Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P32169

- RHAD_ECOLI

UniProt

P32169 - RHAD_ECOLI

Protein

Rhamnulose-1-phosphate aldolase

Gene

rhaD

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 1 (01 Oct 1993)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalyzes the reversible cleavage of L-rhamnulose-1-phosphate to dihydroxyacetone phosphate (DHAP) and L-lactaldehyde.

    Catalytic activityi

    L-rhamnulose 1-phosphate = glycerone phosphate + (S)-lactaldehyde.

    Cofactori

    Binds 1 zinc ion per subunit.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei117 – 1171
    Metal bindingi141 – 1411Zinc
    Metal bindingi143 – 1431Zinc
    Metal bindingi212 – 2121Zinc

    GO - Molecular functioni

    1. identical protein binding Source: EcoCyc
    2. metal ion binding Source: UniProtKB-KW
    3. rhamnulose-1-phosphate aldolase activity Source: EcoCyc

    GO - Biological processi

    1. rhamnose catabolic process Source: EcoCyc

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Rhamnose metabolism

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciEcoCyc:RHAMNULPALDOL-MONOMER.
    ECOL316407:JW3873-MONOMER.
    MetaCyc:RHAMNULPALDOL-MONOMER.
    UniPathwayiUPA00541; UER00603.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Rhamnulose-1-phosphate aldolase (EC:4.1.2.19)
    Gene namesi
    Name:rhaD
    Synonyms:rhuA
    Ordered Locus Names:b3902, JW3873
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG11866. rhaD.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 274274Rhamnulose-1-phosphate aldolasePRO_0000209657Add
    BLAST

    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

    GenevestigatoriP32169.

    Interactioni

    Subunit structurei

    Homotetramer.

    Protein-protein interaction databases

    IntActiP32169. 7 interactions.
    STRINGi511145.b3902.

    Structurei

    Secondary structure

    1
    274
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 63
    Helixi8 – 2215
    Beta strandi31 – 366
    Helixi39 – 424
    Helixi43 – 486
    Beta strandi54 – 574
    Helixi63 – 653
    Beta strandi69 – 746
    Helixi79 – 813
    Turni82 – 843
    Helixi86 – 894
    Beta strandi90 – 956
    Beta strandi99 – 1079
    Turni109 – 1113
    Helixi113 – 1153
    Helixi118 – 13114
    Turni132 – 1343
    Beta strandi138 – 1425
    Helixi145 – 1506
    Turni151 – 1533
    Helixi158 – 16710
    Helixi172 – 1754
    Beta strandi180 – 1823
    Beta strandi188 – 1903
    Helixi191 – 20111
    Beta strandi205 – 2095
    Turni210 – 2123
    Beta strandi213 – 2208
    Helixi221 – 24323
    Helixi256 – 2638
    Helixi269 – 2724

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GT7X-ray2.70A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T1-274[»]
    1OJRX-ray1.35A1-274[»]
    2UYUX-ray1.96A/E1-274[»]
    2UYVX-ray2.20A/B/C/D1-274[»]
    2V29X-ray2.03A/B1-274[»]
    2V2AX-ray1.75A1-274[»]
    2V2BX-ray1.50A1-274[»]
    2V9EX-ray1.58A/B1-272[»]
    2V9FX-ray2.10A1-272[»]
    2V9GX-ray2.70A/B/C/D1-274[»]
    2V9IX-ray1.80A/B1-273[»]
    2V9LX-ray1.23A1-274[»]
    2V9MX-ray1.30A/B1-274[»]
    2V9NX-ray1.40A/B/C/D1-274[»]
    2V9OX-ray1.95A/E1-274[»]
    ProteinModelPortaliP32169.
    SMRiP32169. Positions 1-274.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP32169.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0235.
    HOGENOMiHOG000279628.
    KOiK01629.
    OMAiDMWLKGW.
    OrthoDBiEOG61GGBF.
    PhylomeDBiP32169.

    Family and domain databases

    Gene3Di3.40.225.10. 1 hit.
    HAMAPiMF_00770. RhaD.
    InterProiIPR001303. Aldolase_II/adducin_N.
    IPR013447. Rhamnulose-1-P_Aldolase.
    [Graphical view]
    PfamiPF00596. Aldolase_II. 1 hit.
    [Graphical view]
    SMARTiSM01007. Aldolase_II. 1 hit.
    [Graphical view]
    SUPFAMiSSF53639. SSF53639. 1 hit.
    TIGRFAMsiTIGR02624. rhamnu_1P_ald. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P32169-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQNITQSWFV QGMIKATTDA WLKGWDERNG GNLTLRLDDA DIAPYHDNFH    50
    QQPRYIPLSQ PMPLLANTPF IVTGSGKFFR NVQLDPAANL GIVKVDSDGA 100
    GYHILWGLTN EAVPTSELPA HFLSHCERIK ATNGKDRVIM HCHATNLIAL 150
    TYVLENDTAV FTRQLWEGST ECLVVFPDGV GILPWMVPGT DEIGQATAQE 200
    MQKHSLVLWP FHGVFGSGPT LDETFGLIDT AEKSAQVLVK VYSMGGMKQT 250
    ISREELIALG KRFGVTPLAS ALAL 274
    Length:274
    Mass (Da):30,145
    Last modified:October 1, 1993 - v1
    Checksum:iF9FF0BE156F4E63D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X60472 Genomic DNA. Translation: CAA43003.1.
    L19201 Genomic DNA. Translation: AAB03035.1.
    U00096 Genomic DNA. Translation: AAC76884.1.
    AP009048 Genomic DNA. Translation: BAE77407.1.
    PIRiC48649.
    RefSeqiNP_418338.1. NC_000913.3.
    YP_491548.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76884; AAC76884; b3902.
    BAE77407; BAE77407; BAE77407.
    GeneIDi12931682.
    948401.
    KEGGiecj:Y75_p3284.
    eco:b3902.
    PATRICi32123313. VBIEscCol129921_4017.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X60472 Genomic DNA. Translation: CAA43003.1 .
    L19201 Genomic DNA. Translation: AAB03035.1 .
    U00096 Genomic DNA. Translation: AAC76884.1 .
    AP009048 Genomic DNA. Translation: BAE77407.1 .
    PIRi C48649.
    RefSeqi NP_418338.1. NC_000913.3.
    YP_491548.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GT7 X-ray 2.70 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T 1-274 [» ]
    1OJR X-ray 1.35 A 1-274 [» ]
    2UYU X-ray 1.96 A/E 1-274 [» ]
    2UYV X-ray 2.20 A/B/C/D 1-274 [» ]
    2V29 X-ray 2.03 A/B 1-274 [» ]
    2V2A X-ray 1.75 A 1-274 [» ]
    2V2B X-ray 1.50 A 1-274 [» ]
    2V9E X-ray 1.58 A/B 1-272 [» ]
    2V9F X-ray 2.10 A 1-272 [» ]
    2V9G X-ray 2.70 A/B/C/D 1-274 [» ]
    2V9I X-ray 1.80 A/B 1-273 [» ]
    2V9L X-ray 1.23 A 1-274 [» ]
    2V9M X-ray 1.30 A/B 1-274 [» ]
    2V9N X-ray 1.40 A/B/C/D 1-274 [» ]
    2V9O X-ray 1.95 A/E 1-274 [» ]
    ProteinModelPortali P32169.
    SMRi P32169. Positions 1-274.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P32169. 7 interactions.
    STRINGi 511145.b3902.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76884 ; AAC76884 ; b3902 .
    BAE77407 ; BAE77407 ; BAE77407 .
    GeneIDi 12931682.
    948401.
    KEGGi ecj:Y75_p3284.
    eco:b3902.
    PATRICi 32123313. VBIEscCol129921_4017.

    Organism-specific databases

    EchoBASEi EB1812.
    EcoGenei EG11866. rhaD.

    Phylogenomic databases

    eggNOGi COG0235.
    HOGENOMi HOG000279628.
    KOi K01629.
    OMAi DMWLKGW.
    OrthoDBi EOG61GGBF.
    PhylomeDBi P32169.

    Enzyme and pathway databases

    UniPathwayi UPA00541 ; UER00603 .
    BioCyci EcoCyc:RHAMNULPALDOL-MONOMER.
    ECOL316407:JW3873-MONOMER.
    MetaCyc:RHAMNULPALDOL-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P32169.
    PROi P32169.

    Gene expression databases

    Genevestigatori P32169.

    Family and domain databases

    Gene3Di 3.40.225.10. 1 hit.
    HAMAPi MF_00770. RhaD.
    InterProi IPR001303. Aldolase_II/adducin_N.
    IPR013447. Rhamnulose-1-P_Aldolase.
    [Graphical view ]
    Pfami PF00596. Aldolase_II. 1 hit.
    [Graphical view ]
    SMARTi SM01007. Aldolase_II. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53639. SSF53639. 1 hit.
    TIGRFAMsi TIGR02624. rhamnu_1P_ald. 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. "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.
    5. "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.
    6. "Escherichia coli proteome analysis using the gene-protein database."
      VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
      Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY 2D-GEL.
    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 L-rhamnulose-1-phosphate aldolase (class II) solved by low-resolution SIR phasing and 20-fold NCS averaging."
      Kroemer M., Schulz G.E.
      Acta Crystallogr. D 58:824-832(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
    9. "Structure and catalytic mechanism of L-rhamnulose-1-phosphate aldolase."
      Kroemer M., Merkel I., Schulz G.E.
      Biochemistry 42:10560-10568(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).

    Entry informationi

    Entry nameiRHAD_ECOLI
    AccessioniPrimary (citable) accession number: P32169
    Secondary accession number(s): Q2M8J9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: October 1, 1993
    Last modified: October 1, 2014
    This is version 117 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