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 27-MAR-2024, entry version 192. 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, GN ECO:0000303|PubMed:3549454}; OrderedLocusNames=b0061, JW0060; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadota; 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 RT 0-2.4 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; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00989, ECO:0000269|PubMed:10769139, CC ECO:0000269|PubMed:11732895, ECO:0000269|PubMed:11732896, CC 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 CC 5-phosphate (LRu5P) as substrate (PubMed:11732896). kcat is 17.3 CC sec(-1) for L-ribulose 5-phosphate (LRu5P) as substrate CC (PubMed:10769139). kcat is 10.6 sec(-1) for L-ribulose 5-phosphate CC (LRu5P) as substrate (at pH 7) (PubMed:10769138). kcat is 4.23 CC sec(-1) for L-ribulose 5-phosphate (LRu5P) as substrate (at pH 5.5) CC (PubMed:10769138). {ECO:0000269|PubMed:10769138, CC ECO:0000269|PubMed:10769139, ECO:0000269|PubMed:11732896, CC 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}. 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; 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; 511145-b0061; -. DR EnsemblBacteria; AAC73172; AAC73172; b0061. DR GeneID; 83578001; -. 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; PCVLTMM; -. DR OrthoDB; 9786287at2; -. DR PhylomeDB; P08203; -. DR BioCyc; EcoCyc:RIBULPEPIM-MONOMER; -. DR BioCyc; MetaCyc:RIBULPEPIM-MONOMER; -. 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:0042802; F:identical protein binding; IDA:EcoCyc. 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 CDD; cd00398; Aldolase_II; 1. DR Gene3D; 3.40.225.10; Class II aldolase/adducin N-terminal domain; 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 NCBIfam; TIGR00760; araD; 1. DR PANTHER; PTHR22789; FUCULOSE PHOSPHATE ALDOLASE; 1. DR PANTHER; PTHR22789:SF15; L-RIBULOSE-5-PHOSPHATE 4-EPIMERASE ARAD; 1. DR Pfam; PF00596; Aldolase_II; 1. DR SMART; SM01007; Aldolase_II; 1. DR SUPFAM; SSF53639; AraD/HMP-PK domain-like; 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 //