DLMIS_THEOJ
ID DLMIS_THEOJ Reviewed; 181 AA.
AC D9RZ53;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=D-lyxose/D-mannose isomerase {ECO:0000305};
DE EC=5.3.1.15 {ECO:0000269|Ref.2};
DE EC=5.3.1.7 {ECO:0000269|Ref.2};
GN OrderedLocusNames=Toce_1877 {ECO:0000312|EMBL:ADL08607.1};
OS Thermosediminibacter oceani (strain ATCC BAA-1034 / DSM 16646 /
OS JW/IW-1228P).
OC Bacteria; Firmicutes; Clostridia; Thermosediminibacterales;
OC Thermosediminibacteraceae; Thermosediminibacter.
OX NCBI_TaxID=555079;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1034 / DSM 16646 / JW/IW-1228P;
RX PubMed=21304740; DOI=10.4056/sigs.1133078;
RA Pitluck S., Yasawong M., Munk C., Nolan M., Lapidus A., Lucas S.,
RA Glavina Del Rio T., Tice H., Cheng J.F., Bruce D., Detter C., Tapia R.,
RA Han C., Goodwin L., Liolios K., Ivanova N., Mavromatis K., Mikhailova N.,
RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Rohde M., Spring S., Sikorski J., Goker M., Woyke T.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA Klenk H.P.;
RT "Complete genome sequence of Thermosediminibacter oceani type strain
RT (JW/IW-1228P).";
RL Stand. Genomic Sci. 3:108-116(2010).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBUNIT.
RC STRAIN=ATCC BAA-1034 / DSM 16646 / JW/IW-1228P;
RX DOI=10.1016/j.procbio.2016.08.023;
RA Yu L., Zhang W., Zhang T., Jiang B., Mu W.;
RT "Efficient biotransformation of D-fructose to D-mannose by a thermostable
RT D-lyxose isomerase from Thermosediminibacter oceani.";
RL Process Biochem. 51:2026-2033(2016).
CC -!- FUNCTION: Sugar isomerase that catalyzes the reversible isomerization
CC of D-lyxose to D-xylulose, and D-mannose to D-fructose (Ref.2). Shows
CC optimum activity using D-lyxose as substrate, but can also effectively
CC catalyze the isomerization between D-fructose and D-mannose (Ref.2).
CC {ECO:0000269|Ref.2}.
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|Ref.2};
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|Ref.2};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|Ref.2};
CC Note=Can also use Ni(2+), Co(2+) or Fe(2+), with lower efficiency.
CC {ECO:0000269|Ref.2};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=15.5 mM for D-lyxose {ECO:0000269|Ref.2};
CC KM=32.8 mM for D-mannose {ECO:0000269|Ref.2};
CC KM=27.3 mM for D-fructose {ECO:0000269|Ref.2};
CC Note=kcat is 3108 min(-1) with D-lyxose as substrate. kcat is 5686
CC min(-1) with D-mannose as substrate. kcat is 1030 min(-1) with D-
CC fructose as substrate. {ECO:0000269|Ref.2};
CC pH dependence:
CC Optimum pH is 6.5. Retains more than 50% of maximal activity from pH
CC 5.0 to 8.0. {ECO:0000269|Ref.2};
CC Temperature dependence:
CC Optimum temperature is 65 degrees Celsius. Highly thermostable at 80
CC degrees Celsius. {ECO:0000269|Ref.2};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the D-lyxose ketol-isomerase family.
CC {ECO:0000305}.
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DR EMBL; CP002131; ADL08607.1; -; Genomic_DNA.
DR RefSeq; WP_013276628.1; NC_014377.1.
DR STRING; 555079.Toce_1877; -.
DR EnsemblBacteria; ADL08607; ADL08607; Toce_1877.
DR KEGG; toc:Toce_1877; -.
DR eggNOG; COG3822; Bacteria.
DR HOGENOM; CLU_1553334_0_0_9; -.
DR OMA; TFRCRWG; -.
DR OrthoDB; 1475761at2; -.
DR BRENDA; 5.3.1.15; 16127.
DR BRENDA; 5.3.1.7; 16127.
DR Proteomes; UP000000272; Chromosome.
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 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; Isomerase; Manganese; Metal-binding;
KW Reference proteome.
FT CHAIN 1..181
FT /note="D-lyxose/D-mannose isomerase"
FT /id="PRO_0000455825"
FT BINDING 75
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:A0A256XLS3"
FT BINDING 77
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:A0A256XLS3"
FT BINDING 88
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:A0A256XLS3"
FT BINDING 143
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:A0A256XLS3"
SQ SEQUENCE 181 AA; 20841 MW; 5225D39E15930CA2 CRC64;
MLKKSKVKEI QEKVYEALKK ANIAITPEEK ENIEVADFGL GDLENTGLQL LVYVNTDRYC
AKELVLFPGQ TCPEHRHPPV NGKPGKQETF RCRYGKVYLY VEGEKTENPH CRPPKGSEQY
YTVWHEIELN PGEQYTIEPN TLHWFQAGEE GAIVSEFSSH SDDESDIFTD PRIKRIPEIE
D
