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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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi226 – 2261Zinc
Metal bindingi259 – 2591Zinc
Metal bindingi262 – 2621Manganese
Metal bindingi286 – 2861Zinc
Metal bindingi294 – 2941Manganese
Metal bindingi296 – 2961Manganese
Metal bindingi326 – 3261Zinc

GO - Molecular functioni

  1. identical protein binding Source: EcoCyc
  2. L-rhamnose isomerase activity Source: EcoCyc
  3. manganese ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. L-lyxose metabolic process Source: EcoCyc
  2. 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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11867. rhaA.

Subcellular locationi

Cytoplasm Curated

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 419419L-rhamnose isomerasePRO_0000090552Add
BLAST

Proteomic databases

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

Gene expression databases

GenevestigatoriP32170.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

DIPiDIP-10690N.
STRINGi511145.b3903.

Structurei

Secondary structure

1
419
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1815Combined sources
Helixi23 – 308Combined sources
Beta strandi35 – 384Combined sources
Helixi39 – 424Combined sources
Turni43 – 453Combined sources
Beta strandi48 – 536Combined sources
Helixi72 – 8413Combined sources
Beta strandi90 – 956Combined sources
Helixi96 – 983Combined sources
Helixi107 – 1093Combined sources
Helixi112 – 1154Combined sources
Helixi116 – 1249Combined sources
Beta strandi128 – 1325Combined sources
Beta strandi136 – 1383Combined sources
Helixi139 – 1413Combined sources
Helixi152 – 17625Combined sources
Beta strandi180 – 1845Combined sources
Beta strandi189 – 1924Combined sources
Helixi198 – 21114Combined sources
Turni218 – 2203Combined sources
Beta strandi221 – 2266Combined sources
Beta strandi236 – 2405Combined sources
Helixi242 – 25211Combined sources
Beta strandi255 – 2595Combined sources
Helixi269 – 2768Combined sources
Turni277 – 2793Combined sources
Beta strandi283 – 2875Combined sources
Beta strandi291 – 2944Combined sources
Helixi303 – 31412Combined sources
Turni318 – 3203Combined sources
Beta strandi321 – 3255Combined sources
Helixi334 – 35320Combined sources
Helixi357 – 3648Combined sources
Turni365 – 3673Combined sources
Helixi369 – 37911Combined sources
Helixi384 – 39411Combined sources
Helixi403 – 41311Combined sources
Turni414 – 4163Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 3-418.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32170.

Family & Domainsi

Sequence similaritiesi

Belongs to the rhamnose isomerase family.Curated

Phylogenomic databases

eggNOGiCOG4806.
HOGENOMiHOG000269679.
InParanoidiP32170.
KOiK01813.
OMAiISLHCWQ.
OrthoDBiEOG6KMB74.
PhylomeDBiP32170.

Family and domain databases

Gene3Di3.20.20.150. 1 hit.
HAMAPiMF_00541. RhaA.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti359 – 3602EL → DV in AAB03036 (PubMed:8346018).Curated
Sequence conflicti366 – 3661A → P in CAA43002 (PubMed:8396120).Curated

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.
RefSeqiYP_026276.1. NC_000913.3.
YP_491547.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAT48234; AAT48234; b3903.
BAE77406; BAE77406; BAE77406.
GeneIDi12931684.
948400.
KEGGiecj:Y75_p3283.
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.
RefSeqiYP_026276.1. NC_000913.3.
YP_491547.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 3-418.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-10690N.
STRINGi511145.b3903.

Proteomic databases

PRIDEiP32170.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAT48234; AAT48234; b3903.
BAE77406; BAE77406; BAE77406.
GeneIDi12931684.
948400.
KEGGiecj:Y75_p3283.
eco:b3903.
PATRICi32123315. VBIEscCol129921_4018.

Organism-specific databases

EchoBASEiEB1813.
EcoGeneiEG11867. rhaA.

Phylogenomic databases

eggNOGiCOG4806.
HOGENOMiHOG000269679.
InParanoidiP32170.
KOiK01813.
OMAiISLHCWQ.
OrthoDBiEOG6KMB74.
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.

Gene expression databases

GenevestigatoriP32170.

Family and domain databases

Gene3Di3.20.20.150. 1 hit.
HAMAPiMF_00541. RhaA.
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...

Publicationsi

« Hide 'large scale' publications
  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(1992) [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(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. 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(2005) [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(1992) [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(1999) [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(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), SUBUNIT.

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: January 7, 2015
This is version 129 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

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.