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P32156 (RHAM_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 102. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
L-rhamnose mutarotase

EC=5.1.3.n3
Alternative name(s):
Rhamnose 1-epimerase
Type-3 mutarotase
Gene names
Name:rhaM
Synonyms:yiiL
Ordered Locus Names:b3901, JW3872
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length104 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the anomeric conversion of L-rhamnose. Ref.4

Catalytic activity

Alpha-L-rhamnose = beta-L-rhamnose. HAMAP-Rule MF_01663

Pathway

Carbohydrate metabolism; L-rhamnose metabolism. HAMAP-Rule MF_01663

Subunit structure

Homodimer. Ref.5

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_01663.

Sequence similarities

Belongs to the rhamnose mutarotase family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Rhamnose metabolism
   Cellular componentCytoplasm
   Molecular functionIsomerase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processrhamnose catabolic process

Inferred from mutant phenotype Ref.5. Source: EcoCyc

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionracemase and epimerase activity, acting on carbohydrates and derivatives

Inferred from direct assay Ref.4. Source: EcoCyc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

gloAP0AC811EBI-1134000,EBI-551143

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 104104L-rhamnose mutarotase HAMAP-Rule MF_01663
PRO_0000169687

Regions

Region76 – 772Substrate binding HAMAP-Rule MF_01663

Sites

Active site221Proton donor Probable
Binding site181Substrate
Binding site411Substrate

Experimental info

Mutagenesis181Y → F: Loss of mutarotase activity. Ref.5

Secondary structure

...................... 104
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P32156 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: 6A276C08E0EEC7E2

FASTA10412,265
        10         20         30         40         50         60 
MIRKAFVMQV NPDAHEEYQR RHNPIWPELE AVLKSHGAHN YAIYLDKARN LLFAMVEIES 

        70         80         90        100 
EERWNAVAST DVCQRWWKYM TDVMPANPDN SPVSSELQEV FYLP 

« Hide

References

« Hide 'large scale' references
[1]"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.
[2]"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.
[3]"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.
[4]"NMR application probes a novel and ubiquitous family of enzymes that alter monosaccharide configuration."
Ryu K.-S., Kim C., Kim I., Yoo S., Choi B.-S., Park C.
J. Biol. Chem. 279:25544-25548(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A MUTAROTASE.
[5]"Structural insights into the monosaccharide specificity of Escherichia coli rhamnose mutarotase."
Ryu K.-S., Kim J.-I., Cho S.-J., Park D., Park C., Cheong H.-K., Lee J.-O., Choi B.-S.
J. Mol. Biol. 349:153-162(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH L-RHAMNOSE, SUBUNIT, MUTAGENESIS OF TYR-18, REACTION MECHANISM.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L19201 Genomic DNA. Translation: AAB03034.1.
U00096 Genomic DNA. Translation: AAC76883.1.
AP009048 Genomic DNA. Translation: BAE77408.1.
PIRS40845.
RefSeqNP_418337.1. NC_000913.3.
YP_491549.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1X8DX-ray1.80A/B/C/D1-104[»]
ProteinModelPortalP32156.
SMRP32156. Positions 1-104.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP32156. 2 interactions.
STRING511145.b3901.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76883; AAC76883; b3901.
BAE77408; BAE77408; BAE77408.
GeneID12933648.
948402.
KEGGecj:Y75_p3285.
eco:b3901.
PATRIC32123311. VBIEscCol129921_4016.

Organism-specific databases

EchoBASEEB1811.
EcoGeneEG11865. rhaM.

Phylogenomic databases

eggNOGCOG3254.
HOGENOMHOG000250144.
KOK03534.
OMAKRHDEIW.
OrthoDBEOG64NB3R.
PhylomeDBP32156.
ProtClustDBCLSK880814.

Enzyme and pathway databases

BioCycEcoCyc:EG11865-MONOMER.
ECOL316407:JW3872-MONOMER.
MetaCyc:EG11865-MONOMER.
UniPathwayUPA00125.

Gene expression databases

GenevestigatorP32156.

Family and domain databases

HAMAPMF_01663. L_rham_rotase.
InterProIPR011008. Dimeric_a/b-barrel.
IPR013448. L-rhamnose_1-epimerase.
IPR008000. Rhamnose_mutarotase.
[Graphical view]
PfamPF05336. DUF718. 1 hit.
[Graphical view]
SUPFAMSSF54909. SSF54909. 1 hit.
TIGRFAMsTIGR02625. YiiL_rotase. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP32156.
PROP32156.

Entry information

Entry nameRHAM_ECOLI
AccessionPrimary (citable) accession number: P32156
Secondary accession number(s): Q2M8J8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: April 16, 2014
This is version 102 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