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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
 
 
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