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P37351

- RPIB_ECOLI

UniProt

P37351 - RPIB_ECOLI

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Protein
Ribose-5-phosphate isomerase B
Gene
rpiB, yjcA, b4090, JW4051
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

D-ribose 5-phosphate = D-ribulose 5-phosphate.3 Publications
D-allose 6-phosphate = D-allulose 6-phosphate.3 Publications

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. KM=0.5 mM for D-allose 6-phosphate (PubMed: 18640127)

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.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei10 – 101Substrate
Binding sitei17 – 171Substrate
Active sitei66 – 661Proton acceptor Inferred
Active sitei99 – 991Proton donor Inferred
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
Complete GO annotation...

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 B
PRO_0000208163Add
BLAST

Proteomic databases

PaxDbiP37351.
PRIDEiP37351.

Expressioni

Inductioni

Induced by ribose and repressed by RpiR.3 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

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.

Miscellaneous databases

EvolutionaryTraceiP37351.

Family & Domainsi

Region

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

Sequence similaritiesi

Belongs to the LacAB/RpiB family.

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

« Hide 'large scale' publications
  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: May 14, 2014
This is version 122 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

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