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P32170 (RHAA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 124. 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:
L-rhamnose isomerase

EC=5.3.1.14
Gene names
Name:rhaA
Ordered Locus Names:b3903, JW5561
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length419 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

L-rhamnopyranose = L-rhamnulose. HAMAP-Rule MF_00541

Cofactor

Binds 1 manganese ion per subunit.

Pathway

Carbohydrate degradation; L-rhamnose degradation; glycerone phosphate from L-rhamnose: step 1/3. HAMAP-Rule MF_00541

Subunit structure

Homotetramer. Ref.8

Subcellular location

Cytoplasm Probable HAMAP-Rule MF_00541.

Induction

Induced by L-rhamnose via the RhaR-RhaS regulatory cascade. Binding of the cAMP receptor protein (CRP) is required for full expression. Ref.6 Ref.7

Miscellaneous

In the crystal structure, RhaA appears to bind a zinc ion at a structural site. However, the metal ion may be different in vivo.

Sequence similarities

Belongs to the rhamnose isomerase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 419419L-rhamnose isomerase HAMAP-Rule MF_00541
PRO_0000090552

Sites

Metal binding2261Zinc
Metal binding2591Zinc
Metal binding2621Manganese
Metal binding2861Zinc
Metal binding2941Manganese
Metal binding2961Manganese
Metal binding3261Zinc

Experimental info

Sequence conflict359 – 3602EL → DV in AAB03036. Ref.2
Sequence conflict3661A → P in CAA43002. Ref.1

Secondary structure

................................................................... 419
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P32170 [UniParc].

Last modified October 11, 2004. Version 2.
Checksum: D237E95BD24999BA

FASTA41947,199
        10         20         30         40         50         60 
MTTQLEQAWE LAKQRFAAVG IDVEEALRQL DRLPVSMHCW QGDDVSGFEN PEGSLTGGIQ 

        70         80         90        100        110        120 
ATGNYPGKAR NASELRADLE QAMRLIPGPK RLNLHAIYLE SDTPVSRDQI KPEHFKNWVE 

       130        140        150        160        170        180 
WAKANQLGLD FNPSCFSHPL SADGFTLSHA DDSIRQFWID HCKASRRVSA YFGEQLGTPS 

       190        200        210        220        230        240 
VMNIWIPDGM KDITVDRLAP RQRLLAALDE VISEKLNPAH HIDAVESKLF GIGAESYTVG 

       250        260        270        280        290        300 
SNEFYMGYAT SRQTALCLDA GHFHPTEVIS DKISAAMLYV PQLLLHVSRP VRWDSDHVVL 

       310        320        330        340        350        360 
LDDETQAIAS EIVRHDLFDR VHIGLDFFDA SINRIAAWVI GTRNMKKALL RALLEPTAEL 

       370        380        390        400        410 
RKLEAAGDYT ARLALLEEQK SLPWQAVWEM YCQRHDTPAG SEWLESVRAY EKEILSRRG 

« 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]"Escherichia coli K-12: a cooperatively developed annotation snapshot -- 2005."
Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R., Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T., Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H., Thomson N.R., Wishart D., Wanner B.L.
Nucleic Acids Res. 34:1-9(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION TO 359-360.
[5]"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.
[6]"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.
[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 rhamnose isomerase from Escherichia coli and its relation with xylose isomerase illustrates a change between inter and intra-subunit complementation during evolution."
Korndoerfer I.P., Fessner W.-D., Matthews B.W.
J. Mol. Biol. 300:917-933(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X60472 Genomic DNA. Translation: CAA43002.1.
L19201 Genomic DNA. Translation: AAB03036.1.
U00096 Genomic DNA. Translation: AAT48234.1.
AP009048 Genomic DNA. Translation: BAE77406.1.
PIRS40847.
RefSeqYP_026276.1. NC_000913.3.
YP_491547.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1D8WX-ray1.60A/B/C/D1-419[»]
1DE5X-ray2.20A/B/C/D1-419[»]
1DE6X-ray2.10A/B/C/D1-419[»]
DisProtDP00429.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-10690N.
STRING511145.b3903.

Proteomic databases

PRIDEP32170.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAT48234; AAT48234; b3903.
BAE77406; BAE77406; BAE77406.
GeneID12931684.
948400.
KEGGecj:Y75_p3283.
eco:b3903.
PATRIC32123315. VBIEscCol129921_4018.

Organism-specific databases

EchoBASEEB1813.
EcoGeneEG11867. rhaA.

Phylogenomic databases

eggNOGCOG4806.
HOGENOMHOG000269679.
KOK01813.
OMAIPVSMHC.
OrthoDBEOG6KMB74.
PhylomeDBP32170.

Enzyme and pathway databases

BioCycEcoCyc:RHAMNISOM-MONOMER.
ECOL316407:JW5561-MONOMER.
MetaCyc:RHAMNISOM-MONOMER.
BRENDA5.3.1.14. 2026.
UniPathwayUPA00541; UER00601.

Gene expression databases

GenevestigatorP32170.

Family and domain databases

Gene3D3.20.20.150. 1 hit.
HAMAPMF_00541. RhaA.
InterProIPR009308. Rhamnose_isomerase.
IPR013022. Xyl_isomerase-like_TIM-brl.
[Graphical view]
PfamPF06134. RhaA. 1 hit.
[Graphical view]
SUPFAMSSF51658. SSF51658. 1 hit.
TIGRFAMsTIGR01748. rhaA. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP32170.
PROP32170.

Entry information

Entry nameRHAA_ECOLI
AccessionPrimary (citable) accession number: P32170
Secondary accession number(s): Q2M8K0, Q6BEY0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 11, 2004
Last modified: July 9, 2014
This is version 124 of the entry and version 2 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