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P37351

- RPIB_ECOLI

UniProt

P37351 - RPIB_ECOLI

Protein

Ribose-5-phosphate isomerase B

Gene

rpiB

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

    In addition to its activity on D-ribose 5-phosphate it probably also has activity on D-allose 6-phosphate.4 Publications

    Catalytic activityi

    D-ribose 5-phosphate = D-ribulose 5-phosphate.
    D-allose 6-phosphate = D-allulose 6-phosphate.

    Enzyme regulationi

    Inhibited by iodoacetate and glucose 6-phosphate.2 Publications

    Kineticsi

    1. KM=0.83 mM for D-ribose 5-phosphate (at 37 degrees Celsius)(PubMed: 1104357)3 Publications
    2. KM=1.23 mM for D-ribose 5-phosphate (PubMed: 18640127)3 Publications
    3. KM=0.5 mM for D-allose 6-phosphate (PubMed: 18640127)3 Publications

    Temperature dependencei

    After incubation at 45 degrees Celsius for 30 minutes RpiB retains 65% of its original activities. At 60 degrees Celsius RpiB is rapidly inactivated.3 Publications

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei10 – 101Substrate
    Binding sitei17 – 171Substrate
    Active sitei66 – 661Proton acceptor1 Publication
    Active sitei99 – 991Proton donor1 Publication
    Binding sitei110 – 1101Substrate
    Binding sitei133 – 1331Substrate
    Binding sitei137 – 1371Substrate

    GO - Molecular functioni

    1. allose 6-phosphate isomerase activity Source: EcoCyc
    2. ribose-5-phosphate isomerase activity Source: EcoCyc

    GO - Biological processi

    1. D-allose catabolic process Source: EcoCyc
    2. pentose-phosphate shunt Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Isomerase

    Keywords - Biological processi

    Carbohydrate metabolism

    Enzyme and pathway databases

    BioCyciEcoCyc:RIB5PISOMB-MONOMER.
    ECOL316407:JW4051-MONOMER.
    MetaCyc:RIB5PISOMB-MONOMER.
    SABIO-RKP37351.
    UniPathwayiUPA00115; UER00412.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribose-5-phosphate isomerase B (EC:5.3.1.6)
    Alternative name(s):
    Phosphoriboisomerase B
    Gene namesi
    Name:rpiB
    Synonyms:yjcA
    Ordered Locus Names:b4090, JW4051
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG11827. rpiB.

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi99 – 991H → N: Strongly reduced enzyme activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 149149Ribose-5-phosphate isomerase BPRO_0000208163Add
    BLAST

    Proteomic databases

    PaxDbiP37351.
    PRIDEiP37351.

    Expressioni

    Inductioni

    Induced by ribose and repressed by RpiR.2 Publications

    Gene expression databases

    GenevestigatoriP37351.

    Interactioni

    Subunit structurei

    Homodimer, and homotetramer.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    rplJP0A7J31EBI-557460,EBI-546827

    Protein-protein interaction databases

    DIPiDIP-10740N.
    IntActiP37351. 3 interactions.
    MINTiMINT-1235144.
    STRINGi511145.b4090.

    Structurei

    Secondary structure

    1
    149
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 86
    Helixi12 – 154
    Helixi16 – 2510
    Beta strandi29 – 324
    Beta strandi37 – 393
    Helixi43 – 5513
    Beta strandi58 – 6912
    Helixi70 – 778
    Beta strandi84 – 863
    Helixi90 – 10011
    Beta strandi104 – 1085
    Turni109 – 1113
    Helixi114 – 12613
    Helixi134 – 14512

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1NN4X-ray2.20A/B/C/D1-149[»]
    2VVRX-ray2.10A/B/C/D/E/F1-149[»]
    ProteinModelPortaliP37351.
    SMRiP37351. Positions 1-147.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP37351.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni67 – 726Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the LacAB/RpiB family.Curated

    Phylogenomic databases

    eggNOGiCOG0698.
    HOGENOMiHOG000226301.
    KOiK01808.
    OMAiETHHANQ.
    OrthoDBiEOG679TJ4.
    PhylomeDBiP37351.

    Family and domain databases

    Gene3Di3.40.1400.10. 1 hit.
    InterProiIPR004785. RpiB.
    IPR003500. RpiB_LacA_LacB.
    [Graphical view]
    PANTHERiPTHR30345. PTHR30345. 1 hit.
    PfamiPF02502. LacAB_rpiB. 1 hit.
    [Graphical view]
    PIRSFiPIRSF005384. RpiB_LacA_B. 1 hit.
    SUPFAMiSSF89623. SSF89623. 1 hit.
    TIGRFAMsiTIGR01120. rpiB. 1 hit.
    TIGR00689. rpiB_lacA_lacB. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P37351-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKKIAFGCDH VGFILKHEIV AHLVERGVEV IDKGTWSSER TDYPHYASQV    50
    ALAVAGGEVD GGILICGTGV GISIAANKFA GIRAVVCSEP YSAQLSRQHN 100
    DTNVLAFGSR VVGLELAKMI VDAWLGAQYE GGRHQQRVEA ITAIEQRRN 149
    Length:149
    Mass (Da):16,073
    Last modified:February 1, 1995 - v2
    Checksum:iBE610B5F995CEEB6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X82203 Genomic DNA. Translation: CAA57688.1.
    U14003 Genomic DNA. Translation: AAA96989.1.
    U00096 Genomic DNA. Translation: AAC77051.1.
    AP009048 Genomic DNA. Translation: BAE78093.1.
    D90227 Genomic DNA. Translation: BAA21501.1.
    PIRiJC6054.
    RefSeqiNP_418514.1. NC_000913.3.
    YP_492234.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC77051; AAC77051; b4090.
    BAE78093; BAE78093; BAE78093.
    GeneIDi12933689.
    948602.
    KEGGiecj:Y75_p3978.
    eco:b4090.
    PATRICi32123739. VBIEscCol129921_4218.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X82203 Genomic DNA. Translation: CAA57688.1 .
    U14003 Genomic DNA. Translation: AAA96989.1 .
    U00096 Genomic DNA. Translation: AAC77051.1 .
    AP009048 Genomic DNA. Translation: BAE78093.1 .
    D90227 Genomic DNA. Translation: BAA21501.1 .
    PIRi JC6054.
    RefSeqi NP_418514.1. NC_000913.3.
    YP_492234.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1NN4 X-ray 2.20 A/B/C/D 1-149 [» ]
    2VVR X-ray 2.10 A/B/C/D/E/F 1-149 [» ]
    ProteinModelPortali P37351.
    SMRi P37351. Positions 1-147.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-10740N.
    IntActi P37351. 3 interactions.
    MINTi MINT-1235144.
    STRINGi 511145.b4090.

    Proteomic databases

    PaxDbi P37351.
    PRIDEi P37351.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC77051 ; AAC77051 ; b4090 .
    BAE78093 ; BAE78093 ; BAE78093 .
    GeneIDi 12933689.
    948602.
    KEGGi ecj:Y75_p3978.
    eco:b4090.
    PATRICi 32123739. VBIEscCol129921_4218.

    Organism-specific databases

    EchoBASEi EB1774.
    EcoGenei EG11827. rpiB.

    Phylogenomic databases

    eggNOGi COG0698.
    HOGENOMi HOG000226301.
    KOi K01808.
    OMAi ETHHANQ.
    OrthoDBi EOG679TJ4.
    PhylomeDBi P37351.

    Enzyme and pathway databases

    UniPathwayi UPA00115 ; UER00412 .
    BioCyci EcoCyc:RIB5PISOMB-MONOMER.
    ECOL316407:JW4051-MONOMER.
    MetaCyc:RIB5PISOMB-MONOMER.
    SABIO-RK P37351.

    Miscellaneous databases

    EvolutionaryTracei P37351.
    PROi P37351.

    Gene expression databases

    Genevestigatori P37351.

    Family and domain databases

    Gene3Di 3.40.1400.10. 1 hit.
    InterProi IPR004785. RpiB.
    IPR003500. RpiB_LacA_LacB.
    [Graphical view ]
    PANTHERi PTHR30345. PTHR30345. 1 hit.
    Pfami PF02502. LacAB_rpiB. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF005384. RpiB_LacA_B. 1 hit.
    SUPFAMi SSF89623. SSF89623. 1 hit.
    TIGRFAMsi TIGR01120. rpiB. 1 hit.
    TIGR00689. rpiB_lacA_lacB. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Ribose catabolism of Escherichia coli: characterization of the rpiB gene encoding ribose phosphate isomerase B and of the rpiR gene, which is involved in regulation of rpiB expression."
      Soerensen K.I., Hove-Jensen B.
      J. Bacteriol. 178:1003-1011(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION.
      Strain: K12.
    2. "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
      Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
      Nucleic Acids Res. 23:2105-2119(1995) [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. "Molecular analysis of the cryptic and functional phn operons for phosphonate use in Escherichia coli K-12."
      Makino K., Kim S.K., Shinagawa H., Amemura M., Nakata A.
      J. Bacteriol. 173:2665-2672(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 82-149.
      Strain: K12.
    6. "Regulation of ribose metabolism in Escherichia coli. II. Evidence for two ribose-5-phosphate isomerase activities."
      David J., Wiesmeyer H.
      Biochim. Biophys. Acta 208:56-67(1970) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION.
    7. "Two ribose-5-phosphate isomerases from Escherichia coli K12: partial characterisation of the enzymes and consideration of their possible physiological roles."
      Essenberg M.K., Cooper R.A.
      Eur. J. Biochem. 55:323-332(1975) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION.
    8. "Intrinsic and extrinsic approaches for detecting genes in a bacterial genome."
      Borodovsky M., Rudd K.E., Koonin E.V.
      Nucleic Acids Res. 22:4756-4767(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION.
    9. "The D-allose operon of Escherichia coli K-12."
      Kim C., Song S., Park C.
      J. Bacteriol. 179:7631-7637(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROBABLE ADDITIONAL FUNCTION.
    10. "The 2.2 A resolution structure of RpiB/AlsB from Escherichia coli illustrates a new approach to the ribose-5-phosphate isomerase reaction."
      Zhang R.G., Andersson C.E., Skarina T., Evdokimova E., Edwards A.M., Joachimiak A., Savchenko A., Mowbray S.L.
      J. Mol. Biol. 332:1083-1094(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS), CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
    11. "D-ribose-5-phosphate isomerase B from Escherichia coli is also a functional D-allose-6-phosphate isomerase, while the Mycobacterium tuberculosis enzyme is not."
      Roos A.K., Mariano S., Kowalinski E., Salmon L., Mowbray S.L.
      J. Mol. Biol. 382:667-679(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-99, ACTIVE SITE.

    Entry informationi

    Entry nameiRPIB_ECOLI
    AccessioniPrimary (citable) accession number: P37351
    Secondary accession number(s): O32564, Q2M6L3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 123 of the entry and version 2 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