RPIB_ECOLI
ID RPIB_ECOLI Reviewed; 149 AA.
AC P37351; O32564; Q2M6L3;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Ribose-5-phosphate isomerase B {ECO:0000303|PubMed:8576032};
DE EC=5.3.1.6 {ECO:0000269|PubMed:1104357, ECO:0000269|PubMed:18640127};
DE AltName: Full=Phosphoriboisomerase B {ECO:0000303|PubMed:8576032};
GN Name=rpiB {ECO:0000303|PubMed:8576032}; Synonyms=yjcA;
GN OrderedLocusNames=b4090, JW4051;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RC STRAIN=K12;
RX PubMed=8576032; DOI=10.1128/jb.178.4.1003-1011.1996;
RA Soerensen K.I., Hove-Jensen B.;
RT "Ribose catabolism of Escherichia coli: characterization of the rpiB gene
RT encoding ribose phosphate isomerase B and of the rpiR gene, which is
RT involved in regulation of rpiB expression.";
RL J. Bacteriol. 178:1003-1011(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 82-149.
RC STRAIN=K12;
RX PubMed=1840580; DOI=10.1128/jb.173.8.2665-2672.1991;
RA Makino K., Kim S.K., Shinagawa H., Amemura M., Nakata A.;
RT "Molecular analysis of the cryptic and functional phn operons for
RT phosphonate use in Escherichia coli K-12.";
RL J. Bacteriol. 173:2665-2672(1991).
RN [6]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=4909663; DOI=10.1016/0304-4165(70)90048-6;
RA David J., Wiesmeyer H.;
RT "Regulation of ribose metabolism in Escherichia coli. II. Evidence for two
RT ribose-5-phosphate isomerase activities.";
RL Biochim. Biophys. Acta 208:56-67(1970).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND INDUCTION.
RX PubMed=1104357; DOI=10.1111/j.1432-1033.1975.tb02166.x;
RA Essenberg M.K., Cooper R.A.;
RT "Two ribose-5-phosphate isomerases from Escherichia coli K12: partial
RT characterisation of the enzymes and consideration of their possible
RT physiological roles.";
RL Eur. J. Biochem. 55:323-332(1975).
RN [8]
RP IDENTIFICATION.
RX PubMed=7984428; DOI=10.1093/nar/22.22.4756;
RA Borodovsky M., Rudd K.E., Koonin E.V.;
RT "Intrinsic and extrinsic approaches for detecting genes in a bacterial
RT genome.";
RL Nucleic Acids Res. 22:4756-4767(1994).
RN [9]
RP PROBABLE ADDITIONAL FUNCTION.
RX PubMed=9401019; DOI=10.1128/jb.179.24.7631-7637.1997;
RA Kim C., Song S., Park C.;
RT "The D-allose operon of Escherichia coli K-12.";
RL J. Bacteriol. 179:7631-7637(1997).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS), CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=14499611; DOI=10.1016/j.jmb.2003.08.009;
RA Zhang R.G., Andersson C.E., Skarina T., Evdokimova E., Edwards A.M.,
RA Joachimiak A., Savchenko A., Mowbray S.L.;
RT "The 2.2 A resolution structure of RpiB/AlsB from Escherichia coli
RT illustrates a new approach to the ribose-5-phosphate isomerase reaction.";
RL J. Mol. Biol. 332:1083-1094(2003).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-99, ACTIVE SITE, AND
RP SUBUNIT.
RX PubMed=18640127; DOI=10.1016/j.jmb.2008.06.090;
RA Roos A.K., Mariano S., Kowalinski E., Salmon L., Mowbray S.L.;
RT "D-ribose-5-phosphate isomerase B from Escherichia coli is also a
RT functional D-allose-6-phosphate isomerase, while the Mycobacterium
RT tuberculosis enzyme is not.";
RL J. Mol. Biol. 382:667-679(2008).
CC -!- FUNCTION: Catalyzes the interconversion of ribulose-5-P and ribose-5-P.
CC It probably also has activity on D-allose 6-phosphate.
CC {ECO:0000269|PubMed:1104357, ECO:0000269|PubMed:18640127,
CC ECO:0000269|PubMed:4909663, ECO:0000269|PubMed:8576032}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosphate;
CC Xref=Rhea:RHEA:14657, ChEBI:CHEBI:58121, ChEBI:CHEBI:58273;
CC EC=5.3.1.6; Evidence={ECO:0000269|PubMed:1104357,
CC ECO:0000269|PubMed:18640127};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-allose 6-phosphate = D-allulose 6-phosphate;
CC Xref=Rhea:RHEA:28430, ChEBI:CHEBI:58328, ChEBI:CHEBI:61519;
CC Evidence={ECO:0000269|PubMed:18640127};
CC -!- ACTIVITY REGULATION: Inhibited by iodoacetate and glucose 6-phosphate.
CC {ECO:0000269|PubMed:1104357, ECO:0000269|PubMed:4909663}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.83 mM for D-ribose 5-phosphate (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:1104357};
CC KM=1.23 mM for D-ribose 5-phosphate {ECO:0000269|PubMed:18640127};
CC KM=0.5 mM for D-allose 6-phosphate {ECO:0000269|PubMed:18640127};
CC Temperature dependence:
CC After incubation at 45 degrees Celsius for 30 minutes RpiB retains
CC 65% of its original activities. At 60 degrees Celsius RpiB is rapidly
CC inactivated. {ECO:0000269|PubMed:1104357,
CC ECO:0000269|PubMed:14499611, ECO:0000269|PubMed:18640127};
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-ribose
CC 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step
CC 1/1.
CC -!- SUBUNIT: Homodimer, and homotetramer. {ECO:0000269|PubMed:14499611,
CC ECO:0000269|PubMed:18640127}.
CC -!- INTERACTION:
CC P37351; P0A7J3: rplJ; NbExp=2; IntAct=EBI-557460, EBI-546827;
CC -!- INDUCTION: Induced by ribose and repressed by RpiR.
CC {ECO:0000269|PubMed:1104357, ECO:0000269|PubMed:8576032}.
CC -!- SIMILARITY: Belongs to the LacAB/RpiB family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X82203; CAA57688.1; -; Genomic_DNA.
DR EMBL; U14003; AAA96989.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77051.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78093.1; -; Genomic_DNA.
DR EMBL; D90227; BAA21501.1; -; Genomic_DNA.
DR PIR; JC6054; JC6054.
DR RefSeq; NP_418514.1; NC_000913.3.
DR RefSeq; WP_000716794.1; NZ_STEB01000014.1.
DR PDB; 1NN4; X-ray; 2.20 A; A/B/C/D=1-149.
DR PDB; 2VVR; X-ray; 2.10 A; A/B/C/D/E/F=1-149.
DR PDBsum; 1NN4; -.
DR PDBsum; 2VVR; -.
DR AlphaFoldDB; P37351; -.
DR SMR; P37351; -.
DR BioGRID; 4262683; 7.
DR DIP; DIP-10740N; -.
DR IntAct; P37351; 3.
DR STRING; 511145.b4090; -.
DR jPOST; P37351; -.
DR PaxDb; P37351; -.
DR PRIDE; P37351; -.
DR EnsemblBacteria; AAC77051; AAC77051; b4090.
DR EnsemblBacteria; BAE78093; BAE78093; BAE78093.
DR GeneID; 948602; -.
DR KEGG; ecj:JW4051; -.
DR KEGG; eco:b4090; -.
DR PATRIC; fig|1411691.4.peg.2610; -.
DR EchoBASE; EB1774; -.
DR eggNOG; COG0698; Bacteria.
DR HOGENOM; CLU_091396_4_1_6; -.
DR InParanoid; P37351; -.
DR OMA; DYPPFCL; -.
DR PhylomeDB; P37351; -.
DR BioCyc; EcoCyc:RIB5PISOMB-MON; -.
DR BioCyc; MetaCyc:RIB5PISOMB-MON; -.
DR SABIO-RK; P37351; -.
DR UniPathway; UPA00115; UER00412.
DR EvolutionaryTrace; P37351; -.
DR PRO; PR:P37351; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0008786; F:allose 6-phosphate isomerase activity; IDA:EcoCyc.
DR GO; GO:0016853; F:isomerase activity; IBA:GO_Central.
DR GO; GO:0004751; F:ribose-5-phosphate isomerase activity; IDA:EcoCyc.
DR GO; GO:0019316; P:D-allose catabolic process; IMP:EcoCyc.
DR GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; IBA:GO_Central.
DR Gene3D; 3.40.1400.10; -; 1.
DR InterPro; IPR004785; RpiB.
DR InterPro; IPR003500; RpiB_LacA_LacB.
DR InterPro; IPR036569; RpiB_LacA_LacB_sf.
DR Pfam; PF02502; LacAB_rpiB; 1.
DR PIRSF; PIRSF005384; RpiB_LacA_B; 1.
DR SUPFAM; SSF89623; SSF89623; 1.
DR TIGRFAMs; TIGR01120; rpiB; 1.
DR TIGRFAMs; TIGR00689; rpiB_lacA_lacB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Isomerase; Reference proteome.
FT CHAIN 1..149
FT /note="Ribose-5-phosphate isomerase B"
FT /id="PRO_0000208163"
FT ACT_SITE 66
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:18640127"
FT ACT_SITE 99
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:18640127"
FT BINDING 9..10
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000250|UniProtKB:P9WKD7"
FT BINDING 67..71
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000250|UniProtKB:P9WKD7"
FT BINDING 100
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000250|UniProtKB:P9WKD7"
FT BINDING 110
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000250|UniProtKB:P9WKD7"
FT BINDING 133
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000250|UniProtKB:P9WKD7"
FT BINDING 137
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000250|UniProtKB:P9WKD7"
FT MUTAGEN 99
FT /note="H->N: Strongly reduced enzyme activity."
FT /evidence="ECO:0000269|PubMed:18640127"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:2VVR"
FT HELIX 12..15
FT /evidence="ECO:0007829|PDB:2VVR"
FT HELIX 16..25
FT /evidence="ECO:0007829|PDB:2VVR"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:2VVR"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:2VVR"
FT HELIX 43..55
FT /evidence="ECO:0007829|PDB:2VVR"
FT STRAND 58..69
FT /evidence="ECO:0007829|PDB:2VVR"
FT HELIX 70..77
FT /evidence="ECO:0007829|PDB:2VVR"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:2VVR"
FT HELIX 90..100
FT /evidence="ECO:0007829|PDB:2VVR"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:2VVR"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:2VVR"
FT HELIX 114..126
FT /evidence="ECO:0007829|PDB:2VVR"
FT HELIX 134..145
FT /evidence="ECO:0007829|PDB:2VVR"
SQ SEQUENCE 149 AA; 16073 MW; BE610B5F995CEEB6 CRC64;
MKKIAFGCDH VGFILKHEIV AHLVERGVEV IDKGTWSSER TDYPHYASQV ALAVAGGEVD
GGILICGTGV GISIAANKFA GIRAVVCSEP YSAQLSRQHN DTNVLAFGSR VVGLELAKMI
VDAWLGAQYE GGRHQQRVEA ITAIEQRRN
