DLYKI_COHLA
ID DLYKI_COHLA Reviewed; 182 AA.
AC A3E7Z6;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=D-lyxose ketol-isomerase {ECO:0000303|PubMed:17189362};
DE EC=5.3.1.15 {ECO:0000269|PubMed:17189362};
DE AltName: Full=D-lyxose isomerase {ECO:0000303|PubMed:17189362, ECO:0000312|EMBL:ABI93960.1};
DE AltName: Full=L-ribose isomerase {ECO:0000303|PubMed:17189362};
OS Cohnella laeviribosi.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Cohnella.
OX NCBI_TaxID=380174;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ABI93960.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-13; 23-31; 44-57
RP AND 153-160, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RC STRAIN=KCTC 3987 / CCUG 52217 / RI-39;
RX PubMed=17189362; DOI=10.1128/jb.01568-06;
RA Cho E.-A., Lee D.-W., Cha Y.-H., Lee S.-J., Jung H.-C., Pan J.-G.,
RA Pyun Y.-R.;
RT "Characterization of a novel D-lyxose isomerase from Cohnella laevoribosii
RT RI-39 sp. nov.";
RL J. Bacteriol. 189:1655-1663(2007).
CC -!- FUNCTION: Sugar isomerase that catalyzes the reversible isomerization
CC of D-lyxose to D-xylulose (PubMed:17189362). Shows weak activity with
CC D-mannose and L-ribose (PubMed:17189362).
CC {ECO:0000269|PubMed:17189362}.
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:17189362};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:17189362};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=22.4 mM for D-lyxose (in the presence of 1 mM Mn(2+))
CC {ECO:0000269|PubMed:17189362};
CC KM=121.7 mM for L-ribose (in the presence of 1 mM Mn(2+))
CC {ECO:0000269|PubMed:17189362};
CC KM=34.0 mM for D-mannose (in the presence of 1 mM Mn(2+))
CC {ECO:0000269|PubMed:17189362};
CC Vmax=5434.8 umol/min/mg enzyme toward D-lyxose (in the presence of 1
CC mM Mn(2+)) {ECO:0000269|PubMed:17189362};
CC Vmax=75.5 umol/min/mg enzyme toward L-ribose (in the presence of 1 mM
CC Mn(2+)) {ECO:0000269|PubMed:17189362};
CC Vmax=131.8 umol/min/mg enzyme toward D-mannose (in the presence of 1
CC mM Mn(2+)) {ECO:0000269|PubMed:17189362};
CC pH dependence:
CC Optimum pH is 6.5. {ECO:0000269|PubMed:17189362};
CC Temperature dependence:
CC Optimum temperature is 70 degrees Celsius.
CC {ECO:0000269|PubMed:17189362};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17189362}.
CC -!- SIMILARITY: Belongs to the D-lyxose ketol-isomerase family.
CC {ECO:0000305}.
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DR EMBL; DQ978225; ABI93960.1; -; Genomic_DNA.
DR AlphaFoldDB; A3E7Z6; -.
DR SMR; A3E7Z6; -.
DR PRIDE; A3E7Z6; -.
DR BRENDA; 5.3.1.15; 9328.
DR SABIO-RK; A3E7Z6; -.
DR GO; GO:0047828; F:D-lyxose ketol-isomerase activity; IDA:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IDA:UniProtKB.
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 Carbohydrate metabolism; Direct protein sequencing; Isomerase; Manganese;
KW Metal-binding.
FT CHAIN 1..182
FT /note="D-lyxose ketol-isomerase"
FT /id="PRO_0000352785"
FT BINDING 74
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:A0A256XLS3"
FT BINDING 76
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:A0A256XLS3"
FT BINDING 87
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:A0A256XLS3"
FT BINDING 142
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:A0A256XLS3"
SQ SEQUENCE 182 AA; 20351 MW; 7BA26F3890A4378A CRC64;
MRGTEWREAR DRVAEMFRKA GIALTPSELE KVEVADFGLG NLAVQGLQLV TYINTDRYCA
KELALFPHQT CPEHLHPPVG GDPGKMETFR CRWGKVFLYV EGEPAASVQA AVPPGSEAYY
TVFHEIVLTP GEQYTIPPGT KHWFQGGPEG AIVSEFSSTS RDEFDIFTDP KVERMPVIEF
DD