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P37351

- RPIB_ECOLI

UniProt

P37351 - RPIB_ECOLI

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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

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
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 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.
InParanoidiP37351.
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

        10         20         30         40         50
MKKIAFGCDH VGFILKHEIV AHLVERGVEV IDKGTWSSER TDYPHYASQV
60 70 80 90 100
ALAVAGGEVD GGILICGTGV GISIAANKFA GIRAVVCSEP YSAQLSRQHN
110 120 130 140
DTNVLAFGSR VVGLELAKMI VDAWLGAQYE GGRHQQRVEA ITAIEQRRN
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.
InParanoidi P37351.
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: October 29, 2014
This is version 124 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