Reviewed, UniProtKB/Swiss-Prot P27580 (CYAA_BRELI)

Names and origin

Protein names

Recommended name:
    Adenylate cyclase
    EC=4.6.1.1
Alternative name(s):
    ATP pyrophosphate-lyase
    Adenylyl cyclase

Gene names

Name:

cya

Organism

Brevibacterium liquefaciens

Taxonomic identifier

37929 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Micrococcaceae › Arthrobacter

Protein attributes

Sequence length	403 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (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 structure	Homodimer.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the adenylyl cyclase class-3 family. Contains 1 guanylate cyclase domain.

Ontologies

Keywords
Biological process	cAMP biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Lyase
Gene Ontology (GO)
Biological process	cAMP biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW intracellular signaling cascade Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW adenylate cyclase activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 403	403	Adenylate cyclase		PRO_0000195743
Regions
	Domain	238 – 347	110	Guanylate cyclase
	Region	31 – 60	30	Pyruvate binding Potential
Sites
	Metal binding	243	1	Magnesium By similarity
	Metal binding	287	1	Magnesium By similarity

Sequences

	Sequence		Length	Mass (Da)
	P27580-1 [UniParc]. Last modified August 1, 1992. Version 1. Checksum: 90293F790E9AAF19	FASTA	403	43,899
	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

References

[1]

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

Cross-references

Sequence databases
EMBLGenBankDDBJ	X57541 Genomic DNA. Translation: CAA40760.1.
PIR	OYFKQ. S15273.
3D structure databases
ModBase	Search...
Enzyme and pathway databases
BRENDA	4.6.1.1. 21513.
Family and domain databases
InterPro	IPR001054. A/G_cyclase. [Graphical view]
Gene3D	G3DSA:3.30.70.1230. A/G_cyclase. 1 hit.
Pfam	PF00211. Guanylate_cyc. 1 hit. [Graphical view]
SMART	SM00044. CYCc. 1 hit. [Graphical view]
PROSITE	PS50125. GUANYLATE_CYCLASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CYAA_BRELI

Accession

Primary (citable) accession number: P27580

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	June 16, 2009
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)