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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: L-rhamnose metabolism

This protein is involved in the pathway L-rhamnose metabolism, which is part of Carbohydrate metabolism.
View all proteins of this organism that are known to be involved in the pathway L-rhamnose metabolism and in Carbohydrate metabolism.

Sites

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

GO - Molecular functioni

GO - Biological processi

  • 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.
BRENDAi5.1.3.32. 2026.
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
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11865. rhaM.

Subcellular locationi

GO - Cellular componenti

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

Proteomic databases

PaxDbiP32156.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi4262642. 28 interactions.
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

eggNOGiENOG4105M10. Bacteria.
COG3254. LUCA.
HOGENOMiHOG000250144.
InParanoidiP32156.
KOiK03534.
OMAiKRHDEIW.
PhylomeDBiP32156.

Family and domain databases

HAMAPiMF_01663. L_rham_rotase. 1 hit.
InterProiIPR011008. Dimeric_a/b-barrel.
IPR013448. L-rhamnose_mutarotase_rhaM.
IPR008000. Rham/fucose_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.
WP_000619493.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76883; AAC76883; b3901.
BAE77408; BAE77408; BAE77408.
GeneIDi948402.
KEGGiecj:JW3872.
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.
WP_000619493.1. NZ_LN832404.1.

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

BioGridi4262642. 28 interactions.
IntActiP32156. 2 interactions.
STRINGi511145.b3901.

Proteomic databases

PaxDbiP32156.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76883; AAC76883; b3901.
BAE77408; BAE77408; BAE77408.
GeneIDi948402.
KEGGiecj:JW3872.
eco:b3901.
PATRICi32123311. VBIEscCol129921_4016.

Organism-specific databases

EchoBASEiEB1811.
EcoGeneiEG11865. rhaM.

Phylogenomic databases

eggNOGiENOG4105M10. Bacteria.
COG3254. LUCA.
HOGENOMiHOG000250144.
InParanoidiP32156.
KOiK03534.
OMAiKRHDEIW.
PhylomeDBiP32156.

Enzyme and pathway databases

UniPathwayiUPA00125.
BioCyciEcoCyc:EG11865-MONOMER.
ECOL316407:JW3872-MONOMER.
MetaCyc:EG11865-MONOMER.
BRENDAi5.1.3.32. 2026.

Miscellaneous databases

EvolutionaryTraceiP32156.
PROiP32156.

Family and domain databases

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

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: September 7, 2016
This is version 119 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

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 one 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.