SGBE_ECOLI
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 03-AUG-2022, entry version 146.
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; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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}.
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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_SSZK01000041.1.
DR AlphaFoldDB; P37680; -.
DR SMR; P37680; -.
DR BioGRID; 4262553; 10.
DR BioGRID; 852406; 9.
DR IntAct; P37680; 13.
DR STRING; 511145.b3583; -.
DR PaxDb; P37680; -.
DR PRIDE; P37680; -.
DR EnsemblBacteria; AAC76607; AAC76607; b3583.
DR EnsemblBacteria; BAE77710; BAE77710; BAE77710.
DR GeneID; 66672528; -.
DR GeneID; 948099; -.
DR KEGG; ecj:JW3555; -.
DR KEGG; eco:b3583; -.
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 PhylomeDB; P37680; -.
DR BioCyc; EcoCyc:EG12287-MON; -.
DR BioCyc; MetaCyc:EG12287-MON; -.
DR PRO; PR:P37680; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
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 Gene3D; 3.40.225.10; -; 1.
DR InterPro; IPR001303; Aldolase_II/adducin_N.
DR InterPro; IPR036409; Aldolase_II/adducin_N_sf.
DR InterPro; IPR004661; AraD.
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 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
