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Protein

L-rhamnose isomerase

Gene

rhaA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

L-rhamnopyranose = L-rhamnulose.

Cofactori

Mn2+Note: Binds 1 Mn2+ ion per subunit.

Pathwayi: L-rhamnose degradation

This protein is involved in step 1 of the subpathway that synthesizes glycerone phosphate from L-rhamnose.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. L-rhamnose isomerase (rhaA)
  2. L-Rhamnulokinase (rhaB)
  3. Rhamnulose-1-phosphate aldolase (rhaD)
This subpathway is part of the pathway L-rhamnose degradation, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes glycerone phosphate from L-rhamnose, the pathway L-rhamnose degradation and in Carbohydrate degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi226Zinc1
Metal bindingi259Zinc1
Metal bindingi262Manganese1
Metal bindingi286Zinc1
Metal bindingi294Manganese1
Metal bindingi296Manganese1
Metal bindingi326Zinc1

GO - Molecular functioni

  • identical protein binding Source: EcoCyc
  • L-rhamnose isomerase activity Source: EcoCyc
  • manganese ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  • L-lyxose metabolic process Source: EcoCyc
  • rhamnose catabolic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Rhamnose metabolism

Keywords - Ligandi

Manganese, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:RHAMNISOM-MONOMER.
ECOL316407:JW5561-MONOMER.
MetaCyc:RHAMNISOM-MONOMER.
BRENDAi5.3.1.14. 2026.
UniPathwayiUPA00541; UER00601.

Names & Taxonomyi

Protein namesi
Recommended name:
L-rhamnose isomerase (EC:5.3.1.14)
Gene namesi
Name:rhaA
Ordered Locus Names:b3903, JW5561
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11867. rhaA.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000905521 – 419L-rhamnose isomeraseAdd BLAST419

Proteomic databases

PaxDbiP32170.
PRIDEiP32170.

Expressioni

Inductioni

Induced by L-rhamnose via the RhaR-RhaS regulatory cascade. Binding of the cAMP receptor protein (CRP) is required for full expression.2 Publications

Interactioni

Subunit structurei

Homotetramer.1 Publication

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

DIPiDIP-10690N.
STRINGi511145.b3903.

Structurei

Secondary structure

1419
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 18Combined sources15
Helixi23 – 30Combined sources8
Beta strandi35 – 38Combined sources4
Helixi39 – 42Combined sources4
Turni43 – 45Combined sources3
Beta strandi48 – 53Combined sources6
Helixi72 – 84Combined sources13
Beta strandi90 – 95Combined sources6
Helixi96 – 98Combined sources3
Helixi107 – 109Combined sources3
Helixi112 – 115Combined sources4
Helixi116 – 124Combined sources9
Beta strandi128 – 132Combined sources5
Beta strandi136 – 138Combined sources3
Helixi139 – 141Combined sources3
Helixi152 – 176Combined sources25
Beta strandi180 – 184Combined sources5
Beta strandi189 – 192Combined sources4
Helixi198 – 211Combined sources14
Turni218 – 220Combined sources3
Beta strandi221 – 226Combined sources6
Beta strandi236 – 240Combined sources5
Helixi242 – 252Combined sources11
Beta strandi255 – 259Combined sources5
Helixi269 – 276Combined sources8
Turni277 – 279Combined sources3
Beta strandi283 – 287Combined sources5
Beta strandi291 – 294Combined sources4
Helixi303 – 314Combined sources12
Turni318 – 320Combined sources3
Beta strandi321 – 325Combined sources5
Helixi334 – 353Combined sources20
Helixi357 – 364Combined sources8
Turni365 – 367Combined sources3
Helixi369 – 379Combined sources11
Helixi384 – 394Combined sources11
Helixi403 – 413Combined sources11
Turni414 – 416Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1D8WX-ray1.60A/B/C/D1-419[»]
1DE5X-ray2.20A/B/C/D1-419[»]
1DE6X-ray2.10A/B/C/D1-419[»]
DisProtiDP00429.
ProteinModelPortaliP32170.
SMRiP32170.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32170.

Family & Domainsi

Sequence similaritiesi

Belongs to the rhamnose isomerase family.Curated

Phylogenomic databases

eggNOGiENOG4105DKG. Bacteria.
COG4806. LUCA.
HOGENOMiHOG000269679.
InParanoidiP32170.
KOiK01813.
OMAiVNLHAIY.
PhylomeDBiP32170.

Family and domain databases

Gene3Di3.20.20.150. 1 hit.
HAMAPiMF_00541. RhaA. 1 hit.
InterProiIPR009308. Rhamnose_isomerase.
IPR013022. Xyl_isomerase-like_TIM-brl.
[Graphical view]
PfamiPF06134. RhaA. 1 hit.
[Graphical view]
SUPFAMiSSF51658. SSF51658. 1 hit.
TIGRFAMsiTIGR01748. rhaA. 1 hit.

Sequencei

Sequence statusi: Complete.

P32170-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTQLEQAWE LAKQRFAAVG IDVEEALRQL DRLPVSMHCW QGDDVSGFEN
60 70 80 90 100
PEGSLTGGIQ ATGNYPGKAR NASELRADLE QAMRLIPGPK RLNLHAIYLE
110 120 130 140 150
SDTPVSRDQI KPEHFKNWVE WAKANQLGLD FNPSCFSHPL SADGFTLSHA
160 170 180 190 200
DDSIRQFWID HCKASRRVSA YFGEQLGTPS VMNIWIPDGM KDITVDRLAP
210 220 230 240 250
RQRLLAALDE VISEKLNPAH HIDAVESKLF GIGAESYTVG SNEFYMGYAT
260 270 280 290 300
SRQTALCLDA GHFHPTEVIS DKISAAMLYV PQLLLHVSRP VRWDSDHVVL
310 320 330 340 350
LDDETQAIAS EIVRHDLFDR VHIGLDFFDA SINRIAAWVI GTRNMKKALL
360 370 380 390 400
RALLEPTAEL RKLEAAGDYT ARLALLEEQK SLPWQAVWEM YCQRHDTPAG
410
SEWLESVRAY EKEILSRRG
Length:419
Mass (Da):47,199
Last modified:October 11, 2004 - v2
Checksum:iD237E95BD24999BA
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti359 – 360EL → DV in AAB03036 (PubMed:8346018).Curated2
Sequence conflicti366A → P in CAA43002 (PubMed:8396120).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60472 Genomic DNA. Translation: CAA43002.1.
L19201 Genomic DNA. Translation: AAB03036.1.
U00096 Genomic DNA. Translation: AAT48234.1.
AP009048 Genomic DNA. Translation: BAE77406.1.
PIRiS40847.
RefSeqiWP_001311268.1. NZ_LN832404.1.
YP_026276.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAT48234; AAT48234; b3903.
BAE77406; BAE77406; BAE77406.
GeneIDi948400.
KEGGiecj:JW5561.
eco:b3903.
PATRICi32123315. VBIEscCol129921_4018.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60472 Genomic DNA. Translation: CAA43002.1.
L19201 Genomic DNA. Translation: AAB03036.1.
U00096 Genomic DNA. Translation: AAT48234.1.
AP009048 Genomic DNA. Translation: BAE77406.1.
PIRiS40847.
RefSeqiWP_001311268.1. NZ_LN832404.1.
YP_026276.1. NC_000913.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1D8WX-ray1.60A/B/C/D1-419[»]
1DE5X-ray2.20A/B/C/D1-419[»]
1DE6X-ray2.10A/B/C/D1-419[»]
DisProtiDP00429.
ProteinModelPortaliP32170.
SMRiP32170.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-10690N.
STRINGi511145.b3903.

Proteomic databases

PaxDbiP32170.
PRIDEiP32170.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAT48234; AAT48234; b3903.
BAE77406; BAE77406; BAE77406.
GeneIDi948400.
KEGGiecj:JW5561.
eco:b3903.
PATRICi32123315. VBIEscCol129921_4018.

Organism-specific databases

EchoBASEiEB1813.
EcoGeneiEG11867. rhaA.

Phylogenomic databases

eggNOGiENOG4105DKG. Bacteria.
COG4806. LUCA.
HOGENOMiHOG000269679.
InParanoidiP32170.
KOiK01813.
OMAiVNLHAIY.
PhylomeDBiP32170.

Enzyme and pathway databases

UniPathwayiUPA00541; UER00601.
BioCyciEcoCyc:RHAMNISOM-MONOMER.
ECOL316407:JW5561-MONOMER.
MetaCyc:RHAMNISOM-MONOMER.
BRENDAi5.3.1.14. 2026.

Miscellaneous databases

EvolutionaryTraceiP32170.
PROiP32170.

Family and domain databases

Gene3Di3.20.20.150. 1 hit.
HAMAPiMF_00541. RhaA. 1 hit.
InterProiIPR009308. Rhamnose_isomerase.
IPR013022. Xyl_isomerase-like_TIM-brl.
[Graphical view]
PfamiPF06134. RhaA. 1 hit.
[Graphical view]
SUPFAMiSSF51658. SSF51658. 1 hit.
TIGRFAMsiTIGR01748. rhaA. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRHAA_ECOLI
AccessioniPrimary (citable) accession number: P32170
Secondary accession number(s): Q2M8K0, Q6BEY0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 11, 2004
Last modified: November 2, 2016
This is version 136 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.

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.