RPIA_ECOLI
ID RPIA_ECOLI Reviewed; 219 AA.
AC P0A7Z0; P27252; Q2M9S8;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Ribose-5-phosphate isomerase A {ECO:0000255|HAMAP-Rule:MF_00170};
DE EC=5.3.1.6 {ECO:0000255|HAMAP-Rule:MF_00170};
DE AltName: Full=Phosphoriboisomerase A {ECO:0000255|HAMAP-Rule:MF_00170};
DE Short=PRI {ECO:0000255|HAMAP-Rule:MF_00170};
GN Name=rpiA {ECO:0000255|HAMAP-Rule:MF_00170}; Synonyms=ygfC;
GN OrderedLocusNames=b2914, JW5475;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-10.
RC STRAIN=K12;
RX PubMed=8366047; DOI=10.1128/jb.175.17.5628-5635.1993;
RA Hove-Jensen B., Maigaard M.;
RT "Escherichia coli rpiA gene encoding ribose phosphate isomerase A.";
RL J. Bacteriol. 175:5628-5635(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Roy I., Leadlay P.F.;
RL Submitted (JUN-1992) to the EMBL/GenBank/DDBJ databases.
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 154-219.
RC STRAIN=K12;
RX PubMed=1917830; DOI=10.1128/jb.173.19.5944-5953.1991;
RA Rex J.H., Aronson B.D., Somerville R.L.;
RT "The tdh and serA operons of Escherichia coli: mutational analysis of the
RT regulatory elements of leucine-responsive genes.";
RL J. Bacteriol. 173:5944-5953(1991).
RN [6]
RP PROTEIN SEQUENCE OF 1-12.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [7]
RP PROTEIN SEQUENCE OF 1-4.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9600841; DOI=10.1006/jmbi.1998.1726;
RA Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C.,
RA Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L.,
RA Hochstrasser D.F.;
RT "Protein identification with N and C-terminal sequence tags in proteome
RT projects.";
RL J. Mol. Biol. 278:599-608(1998).
RN [8]
RP FUNCTION.
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 [9]
RP INDUCTION.
RX PubMed=11945603; DOI=10.1016/0014-5793(71)80202-8;
RA Skinner A.J., Cooper R.A.;
RT "The regulation of ribose-5-phosphate isomerisation in Escherichia coli
RT K12.";
RL FEBS Lett. 12:293-296(1971).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL 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 [11]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS).
RX PubMed=12211039; DOI=10.1002/prot.10203;
RA Rangarajan E.S., Sivaraman J., Matte A., Cygler M.;
RT "Crystal structure of D-ribose-5-phosphate isomerase (RpiA) from
RT Escherichia coli.";
RL Proteins 48:737-740(2002).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS,
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-81; ASP-84 AND LYS-94,
RP ACTIVE SITE, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, REACTION
RP MECHANISM, SUBSTRATE SPECIFICITY, INDUCTION, AND SUBUNIT.
RX PubMed=12517338; DOI=10.1016/s0969-2126(02)00933-4;
RA Zhang R.G., Andersson C.E., Savchenko A., Skarina T., Evdokimova E.,
RA Beasley S., Arrowsmith C.H., Edwards A.M., Joachimiak A., Mowbray S.L.;
RT "Structure of Escherichia coli ribose-5-phosphate isomerase: a ubiquitous
RT enzyme of the pentose phosphate pathway and the Calvin cycle.";
RL Structure 11:31-42(2003).
CC -!- FUNCTION: Involved in the first step of the non-oxidative branch of the
CC pentose phosphate pathway. It catalyzes the reversible conversion of
CC ribose-5-phosphate to ribulose 5-phosphate. Can also act on D-ribose-5-
CC diphosphate and D-ribose-5-triphosphate as substrate.
CC {ECO:0000269|PubMed:1104357, ECO:0000269|PubMed:12517338,
CC ECO:0000269|PubMed:4909663}.
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:0000255|HAMAP-Rule:MF_00170,
CC ECO:0000269|PubMed:1104357, ECO:0000269|PubMed:12517338};
CC -!- ACTIVITY REGULATION: Inhibited by arabinose-5-phosphate, D-erythrose-4-
CC phosphate and D-erythronic acid. {ECO:0000269|PubMed:12517338}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.1 mM for ribose-5-phosphate {ECO:0000269|PubMed:12517338};
CC KM=4.4 mM for D-ribose 5-phosphate (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:1104357};
CC Note=kcat is 2100 sec(-1) for ribose-5-phosphate.;
CC Temperature dependence:
CC After incubation at 45 degrees Celsius for 30 minutes RpiA retains
CC 90% of its original activities. {ECO:0000269|PubMed:1104357,
CC ECO:0000269|PubMed:12517338};
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-ribose
CC 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step
CC 1/1. {ECO:0000255|HAMAP-Rule:MF_00170}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00170,
CC ECO:0000269|PubMed:12517338}.
CC -!- INTERACTION:
CC P0A7Z0; P0A7Z0: rpiA; NbExp=2; IntAct=EBI-909486, EBI-909486;
CC -!- INDUCTION: Constitutively expressed. {ECO:0000269|PubMed:1104357,
CC ECO:0000269|PubMed:11945603, ECO:0000269|PubMed:12517338}.
CC -!- SIMILARITY: Belongs to the ribose 5-phosphate isomerase family.
CC {ECO:0000255|HAMAP-Rule:MF_00170}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA47309.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X73026; CAA51509.1; -; Genomic_DNA.
DR EMBL; X66836; CAA47309.1; ALT_INIT; Genomic_DNA.
DR EMBL; U28377; AAA69081.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75951.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76978.1; -; Genomic_DNA.
DR EMBL; M64630; AAA73015.1; -; Genomic_DNA.
DR PIR; A65076; A65076.
DR RefSeq; NP_417389.1; NC_000913.3.
DR RefSeq; WP_000189743.1; NZ_STEB01000001.1.
DR PDB; 1KS2; X-ray; 1.50 A; A/B=1-219.
DR PDB; 1LKZ; X-ray; 2.50 A; A/B=1-219.
DR PDB; 1O8B; X-ray; 1.25 A; A/B=1-219.
DR PDBsum; 1KS2; -.
DR PDBsum; 1LKZ; -.
DR PDBsum; 1O8B; -.
DR AlphaFoldDB; P0A7Z0; -.
DR SMR; P0A7Z0; -.
DR BioGRID; 4259674; 24.
DR DIP; DIP-10739N; -.
DR STRING; 511145.b2914; -.
DR SWISS-2DPAGE; P0A7Z0; -.
DR jPOST; P0A7Z0; -.
DR PaxDb; P0A7Z0; -.
DR PRIDE; P0A7Z0; -.
DR EnsemblBacteria; AAC75951; AAC75951; b2914.
DR EnsemblBacteria; BAE76978; BAE76978; BAE76978.
DR GeneID; 66673209; -.
DR GeneID; 947407; -.
DR KEGG; ecj:JW5475; -.
DR KEGG; eco:b2914; -.
DR PATRIC; fig|1411691.4.peg.3819; -.
DR EchoBASE; EB1413; -.
DR eggNOG; COG0120; Bacteria.
DR HOGENOM; CLU_056590_1_1_6; -.
DR InParanoid; P0A7Z0; -.
DR OMA; YDWDEVN; -.
DR PhylomeDB; P0A7Z0; -.
DR BioCyc; EcoCyc:RIB5PISOMA-MON; -.
DR BioCyc; MetaCyc:RIB5PISOMA-MON; -.
DR BRENDA; 5.3.1.6; 2026.
DR SABIO-RK; P0A7Z0; -.
DR UniPathway; UPA00115; UER00412.
DR EvolutionaryTrace; P0A7Z0; -.
DR PRO; PR:P0A7Z0; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0004751; F:ribose-5-phosphate isomerase activity; IDA:EcoCyc.
DR GO; GO:0006014; P:D-ribose metabolic process; IMP:EcoCyc.
DR GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; IBA:GO_Central.
DR CDD; cd01398; RPI_A; 1.
DR HAMAP; MF_00170; Rib_5P_isom_A; 1.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR InterPro; IPR020672; Ribose5P_isomerase_typA_subgr.
DR InterPro; IPR004788; Ribose5P_isomerase_type_A.
DR PANTHER; PTHR11934; PTHR11934; 1.
DR Pfam; PF06026; Rib_5-P_isom_A; 1.
DR SUPFAM; SSF100950; SSF100950; 1.
DR TIGRFAMs; TIGR00021; rpiA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Isomerase; Reference proteome.
FT CHAIN 1..219
FT /note="Ribose-5-phosphate isomerase A"
FT /id="PRO_0000158412"
FT ACT_SITE 103
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170,
FT ECO:0000269|PubMed:12517338"
FT BINDING 28..31
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12517338"
FT BINDING 81..84
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12517338"
FT BINDING 94..97
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12517338"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:12517338"
FT MUTAGEN 81
FT /note="D->A: Catalytic efficiency decreases by 10,000-fold,
FT with no measurable effect on affinity binding."
FT /evidence="ECO:0000269|PubMed:12517338"
FT MUTAGEN 84
FT /note="D->A: Activity decreases by 250-fold, with little
FT change on affinity binding."
FT /evidence="ECO:0000269|PubMed:12517338"
FT MUTAGEN 94
FT /note="K->A: Has a 1500-fold lower Catalytic efficiency
FT than the wild-type, but affinity binding is increased by a
FT factor of seven."
FT /evidence="ECO:0000269|PubMed:12517338"
FT HELIX 3..13
FT /evidence="ECO:0007829|PDB:1O8B"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:1O8B"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:1O8B"
FT HELIX 32..40
FT /evidence="ECO:0007829|PDB:1O8B"
FT TURN 41..45
FT /evidence="ECO:0007829|PDB:1O8B"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:1O8B"
FT HELIX 56..62
FT /evidence="ECO:0007829|PDB:1O8B"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:1O8B"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:1O8B"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:1O8B"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:1KS2"
FT HELIX 100..109
FT /evidence="ECO:0007829|PDB:1O8B"
FT STRAND 110..118
FT /evidence="ECO:0007829|PDB:1O8B"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:1O8B"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:1O8B"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:1O8B"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:1O8B"
FT HELIX 140..149
FT /evidence="ECO:0007829|PDB:1O8B"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:1O8B"
FT STRAND 167..173
FT /evidence="ECO:0007829|PDB:1O8B"
FT HELIX 179..187
FT /evidence="ECO:0007829|PDB:1O8B"
FT STRAND 192..198
FT /evidence="ECO:0007829|PDB:1O8B"
FT STRAND 204..210
FT /evidence="ECO:0007829|PDB:1O8B"
FT STRAND 213..217
FT /evidence="ECO:0007829|PDB:1O8B"
SQ SEQUENCE 219 AA; 22860 MW; B53C49CC3DB188BC CRC64;
MTQDELKKAV GWAALQYVQP GTIVGVGTGS TAAHFIDALG TMKGQIEGAV SSSDASTEKL
KSLGIHVFDL NEVDSLGIYV DGADEINGHM QMIKGGGAAL TREKIIASVA EKFICIADAS
KQVDILGKFP LPVEVIPMAR SAVARQLVKL GGRPEYRQGV VTDNGNVILD VHGMEILDPI
AMENAINAIP GVVTVGLFAN RGADVALIGT PDGVKTIVK
