NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 74929;
PubMed=1683468 [NCBI, ExPASy, EBI, Israel, Japan]
Peters E.P., Wilderspin A.F., Wood S.P., Zvelebil M.J.J.M., Sezer O., Danchin A.;
"A pyruvate-stimulated adenylate cyclase has a sequence related to the fes/fps oncogenes and to eukaryotic cyclases.";
Mol. Microbiol. 5:1175-1181(1991).

Comments

FUNCTION: Plays essential roles in regulation of cellular metabolism by catalyzing the synthesis of a second messenger, cAMP.
CATALYTIC ACTIVITY: ATP = 3',5'-cyclic AMP + diphosphate.
COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
ENZYME REGULATION: Pyruvate-stimulated.
SUBUNIT: Homodimer.
SUBCELLULAR LOCATION: Cytoplasm.
SIMILARITY: Belongs to the adenylyl cyclase class-3 family.
SIMILARITY: Contains 1 guanylate cyclase domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X57541; CAA40760.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S15273; OYFKQ.

3D structure databases

ModBase

P27580.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0004016;	Molecular function: adenylate cyclase activity (inferred from electronic annotation from EC).
GO:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006171;	Biological process: cAMP biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0007242;	Biological process: intracellular signaling cascade (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR001054; A/G_cyclase.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.70.1230; A/G_cyclase; 1.

Pfam

PF00211; Guanylate_cyc; 1.
Pfam graphical view of domain structure.

SMART

SM00044; CYCc; 1.
SMART graphical view of domain structure.

PROSITE

PS50125; GUANYLATE_CYCLASE_2; 1.
PROSITE graphical view of domain structure (profiles).

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

cAMP biosynthesis; Cytoplasm; Lyase; Magnesium; Metal-binding.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 403`	`403`	`Adenylate cyclase.`	`PRO_0000195743`
`DOMAIN`	`238 347`	`110`	`Guanylate cyclase.`
`REGION`	`31 60`	`30`	`Pyruvate binding (Potential).`
`METAL`	`243 243`		`Magnesium (By similarity).`
`METAL`	`287 287`		`Magnesium (By similarity).`

Sequence information

Length: 403 AA [This is the length of the unprocessed precursor]

Molecular weight: 43899 Da [This is the MW of the unprocessed precursor]

CRC64: 90293F790E9AAF19 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSTEHTNTPR ADSPQSAAEA VRGARQHAPA ATPAESDPIL ELAEAMEGPL RIPAHTPEAV 

        70         80         90        100        110        120 
RDTVASLEKR LIGGQREFRR REVASEAGVS LHSARKLWRA IGFPELSDDE VFFTEADKKA 

       130        140        150        160        170        180 
LGTMVGMVRE GALTEETAIS LMRSVGQMTD RMVVWQIEAL VEDMIANQNL SDRQARRQLF 

       190        200        210        220        230        240 
SLLPEIIPAI EDLLLYSWRR QLNSAVHRMA LRVETGVAAY NQDRGEDDGG TPLPLARAVG 

       250        260        270        280        290        300 
FADLVSYTSL SRRMNERTLA QLVQRFEAKC AEIISVGGGR LVKTIGDEVL YVAETPQAGA 

       310        320        330        340        350        360 
QIALSLSREL AKDELFPQTR GAVVWGRLLS RLGDIYGPTV NMAARLTSLA EPGTVLTDAI 

       370        380        390        400 
TANTLRNDAR FVLTAQEITA VRGFGDIQPY ELSAGEGAGL VID

P27580 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools