ARAD_ECOLI
ID ARAD_ECOLI Reviewed; 231 AA.
AC P08203;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=L-ribulose-5-phosphate 4-epimerase AraD {ECO:0000255|HAMAP-Rule:MF_00989, ECO:0000303|PubMed:3549454};
DE EC=5.1.3.4 {ECO:0000255|HAMAP-Rule:MF_00989, ECO:0000269|PubMed:10769138, ECO:0000269|PubMed:10769139, ECO:0000269|PubMed:11732896, ECO:0000269|PubMed:4879898, ECO:0000269|PubMed:9548961};
DE AltName: Full=Phosphoribulose isomerase {ECO:0000255|HAMAP-Rule:MF_00989};
GN Name=araD {ECO:0000255|HAMAP-Rule:MF_00989, ECO:0000303|PubMed:3549454};
GN OrderedLocusNames=b0061, JW0060;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=B;
RX PubMed=3549454; DOI=10.1016/0378-1119(86)90067-3;
RA Lee N., Gielow W., Martin R., Hamilton E., Fowler A.;
RT "The organization of the araBAD operon of Escherichia coli.";
RL Gene 47:231-244(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2261080; DOI=10.1089/dna.1990.9.631;
RA Chen H., Sun Y., Stark T., Beattie W., Moses R.E.;
RT "Nucleotide sequence and deletion analysis of the polB gene of Escherichia
RT coli.";
RL DNA Cell Biol. 9:631-635(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2251150; DOI=10.1093/nar/18.22.6722;
RA Mineno J., Fukui H., Ishino Y., Kato I., Shinagawa H.;
RT "Nucleotide sequence of the araD gene of Escherichia coli K12 encoding the
RT L-ribulose 5-phosphate 4-epimerase.";
RL Nucleic Acids Res. 18:6722-6722(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1630901; DOI=10.1093/nar/20.13.3305;
RA Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K.,
RA Mizobuchi K., Nakata A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 0-
RT 2.4 min region.";
RL Nucleic Acids Res. 20:3305-3308(1992).
RN [5]
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 [6]
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 [7]
RP PROTEIN SEQUENCE OF 1-8, AND PRELIMINARY CRYSTALLIZATION.
RX PubMed=8520491; DOI=10.1002/pro.5560040823;
RA Andersson A., Schneider G., Lindqvist Y.;
RT "Purification and preliminary X-ray crystallographic studies of recombinant
RT L-ribulose-5-phosphate 4-epimerase from Escherichia coli.";
RL Protein Sci. 4:1648-1650(1995).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 158-231.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=2034216; DOI=10.1007/bf00273583;
RA Iwasaki H., Ishino Y., Toh H., Nakata A., Shinagawa H.;
RT "Escherichia coli DNA polymerase II is homologous to alpha-like DNA
RT polymerases.";
RL Mol. Gen. Genet. 226:24-33(1991).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 222-231.
RC STRAIN=K12;
RX PubMed=2217198; DOI=10.1073/pnas.87.19.7663;
RA Bonner C.A., Hays S., McEntee K., Goodman M.F.;
RT "DNA polymerase II is encoded by the DNA damage-inducible dinA gene of
RT Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:7663-7667(1990).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=13890280; DOI=10.1128/jb.84.1.137-146.1962;
RA Englesberg E., Anderson R.L., Weinberg R., Lee N., Hoffee P.,
RA Huttenhauer G., Boyer H.;
RT "L-Arabinose-sensitive, L-ribulose 5-phosphate 4-epimerase-deficient
RT mutants of Escherichia coli.";
RL J. Bacteriol. 84:137-146(1962).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=B/R;
RX PubMed=4879898; DOI=10.1016/s0021-9258(18)93175-3;
RA Lee N., Patrick J.W., Masson M.;
RT "Crystalline L-ribulose 5-phosphate 4-epimerase from Escherichia coli.";
RL J. Biol. Chem. 243:4700-4705(1968).
RN [12]
RP INDUCTION.
RX PubMed=328165; DOI=10.1016/0092-8674(77)90072-1;
RA Hirsh J., Schleif R.;
RT "The araC promoter: transcription, mapping and interaction with the araBAD
RT promoter.";
RL Cell 11:545-550(1977).
RN [13]
RP INDUCTION.
RX PubMed=2962192; DOI=10.1073/pnas.84.24.8814;
RA Lee N., Francklyn C., Hamilton E.P.;
RT "Arabinose-induced binding of AraC protein to araI2 activates the araBAD
RT operon promoter.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:8814-8818(1987).
RN [14]
RP INDUCTION.
RX PubMed=7768852; DOI=10.1128/jb.177.12.3438-3442.1995;
RA Johnson C.M., Schleif R.F.;
RT "In vivo induction kinetics of the arabinose promoters in Escherichia
RT coli.";
RL J. Bacteriol. 177:3438-3442(1995).
RN [15]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [16]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF
RP ASP-76; HIS-95 AND HIS-97, MASS SPECTROMETRY, COFACTOR, AND SUBUNIT.
RX PubMed=9548961; DOI=10.1021/bi972984j;
RA Johnson A.E., Tanner M.E.;
RT "Epimerization via carbon-carbon bond cleavage. L-ribulose-5-phosphate 4-
RT epimerase as a masked class II aldolase.";
RL Biochemistry 37:5746-5754(1998).
RN [17]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND REACTION
RP MECHANISM.
RX PubMed=10769138; DOI=10.1021/bi992894+;
RA Lee L.V., Vu M.V., Cleland W.W.;
RT "13C and deuterium isotope effects suggest an aldol cleavage mechanism for
RT L-ribulose-5-phosphate 4-epimerase.";
RL Biochemistry 39:4808-4820(2000).
RN [18]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF
RP HIS-95; HIS-97 AND TYR-229, AND COFACTOR.
RX PubMed=10769139; DOI=10.1021/bi9928952;
RA Lee L.V., Poyner R.R., Vu M.V., Cleland W.W.;
RT "Role of metal ions in the reaction catalyzed by L-ribulose-5-phosphate 4-
RT epimerase.";
RL Biochemistry 39:4821-4830(2000).
RN [19]
RP INDUCTION.
RX PubMed=10913097; DOI=10.1128/jb.182.16.4625-4627.2000;
RA Ibanez E., Gimenez R., Pedraza T., Baldoma L., Aguilar J., Badia J.;
RT "Role of the yiaR and yiaS genes of Escherichia coli in metabolism of
RT endogenously formed L-xylulose.";
RL J. Bacteriol. 182:4625-4627(2000).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH ZINC ION, COFACTOR,
RP AND SUBUNIT.
RX PubMed=11732895; DOI=10.1021/bi0112513;
RA Luo Y., Samuel J., Mosimann S.C., Lee J.E., Tanner M.E., Strynadka N.C.;
RT "The structure of L-ribulose-5-phosphate 4-epimerase: an aldolase-like
RT platform for epimerization.";
RL Biochemistry 40:14763-14771(2001).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANT ASN-120 IN COMPLEX WITH
RP ZINC ION, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP MUTAGENESIS OF ASN-28; LYS-42; ASP-76; THR-116; ASP-120; GLU-142; HIS-218
RP AND TYR-229, ACTIVITY REGULATION, COFACTOR, ACTIVE SITE, REACTION
RP MECHANISM, AND SUBUNIT.
RX PubMed=11732896; DOI=10.1021/bi011252v;
RA Samuel J., Luo Y., Morgan P.M., Strynadka N.C., Tanner M.E.;
RT "Catalysis and binding in L-ribulose-5-phosphate 4-epimerase: a comparison
RT with L-fuculose-1-phosphate aldolase.";
RL Biochemistry 40:14772-14780(2001).
CC -!- FUNCTION: Involved in the degradation of L-arabinose (PubMed:13890280).
CC Catalyzes the interconversion of L-ribulose 5-phosphate (LRu5P) and D-
CC xylulose 5-phosphate (D-Xu5P) via a retroaldol/aldol mechanism (carbon-
CC carbon bond cleavage analogous to a class II aldolase reaction).
CC {ECO:0000255|HAMAP-Rule:MF_00989, ECO:0000269|PubMed:10769138,
CC ECO:0000269|PubMed:10769139, ECO:0000269|PubMed:11732896,
CC ECO:0000269|PubMed:13890280, ECO:0000269|PubMed:4879898,
CC ECO:0000269|PubMed:9548961}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-ribulose 5-phosphate = D-xylulose 5-phosphate;
CC Xref=Rhea:RHEA:22368, ChEBI:CHEBI:57737, ChEBI:CHEBI:58226;
CC EC=5.1.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00989,
CC ECO:0000269|PubMed:10769138, ECO:0000269|PubMed:10769139,
CC ECO:0000269|PubMed:11732896, ECO:0000269|PubMed:4879898,
CC ECO:0000269|PubMed:9548961};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00989,
CC ECO:0000269|PubMed:10769139, ECO:0000269|PubMed:11732895,
CC ECO:0000269|PubMed:11732896, ECO:0000269|PubMed:9548961};
CC Note=Binds 1 zinc ion per subunit (PubMed:9548961, PubMed:10769139,
CC PubMed:11732895, PubMed:11732896). Also able to use cobalt and
CC manganese ions, but less efficiently (PubMed:10769139).
CC {ECO:0000255|HAMAP-Rule:MF_00989, ECO:0000269|PubMed:10769139,
CC ECO:0000269|PubMed:11732895, ECO:0000269|PubMed:11732896,
CC ECO:0000269|PubMed:9548961};
CC -!- ACTIVITY REGULATION: Inhibited by glycolohydroxamate at concentration
CC above 0.1 mM. {ECO:0000269|PubMed:11732896}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.17 uM for Zn(2+) {ECO:0000269|PubMed:10769139};
CC KM=0.29 uM for Co(2+) {ECO:0000269|PubMed:10769139};
CC KM=0.54 uM for Mn(2+) {ECO:0000269|PubMed:10769139};
CC KM=47 uM for L-ribulose 5-phosphate (LRu5P) (with zinc ion)
CC {ECO:0000269|PubMed:10769139, ECO:0000269|PubMed:11732896};
CC KM=87 uM for L-ribulose 5-phosphate (LRu5P) (with zinc ion)
CC {ECO:0000269|PubMed:9548961};
CC KM=95 uM for L-ribulose 5-phosphate (LRu5P) (with zinc ion)
CC {ECO:0000269|PubMed:4879898};
CC KM=110 uM for L-ribulose 5-phosphate (LRu5P) (with cobalt ion)
CC {ECO:0000269|PubMed:10769139};
CC KM=425 uM for L-ribulose 5-phosphate (LRu5P) (with manganese ion)
CC {ECO:0000269|PubMed:10769139};
CC Note=kcat is 20.4 sec(-1) for L-ribulose 5-phosphate (LRu5P) as
CC substrate (PubMed:9548961). kcat is 19.4 sec(-1) for L-ribulose 5-
CC phosphate (LRu5P) as substrate (PubMed:11732896). kcat is 17.3 sec(-
CC 1) for L-ribulose 5-phosphate (LRu5P) as substrate (PubMed:10769139).
CC kcat is 10.6 sec(-1) for L-ribulose 5-phosphate (LRu5P) as substrate
CC (at pH 7) (PubMed:10769138). kcat is 4.23 sec(-1) for L-ribulose 5-
CC phosphate (LRu5P) as substrate (at pH 5.5) (PubMed:10769138).
CC {ECO:0000269|PubMed:10769138, ECO:0000269|PubMed:10769139,
CC ECO:0000269|PubMed:11732896, ECO:0000269|PubMed:9548961};
CC pH dependence:
CC Optimum pH is 7. {ECO:0000269|PubMed:4879898};
CC -!- PATHWAY: Carbohydrate degradation; L-arabinose degradation via L-
CC ribulose; D-xylulose 5-phosphate from L-arabinose (bacterial route):
CC step 3/3. {ECO:0000255|HAMAP-Rule:MF_00989,
CC ECO:0000305|PubMed:13890280}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00989,
CC ECO:0000269|PubMed:11732895, ECO:0000269|PubMed:11732896,
CC ECO:0000269|PubMed:4879898, ECO:0000269|PubMed:9548961}.
CC -!- INDUCTION: Induced by arabinose. Transcription is dependent on the
CC transcription factor AraC, the cAMP receptor protein (CRP) and cAMP
CC (PubMed:328165, PubMed:2962192, PubMed:7768852). Also induced by L-
CC lyxose (PubMed:10913097). {ECO:0000269|PubMed:10913097,
CC ECO:0000269|PubMed:2962192, ECO:0000269|PubMed:328165,
CC ECO:0000269|PubMed:7768852}.
CC -!- MASS SPECTROMETRY: Mass=25522; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:9548961};
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene accumulate large amount
CC of L-ribulose 5-phosphate when incubated with L-arabinose.
CC {ECO:0000269|PubMed:13890280}.
CC -!- SIMILARITY: Belongs to the aldolase class II family. AraD/FucA
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00989, ECO:0000305}.
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DR EMBL; M15263; AAA23464.1; -; Genomic_DNA.
DR EMBL; M35371; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M62646; AAA24405.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73172.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96630.1; -; Genomic_DNA.
DR EMBL; M37727; AAA23683.1; -; Genomic_DNA.
DR EMBL; M38283; AAA63763.1; -; Genomic_DNA.
DR EMBL; X56048; CAA39519.1; -; Genomic_DNA.
DR PIR; E64727; ISECP4.
DR RefSeq; NP_414603.1; NC_000913.3.
DR RefSeq; WP_000888666.1; NZ_STEB01000010.1.
DR PDB; 1JDI; X-ray; 2.40 A; A/B/C/D/E/F=1-231.
DR PDB; 1K0W; X-ray; 2.10 A; A/B/C/D/E/F=1-231.
DR PDBsum; 1JDI; -.
DR PDBsum; 1K0W; -.
DR AlphaFoldDB; P08203; -.
DR SMR; P08203; -.
DR BioGRID; 4263043; 1.
DR DIP; DIP-9126N; -.
DR IntAct; P08203; 4.
DR STRING; 511145.b0061; -.
DR PaxDb; P08203; -.
DR PRIDE; P08203; -.
DR EnsemblBacteria; AAC73172; AAC73172; b0061.
DR EnsemblBacteria; BAB96630; BAB96630; BAB96630.
DR GeneID; 945294; -.
DR KEGG; ecj:JW0060; -.
DR KEGG; eco:b0061; -.
DR PATRIC; fig|1411691.4.peg.2222; -.
DR EchoBASE; EB0053; -.
DR eggNOG; COG0235; Bacteria.
DR HOGENOM; CLU_006033_5_0_6; -.
DR InParanoid; P08203; -.
DR OMA; PIFGTTH; -.
DR PhylomeDB; P08203; -.
DR BioCyc; EcoCyc:RIBULPEPIM-MON; -.
DR BioCyc; MetaCyc:RIBULPEPIM-MON; -.
DR SABIO-RK; P08203; -.
DR UniPathway; UPA00145; UER00567.
DR EvolutionaryTrace; P08203; -.
DR PRO; PR:P08203; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0032991; C:protein-containing complex; IDA:EcoCyc.
DR GO; GO:0016832; F:aldehyde-lyase activity; IBA:GO_Central.
DR GO; GO:0008742; F:L-ribulose-phosphate 4-epimerase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0019569; P:L-arabinose catabolic process to xylulose 5-phosphate; IMP:UniProtKB.
DR GO; GO:0019324; P:L-lyxose metabolic process; IMP:EcoCyc.
DR GO; GO:0019323; P:pentose catabolic process; IBA:GO_Central.
DR Gene3D; 3.40.225.10; -; 1.
DR HAMAP; MF_00989; AraD_entero; 1.
DR InterPro; IPR001303; Aldolase_II/adducin_N.
DR InterPro; IPR036409; Aldolase_II/adducin_N_sf.
DR InterPro; IPR004661; AraD.
DR InterPro; IPR033748; AraD_entero.
DR Pfam; PF00596; Aldolase_II; 1.
DR SMART; SM01007; Aldolase_II; 1.
DR SUPFAM; SSF53639; SSF53639; 1.
DR TIGRFAMs; TIGR00760; araD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Arabinose catabolism; Carbohydrate metabolism; Cobalt;
KW Direct protein sequencing; Isomerase; Manganese; Metal-binding;
KW Reference proteome; Zinc.
FT CHAIN 1..231
FT /note="L-ribulose-5-phosphate 4-epimerase AraD"
FT /id="PRO_0000162919"
FT ACT_SITE 120
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00989,
FT ECO:0000305|PubMed:11732896"
FT ACT_SITE 229
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00989,
FT ECO:0000305|PubMed:11732896"
FT BINDING 27..28
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AB87, ECO:0000255|HAMAP-
FT Rule:MF_00989"
FT BINDING 44..45
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AB87, ECO:0000255|HAMAP-
FT Rule:MF_00989"
FT BINDING 74..75
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AB87, ECO:0000255|HAMAP-
FT Rule:MF_00989"
FT BINDING 76
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00989,
FT ECO:0000305|PubMed:10769138, ECO:0000305|PubMed:9548961"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00989,
FT ECO:0000269|PubMed:11732895, ECO:0000269|PubMed:11732896,
FT ECO:0000305|PubMed:10769138, ECO:0000305|PubMed:10769139,
FT ECO:0007744|PDB:1JDI, ECO:0007744|PDB:1K0W"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00989,
FT ECO:0000269|PubMed:11732895, ECO:0000269|PubMed:11732896,
FT ECO:0000305|PubMed:10769138, ECO:0000305|PubMed:10769139,
FT ECO:0007744|PDB:1JDI, ECO:0007744|PDB:1K0W"
FT BINDING 171
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00989,
FT ECO:0000269|PubMed:11732895, ECO:0000269|PubMed:11732896,
FT ECO:0000305|PubMed:10769138, ECO:0007744|PDB:1JDI,
FT ECO:0007744|PDB:1K0W"
FT MUTAGEN 28
FT /note="N->A: Strong decrease of the affinity for L-ribulose
FT 5-phosphate (LRu5P)."
FT /evidence="ECO:0000269|PubMed:11732896"
FT MUTAGEN 42
FT /note="K->M: Strong decrease of the affinity for L-ribulose
FT 5-phosphate (LRu5P)."
FT /evidence="ECO:0000269|PubMed:11732896"
FT MUTAGEN 76
FT /note="D->N: Mutant shows a strong decrease of the
FT catalytic efficiency, but it retains considerable epimerase
FT activity. The affinity for L-ribulose 5-phosphate (LRu5P)
FT is relatively unaffected."
FT /evidence="ECO:0000269|PubMed:11732896,
FT ECO:0000269|PubMed:9548961"
FT MUTAGEN 95
FT /note="H->N: Mutant shows a strong decrease of the
FT catalytic efficiency and a reduced affinity for Zn(2+)."
FT /evidence="ECO:0000269|PubMed:10769139,
FT ECO:0000269|PubMed:9548961"
FT MUTAGEN 97
FT /note="H->N: Mutant shows a strong decrease of the
FT catalytic efficiency and a reduced affinity for Zn(2+).
FT Inhibited by glycolaldehyde phosphate."
FT /evidence="ECO:0000269|PubMed:10769139,
FT ECO:0000269|PubMed:9548961"
FT MUTAGEN 116
FT /note="T->E,Y: Loss of the epimerase activity due to an
FT increased steric bulk introduced by the mutation which
FT causes a conformational change that is incompatible with
FT catalysis."
FT /evidence="ECO:0000269|PubMed:11732896"
FT MUTAGEN 120
FT /note="D->N: Loss of the epimerase activity."
FT /evidence="ECO:0000269|PubMed:11732896"
FT MUTAGEN 142
FT /note="E->Q: Mutant shows a strong decrease of the
FT catalytic efficiency, but it retains considerable epimerase
FT activity. The affinity for L-ribulose 5-phosphate (LRu5P)
FT is relatively unaffected."
FT /evidence="ECO:0000269|PubMed:11732896"
FT MUTAGEN 218
FT /note="H->N: Mutant shows a strong decrease of the
FT catalytic efficiency, but it retains considerable epimerase
FT activity. The affinity for L-ribulose 5-phosphate (LRu5P)
FT is relatively unaffected."
FT /evidence="ECO:0000269|PubMed:11732896"
FT MUTAGEN 229
FT /note="Y->F: Loss of the epimerase activity."
FT /evidence="ECO:0000269|PubMed:10769139,
FT ECO:0000269|PubMed:11732896"
FT HELIX 3..18
FT /evidence="ECO:0007829|PDB:1K0W"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:1K0W"
FT TURN 34..37
FT /evidence="ECO:0007829|PDB:1K0W"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:1K0W"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:1K0W"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:1K0W"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:1K0W"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:1K0W"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:1K0W"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:1K0W"
FT HELIX 77..86
FT /evidence="ECO:0007829|PDB:1K0W"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:1K0W"
FT HELIX 99..107
FT /evidence="ECO:0007829|PDB:1K0W"
FT HELIX 116..119
FT /evidence="ECO:0007829|PDB:1K0W"
FT HELIX 134..138
FT /evidence="ECO:0007829|PDB:1K0W"
FT HELIX 141..155
FT /evidence="ECO:0007829|PDB:1K0W"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:1K0W"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:1K0W"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:1K0W"
FT STRAND 172..179
FT /evidence="ECO:0007829|PDB:1K0W"
FT HELIX 180..203
FT /evidence="ECO:0007829|PDB:1K0W"
FT HELIX 212..221
FT /evidence="ECO:0007829|PDB:1K0W"
SQ SEQUENCE 231 AA; 25519 MW; 1753F75958332163 CRC64;
MLEDLKRQVL EANLALPKHN LVTLTWGNVS AVDRERGVFV IKPSGVDYSV MTADDMVVVS
IETGEVVEGT KKPSSDTPTH RLLYQAFPSI GGIVHTHSRH ATIWAQAGQS IPATGTTHAD
YFYGTIPCTR KMTDAEINGE YEWETGNVIV ETFEKQGIDA AQMPGVLVHS HGPFAWGKNA
EDAVHNAIVL EEVAYMGIFC RQLAPQLPDM QQTLLDKHYL RKHGAKAYYG Q
