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P32169 (RHAD_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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
Synonyms:rhuA
Ordered Locus Names:b3902, JW3873
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length274 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

Binds 1 zinc ion per subunit.

Pathway

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

Subunit structure

Homotetramer.

Subcellular location

Cytoplasm HAMAP-Rule MF_00770.

Induction

Induced by L-rhamnose via the RhaR-RhaS regulatory cascade. Binding of the cAMP receptor protein (CRP) is required for full expression. Ref.5 Ref.7

Sequence similarities

Belongs to the aldolase class II family. RhaD subfamily.

Ontologies

Keywords
   Biological processRhamnose metabolism
   Cellular componentCytoplasm
   LigandMetal-binding
Zinc
   Molecular functionLyase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processrhamnose catabolic process

Inferred from mutant phenotype PubMed 5341476. Source: EcoCyc

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionidentical protein binding

Inferred from direct assay PubMed 4975916. Source: EcoCyc

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

rhamnulose-1-phosphate aldolase activity

Inferred from direct assay PubMed 4975916. Source: EcoCyc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 274274Rhamnulose-1-phosphate aldolase HAMAP-Rule MF_00770
PRO_0000209657

Sites

Active site1171
Metal binding1411Zinc
Metal binding1431Zinc
Metal binding2121Zinc

Secondary structure

...................................................... 274
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P32169 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: F9FF0BE156F4E63D

FASTA27430,145
        10         20         30         40         50         60 
MQNITQSWFV QGMIKATTDA WLKGWDERNG GNLTLRLDDA DIAPYHDNFH QQPRYIPLSQ 

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

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

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

       250        260        270 
VYSMGGMKQT ISREELIALG KRFGVTPLAS ALAL 

« Hide

References

« Hide 'large scale' references
[1]"Sequencing and characterization of a gene cluster encoding the enzymes for L-rhamnose metabolism in Escherichia coli."
Moralejo P., Egan S.M., Hidalgo E.F., Aguilar J.
J. Bacteriol. 175:5585-5594(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes."
Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.
Nucleic Acids Res. 21:3391-3398(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"A regulatory cascade in the induction of rhaBAD."
Egan S.M., Schleif R.F.
J. Mol. Biol. 234:87-98(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
Strain: ECL116.
[6]"Escherichia coli proteome analysis using the gene-protein database."
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY 2D-GEL.
[7]"Roles of cyclic AMP receptor protein and the carboxyl-terminal domain of the alpha subunit in transcription activation of the Escherichia coli rhaBAD operon."
Holcroft C.C., Egan S.M.
J. Bacteriol. 182:3529-3535(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[8]"The structure of L-rhamnulose-1-phosphate aldolase (class II) solved by low-resolution SIR phasing and 20-fold NCS averaging."
Kroemer M., Schulz G.E.
Acta Crystallogr. D 58:824-832(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
[9]"Structure and catalytic mechanism of L-rhamnulose-1-phosphate aldolase."
Kroemer M., Merkel I., Schulz G.E.
Biochemistry 42:10560-10568(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X60472 Genomic DNA. Translation: CAA43003.1.
L19201 Genomic DNA. Translation: AAB03035.1.
U00096 Genomic DNA. Translation: AAC76884.1.
AP009048 Genomic DNA. Translation: BAE77407.1.
PIRC48649.
RefSeqNP_418338.1. NC_000913.3.
YP_491548.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GT7X-ray2.70A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T1-274[»]
1OJRX-ray1.35A1-274[»]
2UYUX-ray1.96A/E1-274[»]
2UYVX-ray2.20A/B/C/D1-274[»]
2V29X-ray2.03A/B1-274[»]
2V2AX-ray1.75A1-274[»]
2V2BX-ray1.50A1-274[»]
2V9EX-ray1.58A/B1-272[»]
2V9FX-ray2.10A1-272[»]
2V9GX-ray2.70A/B/C/D1-274[»]
2V9IX-ray1.80A/B1-273[»]
2V9LX-ray1.23A1-274[»]
2V9MX-ray1.30A/B1-274[»]
2V9NX-ray1.40A/B/C/D1-274[»]
2V9OX-ray1.95A/E1-274[»]
ProteinModelPortalP32169.
SMRP32169. Positions 1-274.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP32169. 7 interactions.
STRING511145.b3902.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76884; AAC76884; b3902.
BAE77407; BAE77407; BAE77407.
GeneID12931682.
948401.
KEGGecj:Y75_p3284.
eco:b3902.
PATRIC32123313. VBIEscCol129921_4017.

Organism-specific databases

EchoBASEEB1812.
EcoGeneEG11866. rhaD.

Phylogenomic databases

eggNOGCOG0235.
HOGENOMHOG000279628.
KOK01629.
OMADMWLKGW.
OrthoDBEOG61GGBF.
PhylomeDBP32169.

Enzyme and pathway databases

BioCycEcoCyc:RHAMNULPALDOL-MONOMER.
ECOL316407:JW3873-MONOMER.
MetaCyc:RHAMNULPALDOL-MONOMER.
UniPathwayUPA00541; UER00603.

Gene expression databases

GenevestigatorP32169.

Family and domain databases

Gene3D3.40.225.10. 1 hit.
HAMAPMF_00770. RhaD.
InterProIPR001303. Aldolase_II/adducin_N.
IPR013447. Rhamnulose-1-P_Aldolase.
[Graphical view]
PfamPF00596. Aldolase_II. 1 hit.
[Graphical view]
SMARTSM01007. Aldolase_II. 1 hit.
[Graphical view]
SUPFAMSSF53639. SSF53639. 1 hit.
TIGRFAMsTIGR02624. rhamnu_1P_ald. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP32169.
PROP32169.

Entry information

Entry nameRHAD_ECOLI
AccessionPrimary (citable) accession number: P32169
Secondary accession number(s): Q2M8J9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: July 9, 2014
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene