ID   DLMIS_SERPR             Reviewed;         228 AA.
AC   D5MTT1;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   13-JUL-2010, sequence version 1.
DT   03-AUG-2022, entry version 22.
DE   RecName: Full=D-lyxose/D-mannose isomerase {ECO:0000305};
DE            EC=5.3.1.15 {ECO:0000269|PubMed:20695994};
DE            EC=5.3.1.7 {ECO:0000269|PubMed:20695994};
GN   Name=lyxi {ECO:0000312|EMBL:BAJ07463.1};
OS   Serratia proteamaculans.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=28151;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC   STRAIN=KCTC 2936;
RX   PubMed=20695994; DOI=10.1111/j.1472-765x.2010.02903.x;
RA   Park C.-S., Yeom S.-J., Lim Y.-R., Kim Y.-S., Oh D.-K.;
RT   "Substrate specificity of a recombinant D-lyxose isomerase from Serratia
RT   proteamaculans that produces D-lyxose and D-mannose.";
RL   Lett. Appl. Microbiol. 51:343-350(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:20695994). Shows optimum activity using D-lyxose as substrate,
CC       but can also effectively catalyze the isomerization between D-fructose
CC       and D-mannose (PubMed:20695994). Shows lower activity with L-gulose, D-
CC       talose and L-ribose (PubMed:20695994). {ECO:0000269|PubMed:20695994}.
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:20695994};
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:20695994};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:20695994};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=13.3 mM for D-lyxose {ECO:0000269|PubMed:20695994};
CC         KM=32.2 mM for D-mannose {ECO:0000269|PubMed:20695994};
CC         KM=3.83 mM for D-xylulose {ECO:0000269|PubMed:20695994};
CC         KM=19.4 mM for D-fructose {ECO:0000269|PubMed:20695994};
CC         Note=kcat is 30810 sec(-1) with D-lyxose as substrate. kcat is 16170
CC         sec(-1) with D-mannose as substrate. kcat is 31620 sec(-1) with D-
CC         xylulose as substrate. kcat is 4297 sec(-1) with D-fructose as
CC         substrate. {ECO:0000269|PubMed:20695994};
CC       pH dependence:
CC         Optimum pH is 7.5. {ECO:0000269|PubMed:20695994};
CC       Temperature dependence:
CC         Optimum temperature is 40 degrees Celsius.
CC         {ECO:0000269|PubMed:20695994};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20695994}.
CC   -!- SIMILARITY: Belongs to the D-lyxose ketol-isomerase family.
CC       {ECO:0000305}.
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DR   EMBL; AB559947; BAJ07463.1; -; Genomic_DNA.
DR   BRENDA; 5.3.1.15; 8756.
DR   GO; GO:0047828; F:D-lyxose ketol-isomerase activity; IEA:UniProtKB-EC.
DR   Gene3D; 2.60.120.10; -; 1.
DR   InterPro; IPR010864; D-lyxose_isomer.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   Pfam; PF07385; Lyx_isomer; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Isomerase; Manganese; Metal-binding.
FT   CHAIN           1..228
FT                   /note="D-lyxose/D-mannose isomerase"
FT                   /id="PRO_0000455824"
FT   BINDING         103
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:A0A6M7H989"
FT   BINDING         105
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:A0A6M7H989"
FT   BINDING         110
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:A0A6M7H989"
FT   BINDING         171
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:A0A6M7H989"
SQ   SEQUENCE   228 AA;  25933 MW;  40E4B338E8DDD977 CRC64;
     MKPSAVNQIL QQTQHFFARF DVHLPPFAHF SPAVWQQLDR QPWQEVFDLK LGWDVTAFGD
     DDFARKGLTL FTLRNGSPGG KPYAKGYAEK IMHCREAQVT PMHFHWRKRE DIINRGGGNL
     IVELHNADTR DGLAETAVTV TLDGCRQTHA AGSRLRLAPG ESICLTPAIY HSFWGEEGFG
     DVLVGEVSTV NDDDNDNRFL QPLSRFSQIE EDQPPQWLLC HEYLRFIA