Reviewed, UniProtKB/Swiss-Prot P40138 (CYAB_STIAU)

Names and origin

Protein names

Recommended name:
    Adenylate cyclase 2
    EC=4.6.1.1
Alternative name(s):
    ATP pyrophosphate-lyase 2
    Adenylyl cyclase 2
      Short name=AC2

Gene names

Name:

cyaB

Organism

Stigmatella aurantiaca

Taxonomic identifier

41 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Deltaproteobacteria › Myxococcales › Cystobacterineae › Cystobacteraceae › Stigmatella

Protein attributes

Sequence length	352 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	ATP = 3',5'-cyclic AMP + diphosphate.
Cofactor	Binds 1 magnesium ion per subunit By similarity.
Enzyme regulation	Inhibited by adenosine and GTP.
Sequence similarities	In the C-terminal section; belongs to the adenylyl cyclase class-3 family. Contains 1 guanylate cyclase domain. Contains 1 response regulatory domain.

Ontologies

Keywords
Biological process	cAMP biosynthesis
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Lyase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	cAMP biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW intracellular signaling cascade Inferred from electronic annotation. Source: InterPro regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: InterPro two-component signal transduction system (phosphorelay) Inferred from electronic annotation. Source: InterPro
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 two-component response regulator activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 352	352	Adenylate cyclase 2		PRO_0000195748
Regions
	Domain	7 – 124	118	Response regulatory
	Domain	166 – 306	141	Guanylate cyclase
Sites
	Metal binding	171	1	Magnesium By similarity
	Metal binding	215	1	Magnesium By similarity
Amino acid modifications
	Modified residue	58	1	4-aspartylphosphate Potential
Experimental info
	Mutagenesis	58	1	D → Q: Decrease in activity.

Sequences

	Sequence		Length	Mass (Da)
	P40138-1 [UniParc]. Last modified July 15, 1999. Version 3. Checksum: 5DDB4C67B11ABCA6	FASTA	352	38,238
	10 20 30 40 50 60 MLQGHHRVMV VDDSPLACDF VKEGLEALGL GYEVMCFQDP YEALEQVGKV QPAIVLSDLD 70 80 90 100 110 120 MPGIDGLELC WRLKESPSRQ VPVIILTAND SEAERVKGLR AGADDYVNKS ASMAELSARI 130 140 150 160 170 180 ESVMRRTSET ERMRKLFARY TSDAVVEEIL KSPDTVVLTG EKPEVTVLFA DIRNFTGLAE 190 200 210 220 230 240 SLPPEQVVGV LNQVLGRLSD AVLTCGGTLD KFLGDGLMAV WGAPVHRTDD ALRALQAAKM 250 260 270 280 290 300 MMTAMVELRQ AAQAEWAANE RLGRPLVLEL GIGINSGLAV AGNIGGSMRT EYTCIGDAVN 310 320 330 340 350 VAARLCALAG PGEILAGERT RELVSHREMP FEDLPPVRLK GKQQPVPLYR VL

References

[1]	"Bifunctional structure of two adenylyl cyclases from the myxobacterium Stigmatella aurantiaca." Coudart-Cavalli M.-P., Sismeiro O., Danchin A. Biochimie 79:757-767(1997) [PubMed: 9523018] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION, MUTANT GLN-58. Strain: B17R20.
[2]	Danchin A. Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO 163.
[3]	"Phylogeny of adenylyl cyclases." Danchin A. Adv. Second Messenger Phosphoprotein Res. 27:109-162(1993) [PubMed: 8418825] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 149-350.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ223795 Genomic DNA. Translation: CAA11548.1.
PIR	T10905.
3D structure databases
SMR	P40138. Positions 7-219, 162-350.
ModBase	Search...
Enzyme and pathway databases
BRENDA	4.6.1.1. 119283.
Family and domain databases
InterPro	IPR001054. A/G_cyclase. IPR011006. CheY-like. IPR001789. Sig_transdc_resp-reg_receiver. [Graphical view]
Gene3D	G3DSA:3.30.70.1230. A/G_cyclase. 1 hit.
Pfam	PF00211. Guanylate_cyc. 1 hit. PF00072. Response_reg. 1 hit. [Graphical view]
SMART	SM00044. CYCc. 1 hit. SM00448. REC. 1 hit. [Graphical view]
PROSITE	PS50125. GUANYLATE_CYCLASE_2. 1 hit. PS50110. RESPONSE_REGULATORY. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CYAB_STIAU

Accession

Primary (citable) accession number: P40138
Secondary accession number(s): O54080

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	July 15, 1999
Last modified:	January 19, 2010
This is version 54 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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