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Q3Z1N3 (DOSC_SHISS) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Diguanylate cyclase DosC
Short name=DGC
EC=2.7.7.65
Alternative name(s):
Direct oxygen-sensing cyclase
Gene names
Name:dosC
Ordered Locus Names:SSON_1634
OrganismShigella sonnei (strain Ss046) [Complete proteome] [HAMAP]
Taxonomic identifier300269 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Shigella ›

Protein attributes

Sequence length460 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Globin-coupled heme-based oxygen sensor protein displaying diguanylate cyclase (DGC) activity in response to oxygen availability. Thus, catalyzes the synthesis of cyclic diguanylate (c-di-GMP) via the condensation of 2 GTP molecules. Cyclic-di-GMP is a second messenger which controls cell surface-associated traits in bacteria By similarity.

Catalytic activity

2 GTP = 2 diphosphate + cyclic di-3',5'-guanylate.

Cofactor

Binds 1 heme group per subunit By similarity.

Binds 1 Mg2+ per subunit By similarity.

Pathway

Purine metabolism; 3',5'-cyclic di-GMP biosynthesis.

Domain

Is composed of an N-terminal sensory globin-fold domain that binds heme and oxygen, and a C-terminal GGDEF diguanylate cyclase domain By similarity.

Sequence similarities

Contains 1 GGDEF domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 460460Diguanylate cyclase DosC
PRO_0000316157

Regions

Domain325 – 458134GGDEF

Sites

Active site3761Proton acceptor Potential
Metal binding981Iron (heme proximal ligand) By similarity
Metal binding3331Magnesium By similarity
Metal binding3761Magnesium By similarity
Binding site3411Substrate By similarity
Binding site3501Substrate By similarity
Site431Involved in oxygen binding and important for the stability of the Fe(II)-O(2) complex By similarity
Site601Important for oxygen binding and stability of the Fe(II)-O(2) complex By similarity
Site651Critical for restricting water access to the heme distal side to avoid rapid autoxidation By similarity
Site3381Transition state stabilizer Potential

Sequences

Sequence LengthMass (Da)Tools
Q3Z1N3 [UniParc].

Last modified September 27, 2005. Version 1.
Checksum: 81C01550CAF5C4C4

FASTA46053,175
        10         20         30         40         50         60 
MEMYFKRMKD EWTGLVEQAD PLIRAKAAEI AVAHAHYLSI EFYRIVRIDP HAEEFLSNEQ 

        70         80         90        100        110        120 
VERQLKSAME RWIINVLSAQ VDDVERLIQI QHTVAEVHAR IGIPVEIVEM GFRVLKKILY 

       130        140        150        160        170        180 
PVIFSSDYSA AEKLQVYHFS INSIDIAMEV MTRAFTFSDS SASKEDENYR IFSLLENAEE 

       190        200        210        220        230        240 
EKERQIASIL SWEIDIIYKI LLDSDLGSSL PLSQADFGLW FNHKGRHYFS GIAEVGHISR 

       250        260        270        280        290        300 
LIQDFDGIFN QTMRNTRNLN NRSLRVKFLL QIRNTVSQII TLLRELFEEV SRHEVGMDVL 

       310        320        330        340        350        360 
TKLLNRRFLP TIFKREIAHA NRTGTPLSVL IIDVDKFKEI NDTWGHNTGD EILRKVSQAF 

       370        380        390        400        410        420 
YDNVHSSDYV FRYGGDEFII VLTEASENET LRTAERIRSR VEKTKLKAAN GEDIALSLSI 

       430        440        450        460 
GAAMFNGHPD YERLIQIADE ALYIAKRRGR NRVELWKASL

« Hide

References

[1]"Genome dynamics and diversity of Shigella species, the etiologic agents of bacillary dysentery."
Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J., Xu J. expand/collapse author list , Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J., Jin Q.
Nucleic Acids Res. 33:6445-6458(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ss046.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000038 Genomic DNA. Translation: AAZ88329.1.
RefSeqYP_310564.1. NC_007384.1.

3D structure databases

ProteinModelPortalQ3Z1N3.
ModBaseSearch...

Protein-protein interaction databases

STRING300269.SSON_1634.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ88329; AAZ88329; SSON_1634.
GeneID3668663.
KEGGssn:SSON_1634.
PATRIC18737216. VBIShiSon107113_1956.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2199.
HOGENOMHOG000006777.
KOK13069.
OMAHDGHPDY.
ProtClustDBCLSK880042.

Enzyme and pathway databases

BioCycSSON300269:GJJF-1630-MONOMER.
UniPathwayUPA00599.

Family and domain databases

Gene3D1.10.490.10. 1 hit.
InterProIPR001054. A/G_cyclase.
IPR000160. GGDEF_dom.
IPR009050. Globin-like.
IPR012292. Globin_dom.
[Graphical view]
PfamPF00990. GGDEF. 1 hit.
[Graphical view]
SMARTSM00267. GGDEF. 1 hit.
[Graphical view]
SUPFAMSSF55073. A/G_cyclase. 1 hit.
SSF46458. Globin_like. 1 hit.
TIGRFAMsTIGR00254. GGDEF. 1 hit.
PROSITEPS50887. GGDEF. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDOSC_SHISS
AccessionPrimary (citable) accession number: Q3Z1N3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: September 27, 2005
Last modified: May 29, 2013
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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