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P37351 (RPIB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribose-5-phosphate isomerase B

EC=5.3.1.6
Alternative name(s):
Phosphoriboisomerase B
Gene names
Name:rpiB
Synonyms:yjcA
Ordered Locus Names:b4090, JW4051
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length149 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

In addition to its activity on D-ribose 5-phosphate it probably also has activity on D-allose 6-phosphate. Ref.1 Ref.6 Ref.7 Ref.9 Ref.11

Catalytic activity

D-ribose 5-phosphate = D-ribulose 5-phosphate. Ref.7 Ref.10 Ref.11

D-allose 6-phosphate = D-allulose 6-phosphate. Ref.7 Ref.10 Ref.11

Enzyme regulation

Inhibited by iodoacetate and glucose 6-phosphate. Ref.6 Ref.7

Pathway

Carbohydrate degradation; pentose phosphate pathway; D-ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step 1/1.

Subunit structure

Homodimer, and homotetramer. Ref.10

Induction

Induced by ribose and repressed by RpiR. Ref.1 Ref.6 Ref.7

Sequence similarities

Belongs to the LacAB/RpiB family.

Biophysicochemical properties

Kinetic parameters:

KM=0.83 mM for D-ribose 5-phosphate (at 37 degrees Celsius)(PubMed: 1104357) Ref.7 Ref.10 Ref.11

KM=1.23 mM for D-ribose 5-phosphate (PubMed: 18640127)

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

Temperature dependence:

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

Binary interactions

With

Entry

#Exp.

IntAct

Notes

rplJP0A7J31EBI-557460,EBI-546827

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 149149Ribose-5-phosphate isomerase B
PRO_0000208163

Regions

Region67 – 726Substrate binding By similarity

Sites

Active site661Proton acceptor Probable
Active site991Proton donor Probable
Binding site101Substrate
Binding site171Substrate
Binding site1101Substrate
Binding site1331Substrate
Binding site1371Substrate

Experimental info

Mutagenesis991H → N: Strongly reduced enzyme activity. Ref.11

Secondary structure

.......................... 149
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P37351 [UniParc].

Last modified February 1, 1995. Version 2.
Checksum: BE610B5F995CEEB6

FASTA14916,073
        10         20         30         40         50         60 
MKKIAFGCDH VGFILKHEIV AHLVERGVEV IDKGTWSSER TDYPHYASQV ALAVAGGEVD 

        70         80         90        100        110        120 
GGILICGTGV GISIAANKFA GIRAVVCSEP YSAQLSRQHN DTNVLAFGSR VVGLELAKMI 

       130        140 
VDAWLGAQYE GGRHQQRVEA ITAIEQRRN 

« Hide

References

« Hide 'large scale' references
[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]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRJC6054.
RefSeqNP_418514.1. NC_000913.3.
YP_492234.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1NN4X-ray2.20A/B/C/D1-149[»]
2VVRX-ray2.10A/B/C/D/E/F1-149[»]
ProteinModelPortalP37351.
SMRP37351. Positions 1-147.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-10740N.
IntActP37351. 3 interactions.
MINTMINT-1235144.
STRING511145.b4090.

Proteomic databases

PaxDbP37351.
PRIDEP37351.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC77051; AAC77051; b4090.
BAE78093; BAE78093; BAE78093.
GeneID12933689.
948602.
KEGGecj:Y75_p3978.
eco:b4090.
PATRIC32123739. VBIEscCol129921_4218.

Organism-specific databases

EchoBASEEB1774.
EcoGeneEG11827. rpiB.

Phylogenomic databases

eggNOGCOG0698.
HOGENOMHOG000226301.
KOK01808.
OMAETHHANQ.
OrthoDBEOG679TJ4.
PhylomeDBP37351.

Enzyme and pathway databases

BioCycEcoCyc:RIB5PISOMB-MONOMER.
ECOL316407:JW4051-MONOMER.
MetaCyc:RIB5PISOMB-MONOMER.
SABIO-RKP37351.
UniPathwayUPA00115; UER00412.

Gene expression databases

GenevestigatorP37351.

Family and domain databases

Gene3D3.40.1400.10. 1 hit.
InterProIPR004785. RpiB.
IPR003500. RpiB_LacA_LacB.
[Graphical view]
PANTHERPTHR30345. PTHR30345. 1 hit.
PfamPF02502. LacAB_rpiB. 1 hit.
[Graphical view]
PIRSFPIRSF005384. RpiB_LacA_B. 1 hit.
SUPFAMSSF89623. SSF89623. 1 hit.
TIGRFAMsTIGR01120. rpiB. 1 hit.
TIGR00689. rpiB_lacA_lacB. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP37351.
PROP37351.

Entry information

Entry nameRPIB_ECOLI
AccessionPrimary (citable) accession number: P37351
Secondary accession number(s): O32564, Q2M6L3
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene