteinModelPortaliP00936
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 535CatalyticAdd BLAST535
Regioni541 – 848RegulatoryAdd BLAST308

Sequence similaritiesi

Belongs to the adenylyl cyclase class-1 family.Curated

Phylogenomic databases

eggNOGiENOG4107T0K Bacteria
COG3072 LUCA
HOGENOMiHOG000270910
InParanoidiP00936
KOiK05851
OMAiHPLLPGY

Family and domain databases

InterProiView protein in InterPro
IPR000274 Adenylate_cyclase_1
IPR024686 Adenylate_cyclase_1_CS
IPR024685 Adenylate_cyclase_1_N
PANTHERiPTHR38760 PTHR38760, 1 hit
PfamiView protein in Pfam
PF12633 Adenyl_cycl_N, 1 hit
PF01295 Adenylate_cycl, 1 hit
PIRSFiPIRSF001444 Adenylate_cycl, 1 hit
PROSITEiView protein in PROSITE
PS01092 ADENYLATE_CYCLASE_1_1, 1 hit
PS01093 ADENYLATE_CYCLASE_1_2, 1 hit

Sequencei

Sequence statusi: Complete.

P00936-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MYLYIETLKQ RLDAINQLRV DRALAAMGPA FQQVYSLLPT LLHYHHPLMP
60 70 80 90 100
GYLDGNVPKG ICLYTPDETQ RHYLNELELY RGMSVQDPPK GELPITGVYT
110 120 130 140 150
MGSTSSVGQS CSSDLDIWVC HQSWLDSEER QLLQRKCSLL ENWAASLGVE
160 170 180 190 200
VSFFLIDENR FRHNESGSLG GEDCGSTQHI LLLDEFYRTA VRLAGKRILW
210 220 230 240 250
NMVPCDEEEH YDDYVMTLYA QGVLTPNEWL DLGGLSSLSA EEYFGASLWQ
260 270 280 290 300
LYKSIDSPYK AVLKTLLLEA YSWEYPNPRL LAKDIKQRLH DGEIVSFGLD
310 320 330 340 350
PYCMMLERVT EYLTAIEDFT RLDLVRRCFY LKVCEKLSRE RACVGWRRAV
360 370 380 390 400
LSQLVSEWGW DEARLAMLDN RANWKIDQVR EAHNELLDAM MQSYRNLIRF
410 420 430 440 450
ARRNNLSVSA SPQDIGVLTR KLYAAFEALP GKVTLVNPQI SPDLSEPNLT
460 470 480 490 500
FIYVPPGRAN RSGWYLYNRA PNIESIISHQ PLEYNRYLNK LVAWAWFNGL
510 520 530 540 550
LTSRTRLYIK GNGIVDLPKL QEMVADVSHH FPLRLPAPTP KALYSPCEIR
560 570 580 590 600
HLAIIVNLEY DPTAAFRNQV VHFDFRKLDV FSFGENQNCL VGSVDLLYRN
610 620 630 640 650
SWNEVRTLHF NGEQSMIEAL KTILGKMHQD AAPPDSVEVF CYSQHLRGLI
660 670 680 690 700
RTRVQQLVSE CIELRLSSTR QETGRFKALR VSGQTWGLFF ERLNVSVQKL
710 720 730 740 750
ENAIEFYGAI SHNKLHGLSV QVETNHVKLP AVVDGFASEG IIQFFFEETQ
760 770 780 790 800
DENGFNIYIL DESNRVEVYH HCEGSKEELV RDVSRFYSSS HDRFTYGSSF
810 820 830 840
INFNLPQFYQ IVKVDGREQV IPFRTKSIGN MPPANQDHDT PLLQQYFS
Length:848
Mass (Da):97,586
Last modified:June 20, 2003 - v5
Checksum:iF0400E3406B15018
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti223V → G in CAA25817 (PubMed:6393056).Curated1
Sequence conflicti223V → G in CAA47280 (PubMed:8874804).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01653 Genomic DNA Translation: CAA25817.1
X66782 Genomic DNA Translation: CAA47280.1
M87049 Genomic DNA Translation: AAA67602.1
U00096 Genomic DNA Translation: AAC76809.1
AP009048 Genomic DNA Translation: BAE77495.1
PIRiG65184 OYEC
RefSeqiNP_418250.1, NC_000913.3
WP_000281668.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC76809; AAC76809; b3806
BAE77495; BAE77495; BAE77495
GeneIDi947755
KEGGiecj:JW3778
eco:b3806
PATRICifig|1411691.4.peg.2902

Similar proteinsi

Cross-referencesi

Web resourcesi

Escherichia coli adenylate cyclase homepage

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01653 Genomic DNA Translation: CAA25817.1
X66782 Genomic DNA Translation: CAA47280.1
M87049 Genomic DNA Translation: AAA67602.1
U00096 Genomic DNA Translation: AAC76809.1
AP009048 Genomic DNA Translation: BAE77495.1
PIRiG65184 OYEC
RefSeqiNP_418250.1, NC_000913.3
WP_000281668.1, NZ_LN832404.1

3D structure databases

ProteinModelPortaliP00936
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262610, 11 interactors
IntActiP00936, 23 interactors
STRINGi316407.85676245

Proteomic databases

PaxDbiP00936
PRIDEiP00936

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76809; AAC76809; b3806
BAE77495; BAE77495; BAE77495
GeneIDi947755
KEGGiecj:JW3778
eco:b3806
PATRICifig|1411691.4.peg.2902

Organism-specific databases

EchoBASEiEB0168
EcoGeneiEG10170 cyaA

Phylogenomic databases

eggNOGiENOG4107T0K Bacteria
COG3072 LUCA
HOGENOMiHOG000270910
InParanoidiP00936
KOiK05851
OMAiHPLLPGY

Enzyme and pathway databases

BioCyciEcoCyc:ADENYLATECYC-MONOMER
MetaCyc:ADENYLATECYC-MONOMER
BRENDAi4.6.1.1 2026

Miscellaneous databases

PROiPR:P00936

Family and domain databases

InterProiView protein in InterPro
IPR000274 Adenylate_cyclase_1
IPR024686 Adenylate_cyclase_1_CS
IPR024685 Adenylate_cyclase_1_N
PANTHERiPTHR38760 PTHR38760, 1 hit
PfamiView protein in Pfam
PF12633 Adenyl_cycl_N, 1 hit
PF01295 Adenylate_cycl, 1 hit
PIRSFiPIRSF001444 Adenylate_cycl, 1 hit
PROSITEiView protein in PROSITE
PS01092 ADENYLATE_CYCLASE_1_1, 1 hit
PS01093 ADENYLATE_CYCLASE_1_2, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiCYAA_ECOLI
AccessioniPrimary (citable) accession number: P00936
Secondary accession number(s): Q2M8B1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: June 20, 2003
Last modified: September 12, 2018
This is version 143 of the entry and version 5 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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