ID SGBE_ECOLI Reviewed; 231 AA. AC P37680; Q2M7P6; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1994, sequence version 1. DT 10-JUN-2026, entry version 160. DE RecName: Full=L-ribulose-5-phosphate 4-epimerase SgbE {ECO:0000303|PubMed:11741871}; DE EC=5.1.3.4 {ECO:0000269|PubMed:11741871}; DE AltName: Full=Phosphoribulose isomerase {ECO:0000305}; GN Name=sgbE {ECO:0000303|PubMed:11741871}; Synonyms=yiaS; GN OrderedLocusNames=b3583, JW3555; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=8041620; DOI=10.1093/nar/22.13.2576; RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.; RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region RT from 76.0 to 81.5 minutes."; RL Nucleic Acids Res. 22:2576-2586(1994). RN [2] 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 [3] 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 [4] RP DISCUSSION OF SEQUENCE. RA Reizer J., Charbit A., Reizer A., Saier M.H. Jr.; RT "Novel phosphotransferases system genes revealed by bacterial genome RT analysis: operons encoding homologues of sugar-specific permease domains of RT the phosphotransferase system and pentose catabolic enzymes."; RL Genome Sci. Technol. 1:53-75(1996). RN [5] RP FUNCTION. 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 [6] RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=11741871; DOI=10.1128/jb.184.1.302-306.2002; RA Yew W.S., Gerlt J.A.; RT "Utilization of L-ascorbate by Escherichia coli K-12: assignments of RT functions to products of the yjf-sga and yia-sgb operons."; RL J. Bacteriol. 184:302-306(2002). CC -!- FUNCTION: Catalyzes the interconversion of L-ribulose 5-phosphate CC (LRu5P) and D-xylulose 5-phosphate (D-Xu5P) via a retroaldol/aldol CC mechanism (carbon-carbon bond cleavage analogous to a class II aldolase CC reaction). May be involved in the utilization of 2,3-diketo-L-gulonate. CC {ECO:0000269|PubMed:10913097, ECO:0000269|PubMed:11741871}. 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:0000269|PubMed:11741871}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000250|UniProtKB:P08203}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P08203}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=705 uM for L-ribulose 5-phosphate (LRu5P) CC {ECO:0000269|PubMed:11741871}; CC Note=kcat is 12 sec(-1) with L-ribulose 5-phosphate (LRu5P) as CC substrate. {ECO:0000269|PubMed:11741871}; CC -!- SIMILARITY: Belongs to the aldolase class II family. AraD/FucA CC subfamily. {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; U00039; AAB18560.1; -; Genomic_DNA. DR EMBL; U00096; AAC76607.1; -; Genomic_DNA. DR EMBL; AP009048; BAE77710.1; -; Genomic_DNA. DR PIR; S47804; S47804. DR RefSeq; NP_418040.1; NC_000913.3. DR RefSeq; WP_000893142.1; NZ_CP009789.1. DR AlphaFoldDB; P37680; -. DR SMR; P37680; -. DR BioGRID; 4262553; 15. DR BioGRID; 852406; 9. DR FunCoup; P37680; 407. DR IntAct; P37680; 13. DR STRING; 511145.b3583; -. DR PaxDb; 511145-b3583; -. DR EnsemblBacteria; AAC76607; AAC76607; b3583. DR GeneID; 948099; -. DR KEGG; ecj:JW3555; -. DR KEGG; eco:b3583; -. DR KEGG; ecoc:C3026_19425; -. DR PATRIC; fig|511145.12.peg.3698; -. DR EchoBASE; EB2195; -. DR eggNOG; COG0235; Bacteria. DR HOGENOM; CLU_006033_5_0_6; -. DR InParanoid; P37680; -. DR OMA; AHERYMT; -. DR OrthoDB; 9786287at2; -. DR PhylomeDB; P37680; -. DR BioCyc; EcoCyc:EG12287-MONOMER; -. DR BioCyc; MetaCyc:EG12287-MONOMER; -. DR PRO; PR:P37680; -. DR Proteomes; UP000000625; Chromosome. DR AbasyAtlas; P37680; -. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. 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; ISS:UniProtKB. DR GO; GO:0019572; P:L-arabinose catabolic process; IEA:InterPro. DR GO; GO:0019324; P:L-lyxose metabolic process; IMP:EcoCyc. DR GO; GO:0019323; P:pentose catabolic process; IMP:EcoCyc. DR CDD; cd00398; Aldolase_II; 1. DR FunFam; 3.40.225.10:FF:000001; L-ribulose-5-phosphate 4-epimerase UlaF; 1. DR Gene3D; 3.40.225.10; Class II aldolase/adducin N-terminal domain; 1. DR InterPro; IPR050197; Aldolase_class_II_sugar_metab. DR InterPro; IPR001303; Aldolase_II/adducin_N. DR InterPro; IPR036409; Aldolase_II/adducin_N_sf. DR InterPro; IPR004661; AraD. DR NCBIfam; TIGR00760; araD; 1. DR NCBIfam; NF006047; PRK08193.1; 1. DR NCBIfam; NF009002; PRK12347.1; 1. DR NCBIfam; NF009003; PRK12348.1; 1. DR PANTHER; PTHR22789; FUCULOSE PHOSPHATE ALDOLASE; 1. DR PANTHER; PTHR22789:SF8; L-RIBULOSE-5-PHOSPHATE 4-EPIMERASE SGBE; 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 Carbohydrate metabolism; Isomerase; Metal-binding; Reference proteome; KW Zinc. FT CHAIN 1..231 FT /note="L-ribulose-5-phosphate 4-epimerase SgbE" FT /id="PRO_0000162923" FT ACT_SITE 120 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000250|UniProtKB:P08203" FT ACT_SITE 229 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000250|UniProtKB:P08203" FT BINDING 27..28 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P0AB87" FT BINDING 44..45 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P0AB87" FT BINDING 74..75 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P0AB87" FT BINDING 76 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:P08203" FT BINDING 95 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:P08203" FT BINDING 97 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:P08203" FT BINDING 171 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:P08203" SQ SEQUENCE 231 AA; 25561 MW; F4FF4D7EC2A80B3A CRC64; MLEQLKADVL AANLALPAHH LVTFTWGNVS AVDETRQWMV IKPSGVEYDV MTADDMVVVE IASGKVVEGS KKPSSDTPTH LALYRRYAEI GGIVHTHSRH ATIWSQAGLD LPAWGTTHAD YFYGAIPCTR QMTAEEINGE YEYQTGEVII ETFEERGRSP AQIPAVLVHS HGPFAWGKNA ADAVHNAVVL EECAYMGLFS RQLAPQLPAM QNELLDKHYL RKHGANAYYG Q //