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Q3YV74 (RHAD_SHISS) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Rhamnulose-1-phosphate aldolase

EC=4.1.2.19
Gene names
Name:rhaD
Ordered Locus Names:SSON_4072
OrganismShigella sonnei (strain Ss046) [Complete proteome] [HAMAP]
Taxonomic identifier300269 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella

Protein attributes

Sequence length274 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the reversible cleavage of L-rhamnulose-1-phosphate to dihydroxyacetone phosphate (DHAP) and L-lactaldehyde By similarity. HAMAP MF_00770

Catalytic activity

L-rhamnulose 1-phosphate = glycerone phosphate + (S)-lactaldehyde. HAMAP MF_00770

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP MF_00770

Pathway

Carbohydrate degradation; L-rhamnose degradation; glycerone phosphate from L-rhamnose: step 3/3. HAMAP MF_00770

Subunit structure

Homotetramer By similarity. HAMAP MF_00770

Subcellular location

Cytoplasm By similarity HAMAP MF_00770.

Sequence similarities

Belongs to the aldolase class II family. RhaD subfamily.

Ontologies

Keywords
   Biological processRhamnose metabolism
   Cellular componentCytoplasm
   LigandMetal-binding
Zinc
   Molecular functionLyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processrhamnose metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

rhamnulose-1-phosphate aldolase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 274274Rhamnulose-1-phosphate aldolase HAMAP MF_00770
PRO_1000017345

Sites

Active site1171 By similarity
Metal binding1411Zinc By similarity
Metal binding1431Zinc By similarity
Metal binding2121Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3YV74 [UniParc].

Last modified September 27, 2005. Version 1.
Checksum: F41C09D12BD3C24C

FASTA27430,006
        10         20         30         40         50         60 
MQNITQSWFV QGMIKATTDA WLKGWDERNG GNLTLRLDDA DIAPYHGNFH AQPRYIPLSQ 

        70         80         90        100        110        120 
PMPLLANTPF IVTGSGKFFR NVQLDPAANL GVVKVDSDGA GYHILWGLTN EAVPTSELPA 

       130        140        150        160        170        180 
HFLSHCERIK ATNGKDRVIM HCHATNLIAL TYVLENDTAV FTRQLWEGST ECLVVFPDGV 

       190        200        210        220        230        240 
GILPWMVPGT DEIGQATAQE MQKHSLVLWP FHGVFGSGST LDETFGLIDT AEKSAQVLVK 

       250        260        270 
VYSMGGMKQT ISREELIALG KRFGVTPLAS ALAL 

« 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: 16275786] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ss046.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000038 Genomic DNA. Translation: AAZ90588.1.
RefSeqYP_312823.1. NC_007384.1.

3D structure databases

ProteinModelPortalQ3YV74.
SMRQ3YV74. Positions 1-274.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3YV74.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000099767; EBESCP00000095796; EBESCG00000098811.
GeneID3669534.
GenomeReviewsGene locus SSON_4072 in contig CP000038_GR.
KEGGssn:SSON_4072.
PATRIC18743122. VBIShiSon107113_4836.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0235.
GeneTreeEBGT00050000009231.
HOGENOMHBG416653.
OMATRTLWQM.
PhylomeDBQ3YV74.
ProtClustDBPRK03634.

Enzyme and pathway databases

BioCycSSON300269:SSO_4072-MONOMER.

Family and domain databases

HAMAPMF_00770. RhaD.
[Tree]
InterProIPR001303. Aldolase_II/adducin_N.
IPR013447. Rhamnulose-1-P_Aldolase.
[Graphical view]
Gene3DG3DSA:3.40.225.10. Aldolase_II/adducin_N. 1 hit.
KOK01629.
PfamPF00596. Aldolase_II. 1 hit.
[Graphical view]
SMARTSM01007. Aldolase_II. 1 hit.
[Graphical view]
SUPFAMSSF53639. Aldolase_II_N. 1 hit.
TIGRFAMsTIGR02624. Rhamnu_1P_ald. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRHAD_SHISS
AccessionPrimary (citable) accession number: Q3YV74
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: September 27, 2005
Last modified: January 25, 2012
This is version 43 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