Ribose-5-phosphate isomerase B - Escherichia coli (strain K12)

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P37351 (RPIB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 114. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	149 AA.
Sequence status	Complete.
Protein existence	Evidence 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.7 Ref.9
Catalytic activity	D-ribose 5-phosphate = D-ribulose 5-phosphate. Ref.8 Ref.9 D-allose 6-phosphate = D-allulose 6-phosphate. Ref.8 Ref.9
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.8
Sequence similarities	Belongs to the LacAB/RpiB family.
Biophysicochemical properties	Kinetic parameters: K_M=1.23 mM for D-ribose 5-phosphate Ref.8 Ref.9 K_M=0.5 mM for D-allose 6-phosphate

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Molecular function	Isomerase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	D-allose catabolic process Inferred from mutant phenotype PubMed 10559180. Source: EcoCyc pentose-phosphate shunt Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	allose 6-phosphate isomerase activity Inferred from direct assay Ref.9. Source: EcoCyc ribose-5-phosphate isomerase activity Inferred from direct assay PubMed 1104357 Ref.9. Source: EcoCyc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
rplJ	P0A7J3	1	EBI-557460,EBI-546827

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 149

149

Ribose-5-phosphate isomerase B

PRO_0000208163

Regions

Region

67 – 72

Substrate binding By similarity

Sites

Active site

Proton acceptor Probable

Active site

Proton donor Probable

Binding site

Substrate

Binding site

Substrate

Binding site

110

Substrate

Binding site

133

Substrate

Binding site

137

Substrate

Experimental info

Mutagenesis

H → N: Strongly reduced enzyme activity. Ref.9

Secondary structure

149

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P37351 [UniParc].

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

FASTA

149

16,073

        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' referencesShow '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]. 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 277:1453-1474(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]	"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.
[7]	"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.
[8]	"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.
[9]	"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.

PIR

JC6054.

RefSeq

NP_418514.1. NC_000913.2.
YP_492234.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P37351.

SMR

P37351. Positions 1-147.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-10740N.

IntAct

P37351. 3 interactions.

MINT

MINT-1235144.

STRING

511145.b4090.

Proteomic databases

PaxDb

P37351.

PRIDE

P37351.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC77051; AAC77051; b4090.
BAE78093; BAE78093; BAE78093.

GeneID

12933689.
948602.

KEGG

ecj:Y75_p3978.
eco:b4090.

PATRIC

32123739. VBIEscCol129921_4218.

Organism-specific databases

EchoBASE

EB1774.

EcoGene

EG11827. rpiB.

Phylogenomic databases

eggNOG

COG0698.

HOGENOM

HOG000226301.

K01808.

OMA

IERREEC.

ProtClustDB

PRK05571.

Enzyme and pathway databases

BioCyc

EcoCyc:RIB5PISOMB-MONOMER.
ECOL316407:JW4051-MONOMER.
MetaCyc:RIB5PISOMB-MONOMER.

SABIO-RK

P37351.

UniPathway

UPA00115; UER00412.

Gene expression databases

Genevestigator

P37351.

Family and domain databases

Gene3D

3.40.1400.10. 1 hit.

InterPro

IPR003500. Rib/Gal_isomrase.
IPR004785. RpiB.
[Graphical view]

PANTHER

PTHR30345. PTHR30345. 1 hit.

Pfam

PF02502. LacAB_rpiB. 1 hit.
[Graphical view]

PIRSF

PIRSF005384. RpiB_LacA_B. 1 hit.

SUPFAM

SSF89623. Rib/Gal_isomrase. 1 hit.

TIGRFAMs

TIGR01120. rpiB. 1 hit.
TIGR00689. rpiB_lacA_lacB. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P37351.

Entry information

Entry name

RPIB_ECOLI

Accession

Primary (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 1, 2013
This is version 114 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents