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P32170

- RHAA_ECOLI

UniProt

P32170 - RHAA_ECOLI

Protein

L-rhamnose isomerase

Gene

rhaA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 2 (11 Oct 2004)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    L-rhamnopyranose = L-rhamnulose.

    Cofactori

    Binds 1 manganese 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

    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: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG11867. rhaA.

    Subcellular locationi

    Cytoplasm Curated

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    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 – 1815
    Helixi23 – 308
    Beta strandi35 – 384
    Helixi39 – 424
    Turni43 – 453
    Beta strandi48 – 536
    Helixi72 – 8413
    Beta strandi90 – 956
    Helixi96 – 983
    Helixi107 – 1093
    Helixi112 – 1154
    Helixi116 – 1249
    Beta strandi128 – 1325
    Beta strandi136 – 1383
    Helixi139 – 1413
    Helixi152 – 17625
    Beta strandi180 – 1845
    Beta strandi189 – 1924
    Helixi198 – 21114
    Turni218 – 2203
    Beta strandi221 – 2266
    Beta strandi236 – 2405
    Helixi242 – 25211
    Beta strandi255 – 2595
    Helixi269 – 2768
    Turni277 – 2793
    Beta strandi283 – 2875
    Beta strandi291 – 2944
    Helixi303 – 31412
    Turni318 – 3203
    Beta strandi321 – 3255
    Helixi334 – 35320
    Helixi357 – 3648
    Turni365 – 3673
    Helixi369 – 37911
    Helixi384 – 39411
    Helixi403 – 41311
    Turni414 – 4163

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP32170.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the rhamnose isomerase family.Curated

    Phylogenomic databases

    eggNOGiCOG4806.
    HOGENOMiHOG000269679.
    KOiK01813.
    OMAiIPVSMHC.
    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

    MTTQLEQAWE LAKQRFAAVG IDVEEALRQL DRLPVSMHCW QGDDVSGFEN    50
    PEGSLTGGIQ ATGNYPGKAR NASELRADLE QAMRLIPGPK RLNLHAIYLE 100
    SDTPVSRDQI KPEHFKNWVE WAKANQLGLD FNPSCFSHPL SADGFTLSHA 150
    DDSIRQFWID HCKASRRVSA YFGEQLGTPS VMNIWIPDGM KDITVDRLAP 200
    RQRLLAALDE VISEKLNPAH HIDAVESKLF GIGAESYTVG SNEFYMGYAT 250
    SRQTALCLDA GHFHPTEVIS DKISAAMLYV PQLLLHVSRP VRWDSDHVVL 300
    LDDETQAIAS EIVRHDLFDR VHIGLDFFDA SINRIAAWVI GTRNMKKALL 350
    RALLEPTAEL RKLEAAGDYT ARLALLEEQK SLPWQAVWEM YCQRHDTPAG 400
    SEWLESVRAY EKEILSRRG 419
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi S40847.
    RefSeqi YP_026276.1. NC_000913.3.
    YP_491547.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1D8W X-ray 1.60 A/B/C/D 1-419 [» ]
    1DE5 X-ray 2.20 A/B/C/D 1-419 [» ]
    1DE6 X-ray 2.10 A/B/C/D 1-419 [» ]
    DisProti DP00429.
    ProteinModelPortali P32170.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-10690N.
    STRINGi 511145.b3903.

    Proteomic databases

    PRIDEi P32170.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAT48234 ; AAT48234 ; b3903 .
    BAE77406 ; BAE77406 ; BAE77406 .
    GeneIDi 12931684.
    948400.
    KEGGi ecj:Y75_p3283.
    eco:b3903.
    PATRICi 32123315. VBIEscCol129921_4018.

    Organism-specific databases

    EchoBASEi EB1813.
    EcoGenei EG11867. rhaA.

    Phylogenomic databases

    eggNOGi COG4806.
    HOGENOMi HOG000269679.
    KOi K01813.
    OMAi IPVSMHC.
    OrthoDBi EOG6KMB74.
    PhylomeDBi P32170.

    Enzyme and pathway databases

    UniPathwayi UPA00541 ; UER00601 .
    BioCyci EcoCyc:RHAMNISOM-MONOMER.
    ECOL316407:JW5561-MONOMER.
    MetaCyc:RHAMNISOM-MONOMER.
    BRENDAi 5.3.1.14. 2026.

    Miscellaneous databases

    EvolutionaryTracei P32170.
    PROi P32170.

    Gene expression databases

    Genevestigatori P32170.

    Family and domain databases

    Gene3Di 3.20.20.150. 1 hit.
    HAMAPi MF_00541. RhaA.
    InterProi IPR009308. Rhamnose_isomerase.
    IPR013022. Xyl_isomerase-like_TIM-brl.
    [Graphical view ]
    Pfami PF06134. RhaA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51658. SSF51658. 1 hit.
    TIGRFAMsi TIGR01748. rhaA. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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(1993) [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(1993) [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(2006) [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(1993) [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(2000) [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(2000) [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: October 1, 2014
    This is version 126 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