Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P40138 (CYAB_STIAU)

Last modified June 16, 2009. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
OrganismStigmatella aurantiaca
Taxonomic identifier41 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaMyxococcalesCystobacterineaeCystobacteraceaeStigmatella

Protein attributes

Sequence length352 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 352352Adenylate cyclase 2
PRO_0000195748

Regions

Domain7 – 124118Response regulatory
Domain166 – 306141Guanylate cyclase

Sites

Metal binding1711Magnesium By similarity
Metal binding2151Magnesium By similarity

Amino acid modifications

Modified residue5814-aspartylphosphate Potential

Experimental info

Mutagenesis581D → Q: Decrease in activity.

Sequences

Sequence LengthMass (Da)Tools
P40138-1 [UniParc].

Last modified July 15, 1999. Version 3.
Checksum: 5DDB4C67B11ABCA6

FASTA35238,238
        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 

« Hide

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

AJ223795 Genomic DNA. Translation: CAA11548.1.
PIRT10905.

3D structure databases

HSSPHSSP built from PDB template 1B00 based on UniProtKB P08402.
ModBaseSearch...

Enzyme and pathway databases

BRENDA4.6.1.1. 119283.

Family and domain databases

InterProIPR001054. A/G_cyclase.
IPR001789. Sig_transdc_resp-reg_receiver.
[Graphical view]
Gene3DG3DSA:3.30.70.1230. A/G_cyclase. 1 hit.
PfamPF00211. Guanylate_cyc. 1 hit.
PF00072. Response_reg. 1 hit.
[Graphical view]
ProDomPD000039. Response_reg. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00044. CYCc. 1 hit.
SM00448. REC. 1 hit.
[Graphical view]
PROSITEPS50125. GUANYLATE_CYCLASE_2. 1 hit.
PS50110. RESPONSE_REGULATORY. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCYAB_STIAU
AccessionPrimary (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: June 16, 2009
This is version 52 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents