ID   SGBU_ECOLI              Reviewed;         286 AA.
AC   P37679; Q2M7P5;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 2.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Putative L-ribulose-5-phosphate 3-epimerase SgbU;
DE            EC=5.1.3.22;
DE   AltName: Full=L-xylulose-5-phosphate 3-epimerase;
GN   Name=sgbU; Synonyms=yiaR; OrderedLocusNames=b3582, JW5650;
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   PUTATIVE 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).
CC   -!- FUNCTION: Catalyzes the isomerization of L-xylulose-5-phosphate to L-
CC       ribulose-5-phosphate (Potential). May be involved in the utilization of
CC       2,3-diketo-L-gulonate. {ECO:0000305}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-ribulose 5-phosphate = L-xylulose 5-phosphate;
CC         Xref=Rhea:RHEA:18497, ChEBI:CHEBI:57829, ChEBI:CHEBI:58226;
CC         EC=5.1.3.22;
CC   -!- SIMILARITY: Belongs to the L-ribulose-5-phosphate 3-epimerase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB18559.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; U00039; AAB18559.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U00096; AAC76606.2; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77711.1; -; Genomic_DNA.
DR   PIR; S47803; S47803.
DR   RefSeq; NP_418039.2; NC_000913.3.
DR   RefSeq; WP_001350555.1; NZ_LN832404.1.
DR   AlphaFoldDB; P37679; -.
DR   SMR; P37679; -.
DR   BioGRID; 4259345; 3.
DR   STRING; 511145.b3582; -.
DR   PaxDb; P37679; -.
DR   PRIDE; P37679; -.
DR   EnsemblBacteria; AAC76606; AAC76606; b3582.
DR   EnsemblBacteria; BAE77711; BAE77711; BAE77711.
DR   GeneID; 948100; -.
DR   KEGG; ecj:JW5650; -.
DR   KEGG; eco:b3582; -.
DR   PATRIC; fig|511145.12.peg.3697; -.
DR   EchoBASE; EB2194; -.
DR   eggNOG; COG3623; Bacteria.
DR   HOGENOM; CLU_082738_0_0_6; -.
DR   InParanoid; P37679; -.
DR   OMA; CKGQFRD; -.
DR   PhylomeDB; P37679; -.
DR   BioCyc; EcoCyc:EG12286-MON; -.
DR   PRO; PR:P37679; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0016861; F:intramolecular oxidoreductase activity, interconverting aldoses and ketoses; IEA:InterPro.
DR   GO; GO:0034015; F:L-ribulose-5-phosphate 3-epimerase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   GO; GO:0019852; P:L-ascorbic acid metabolic process; IBA:GO_Central.
DR   GO; GO:0019324; P:L-lyxose metabolic process; IMP:EcoCyc.
DR   CDD; cd00019; AP2Ec; 1.
DR   InterPro; IPR001719; AP_endonuc_2.
DR   InterPro; IPR004560; L-Ru-5P_3-Epase.
DR   InterPro; IPR036237; Xyl_isomerase-like_sf.
DR   InterPro; IPR013022; Xyl_isomerase-like_TIM-brl.
DR   Pfam; PF01261; AP_endonuc_2; 1.
DR   SUPFAM; SSF51658; SSF51658; 1.
DR   TIGRFAMs; TIGR00542; hxl6Piso_put; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Isomerase; Reference proteome.
FT   CHAIN           1..286
FT                   /note="Putative L-ribulose-5-phosphate 3-epimerase SgbU"
FT                   /id="PRO_0000097718"
SQ   SEQUENCE   286 AA;  32455 MW;  4C849F575E937BF9 CRC64;
     MRNHQLGIYE KALAKDLSWP ERLVLAKSCG FDFVEMSVDE TDERLSRLDW SAAQRTSLVA
     AMIETGVGIP SMCLSAHRRF PFGSRDEAVR ERAREIMSKA IRLARDLGIR TIQLAGYDVY
     YEDHDEGTRQ RFAEGLAWAV EQAAASQVML AVEIMDTAFM NSISKWKKWD EMLASPWFTV
     YPDVGNLSAW GNDVPAELKL GIDRIAAIHL KDTQPVTGQS PGQFRDVPFG EGCVDFVGIF
     KTLHKLNYRG SFLIEMWTEK AKEPVLEIIQ ARRWIEARMQ EAGFIC