DLMIS_ECO57
ID DLMIS_ECO57 Reviewed; 227 AA.
AC A0A6M7H989;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2022, sequence version 1.
DT 03-AUG-2022, entry version 3.
DE RecName: Full=D-lyxose/D-mannose isomerase {ECO:0000305};
DE EC=5.3.1.15 {ECO:0000269|PubMed:20615418};
DE EC=5.3.1.7 {ECO:0000269|PubMed:20615418};
GN OrderedLocusNames=Z5688 {ECO:0000312|EMBL:AAG59285.1};
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2] {ECO:0007744|PDB:3KMH, ECO:0007744|PDB:3MPB}
RP X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) IN COMPLEXES WITH FRUCTOSE AND
RP MANGANESE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, DISULFIDE BOND, AND MUTAGENESIS OF LYS-90; LYS-108;
RP GLU-110; GLU-186; ASP-193 AND ARG-205.
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=20615418; DOI=10.1016/j.jmb.2010.06.063;
RA van Staalduinen L.M., Park C.S., Yeom S.J., Adams-Cioaba M.A., Oh D.K.,
RA Jia Z.;
RT "Structure-based annotation of a novel sugar isomerase from the pathogenic
RT E. coli O157:H7.";
RL J. Mol. Biol. 401:866-881(2010).
CC -!- FUNCTION: Sugar isomerase that catalyzes the reversible isomerization
CC of D-lyxose to D-xylulose, and D-mannose to D-fructose
CC (PubMed:20615418). Shows similar activity toward D-lyxose and D-mannose
CC with a turnover and catalytic efficiency for D-lyxose as a substrate
CC only 1.1- and 1.3-fold higher than those for D-mannose, respectively
CC (PubMed:20615418). Shows weaker activity with L-gulose, D-talose, L-
CC ribose and L-allose (PubMed:20615418). Overexpression enables cell
CC growth on the rare pentose D-lyxose as the sole carbon source
CC (PubMed:20615418). {ECO:0000269|PubMed:20615418}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-lyxose = D-xylulose; Xref=Rhea:RHEA:14201,
CC ChEBI:CHEBI:16789, ChEBI:CHEBI:17140; EC=5.3.1.15;
CC Evidence={ECO:0000269|PubMed:20615418};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-mannose = D-fructose; Xref=Rhea:RHEA:22604,
CC ChEBI:CHEBI:4208, ChEBI:CHEBI:37721; EC=5.3.1.7;
CC Evidence={ECO:0000269|PubMed:20615418};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:20615418};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=16.1 mM for D-lyxose {ECO:0000269|PubMed:20615418};
CC KM=19.8 mM for D-mannose {ECO:0000269|PubMed:20615418};
CC KM=55.2 mM for L-gulose {ECO:0000269|PubMed:20615418};
CC Vmax=14.1 umol/min/mg enzyme with D-lyxose as substrate
CC {ECO:0000269|PubMed:20615418};
CC Vmax=13.1 umol/min/mg enzyme with D-mannose as substrate
CC {ECO:0000269|PubMed:20615418};
CC Vmax=9.09 umol/min/mg enzyme with L-gulose as substrate
CC {ECO:0000269|PubMed:20615418};
CC Note=kcat is 13.7 sec(-1) with D-lyxose as substrate. kcat is 12.7
CC sec(-1) with D-mannose as substrate. kcat is 8.78 sec(-1) with L-
CC gulose as substrate. {ECO:0000269|PubMed:20615418};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:20615418};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.
CC {ECO:0000269|PubMed:20615418};
CC -!- SUBUNIT: Homodimer; disulfide-linked (PubMed:20615418). Dimerization is
CC facilitated through a disulfide bond between the two monomers of the
CC dimeric enzyme (PubMed:20615418). {ECO:0000269|PubMed:20615418}.
CC -!- SIMILARITY: Belongs to the D-lyxose ketol-isomerase family.
CC {ECO:0000305}.
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DR EMBL; AE005174; AAG59285.1; -; Genomic_DNA.
DR PIR; A86103; A86103.
DR PIR; F91262; F91262.
DR PDB; 3KMH; X-ray; 1.58 A; A/B=1-227.
DR PDB; 3MPB; X-ray; 1.91 A; A/B=1-227.
DR PDBsum; 3KMH; -.
DR PDBsum; 3MPB; -.
DR SMR; A0A6M7H989; -.
DR KEGG; ece:Z5688; -.
DR PATRIC; fig|386585.9.peg.5298; -.
DR Proteomes; UP000002519; Chromosome.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR010864; D-lyxose_isomer.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR Pfam; PF07385; Lyx_isomer; 1.
DR SUPFAM; SSF51182; SSF51182; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Disulfide bond; Isomerase;
KW Manganese; Metal-binding.
FT CHAIN 1..227
FT /note="D-lyxose/D-mannose isomerase"
FT /id="PRO_0000455823"
FT BINDING 90
FT /ligand="D-fructose"
FT /ligand_id="ChEBI:CHEBI:37721"
FT /evidence="ECO:0000269|PubMed:20615418,
FT ECO:0007744|PDB:3MPB"
FT BINDING 103..110
FT /ligand="D-fructose"
FT /ligand_id="ChEBI:CHEBI:37721"
FT /evidence="ECO:0000269|PubMed:20615418,
FT ECO:0007744|PDB:3MPB"
FT BINDING 103
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:20615418,
FT ECO:0007744|PDB:3KMH, ECO:0007744|PDB:3MPB"
FT BINDING 105
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:20615418,
FT ECO:0007744|PDB:3KMH, ECO:0007744|PDB:3MPB"
FT BINDING 110
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:20615418,
FT ECO:0007744|PDB:3KMH, ECO:0007744|PDB:3MPB"
FT BINDING 171
FT /ligand="D-fructose"
FT /ligand_id="ChEBI:CHEBI:37721"
FT /evidence="ECO:0000269|PubMed:20615418,
FT ECO:0007744|PDB:3MPB"
FT BINDING 171
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:20615418,
FT ECO:0007744|PDB:3KMH, ECO:0007744|PDB:3MPB"
FT BINDING 186
FT /ligand="D-fructose"
FT /ligand_id="ChEBI:CHEBI:37721"
FT /evidence="ECO:0000269|PubMed:20615418,
FT ECO:0007744|PDB:3MPB"
FT BINDING 193
FT /ligand="D-fructose"
FT /ligand_id="ChEBI:CHEBI:37721"
FT /evidence="ECO:0000269|PubMed:20615418,
FT ECO:0007744|PDB:3MPB"
FT DISULFID 86
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:20615418,
FT ECO:0007744|PDB:3KMH, ECO:0007744|PDB:3MPB"
FT MUTAGEN 90
FT /note="K->A: Retains 0.7% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:20615418"
FT MUTAGEN 108
FT /note="K->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:20615418"
FT MUTAGEN 110
FT /note="E->A: Retains 1.4% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:20615418"
FT MUTAGEN 186
FT /note="E->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:20615418"
FT MUTAGEN 193
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:20615418"
FT MUTAGEN 205
FT /note="R->A: Retains 9% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:20615418"
SQ SEQUENCE 227 AA; 25798 MW; BBB0DB4FD786E50C CRC64;
MKRSAINDIL GHTRQFFSQH DVHLPPFASF SPAQWQQLDT AAWEEVFDLK LGWDVTAFGR
NNFAAHGLTL FTLRNGSAKG MPYVKCYAEK IMHVRDAQVT PMHFHWRKRE DIINRGGGNL
IVELWNADSN EQTADSDITV VIDGCRQKHT AGSQLRLSPG ESICLPPGLY HSFWAEAGFG
DVLVGEVSSV NDDDHDNHFL QPLDRYNLID EDEPAQLVLC NEYRQFR
