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Protein

L-rhamnose mutarotase

Gene

rhaM

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the anomeric conversion of L-rhamnose.1 Publication

Catalytic activityi

Alpha-L-rhamnopyranose = beta-L-rhamnopyranose.2 Publications

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei18 – 181Substrate
Active sitei22 – 221Proton donorCurated
Binding sitei41 – 411Substrate

GO - Molecular functioni

  1. racemase and epimerase activity, acting on carbohydrates and derivatives Source: EcoCyc

GO - Biological processi

  1. rhamnose catabolic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Carbohydrate metabolism, Rhamnose metabolism

Enzyme and pathway databases

BioCyciEcoCyc:EG11865-MONOMER.
ECOL316407:JW3872-MONOMER.
MetaCyc:EG11865-MONOMER.
UniPathwayiUPA00125.

Names & Taxonomyi

Protein namesi
Recommended name:
L-rhamnose mutarotase (EC:5.1.3.322 Publications)
Alternative name(s):
Rhamnose 1-epimerase
Type-3 mutarotase
Gene namesi
Name:rhaM
Synonyms:yiiL
Ordered Locus Names:b3901, JW3872
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG11865. rhaM.

Subcellular locationi

Cytoplasm Curated

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi18 – 181Y → F: Loss of mutarotase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 104104L-rhamnose mutarotasePRO_0000169687Add
BLAST

Expressioni

Gene expression databases

GenevestigatoriP32156.

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
gloAP0AC811EBI-1134000,EBI-551143

Protein-protein interaction databases

IntActiP32156. 2 interactions.
STRINGi511145.b3901.

Structurei

Secondary structure

1
104
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 98Combined sources
Helixi15 – 206Combined sources
Turni21 – 244Combined sources
Helixi27 – 359Combined sources
Beta strandi38 – 469Combined sources
Turni47 – 504Combined sources
Beta strandi51 – 599Combined sources
Helixi61 – 666Combined sources
Helixi67 – 693Combined sources
Helixi71 – 8010Combined sources
Turni81 – 833Combined sources
Beta strandi94 – 963Combined sources
Beta strandi98 – 1036Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X8DX-ray1.80A/B/C/D1-104[»]
ProteinModelPortaliP32156.
SMRiP32156. Positions 1-104.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32156.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni76 – 772Substrate binding

Sequence similaritiesi

Belongs to the rhamnose mutarotase family.Curated

Phylogenomic databases

eggNOGiCOG3254.
HOGENOMiHOG000250144.
InParanoidiP32156.
KOiK03534.
OMAiWAYMADI.
OrthoDBiEOG64NB3R.
PhylomeDBiP32156.

Family and domain databases

HAMAPiMF_01663. L_rham_rotase.
InterProiIPR011008. Dimeric_a/b-barrel.
IPR013448. L-rhamnose_1-epimerase.
IPR008000. Rhamnose_mutarotase.
[Graphical view]
PfamiPF05336. DUF718. 1 hit.
[Graphical view]
SUPFAMiSSF54909. SSF54909. 1 hit.
TIGRFAMsiTIGR02625. YiiL_rotase. 1 hit.

Sequencei

Sequence statusi: Complete.

P32156-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MIRKAFVMQV NPDAHEEYQR RHNPIWPELE AVLKSHGAHN YAIYLDKARN
60 70 80 90 100
LLFAMVEIES EERWNAVAST DVCQRWWKYM TDVMPANPDN SPVSSELQEV

FYLP
Length:104
Mass (Da):12,265
Last modified:October 1, 1993 - v1
Checksum:i6A276C08E0EEC7E2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L19201 Genomic DNA. Translation: AAB03034.1.
U00096 Genomic DNA. Translation: AAC76883.1.
AP009048 Genomic DNA. Translation: BAE77408.1.
PIRiS40845.
RefSeqiNP_418337.1. NC_000913.3.
YP_491549.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76883; AAC76883; b3901.
BAE77408; BAE77408; BAE77408.
GeneIDi12933648.
948402.
KEGGiecj:Y75_p3285.
eco:b3901.
PATRICi32123311. VBIEscCol129921_4016.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L19201 Genomic DNA. Translation: AAB03034.1.
U00096 Genomic DNA. Translation: AAC76883.1.
AP009048 Genomic DNA. Translation: BAE77408.1.
PIRiS40845.
RefSeqiNP_418337.1. NC_000913.3.
YP_491549.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X8DX-ray1.80A/B/C/D1-104[»]
ProteinModelPortaliP32156.
SMRiP32156. Positions 1-104.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP32156. 2 interactions.
STRINGi511145.b3901.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76883; AAC76883; b3901.
BAE77408; BAE77408; BAE77408.
GeneIDi12933648.
948402.
KEGGiecj:Y75_p3285.
eco:b3901.
PATRICi32123311. VBIEscCol129921_4016.

Organism-specific databases

EchoBASEiEB1811.
EcoGeneiEG11865. rhaM.

Phylogenomic databases

eggNOGiCOG3254.
HOGENOMiHOG000250144.
InParanoidiP32156.
KOiK03534.
OMAiWAYMADI.
OrthoDBiEOG64NB3R.
PhylomeDBiP32156.

Enzyme and pathway databases

UniPathwayiUPA00125.
BioCyciEcoCyc:EG11865-MONOMER.
ECOL316407:JW3872-MONOMER.
MetaCyc:EG11865-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP32156.
PROiP32156.

Gene expression databases

GenevestigatoriP32156.

Family and domain databases

HAMAPiMF_01663. L_rham_rotase.
InterProiIPR011008. Dimeric_a/b-barrel.
IPR013448. L-rhamnose_1-epimerase.
IPR008000. Rhamnose_mutarotase.
[Graphical view]
PfamiPF05336. DUF718. 1 hit.
[Graphical view]
SUPFAMiSSF54909. SSF54909. 1 hit.
TIGRFAMsiTIGR02625. YiiL_rotase. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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, CATALYTIC ACTIVITY.
  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, CATALYTIC ACTIVITY, SUBUNIT, MUTAGENESIS OF TYR-18, REACTION MECHANISM.

Entry informationi

Entry nameiRHAM_ECOLI
AccessioniPrimary (citable) accession number: P32156
Secondary accession number(s): Q2M8J8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: January 7, 2015
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.