DLYKI_THEX4
ID DLYKI_THEX4 Reviewed; 180 AA.
AC A0A256XLS3;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2017, sequence version 1.
DT 03-AUG-2022, entry version 10.
DE RecName: Full=D-lyxose ketol-isomerase {ECO:0000305};
DE EC=5.3.1.15 {ECO:0000269|PubMed:34422783};
DE AltName: Full=D-lyxose isomerase {ECO:0000303|PubMed:34422783};
GN ORFNames=B6U94_07925 {ECO:0000312|EMBL:OYT29093.1};
OS Thermofilum sp. (strain ex4484_79).
OC Archaea; Crenarchaeota; Thermoprotei; Thermofilales; Thermofilaceae;
OC Thermofilum; unclassified Thermofilum.
OX NCBI_TaxID=2012527;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ex4484_79;
RX PubMed=28835260; DOI=10.1186/s40168-017-0322-2;
RA Dombrowski N., Seitz K.W., Teske A.P., Baker B.J.;
RT "Genomic insights into potential interdependencies in microbial hydrocarbon
RT and nutrient cycling in hydrothermal sediments.";
RL Microbiome 5:106-106(2017).
RN [2] {ECO:0007744|PDB:7NZO, ECO:0007744|PDB:7NZP, ECO:0007744|PDB:7NZQ}
RP X-RAY CRYSTALLOGRAPHY (1.34 ANGSTROMS) IN COMPLEXES WITH MANGANESE;
RP D-FRUCTOSE AND D-MANNOSE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, BIOTECHNOLOGY, AND DISULFIDE BOND.
RC STRAIN=ex4484_79;
RX PubMed=34422783; DOI=10.3389/fbioe.2021.711487;
RA De Rose S.A., Kuprat T., Isupov M.N., Reinhardt A., Schonheit P.,
RA Littlechild J.A.;
RT "Biochemical and structural characterisation of a novel D-lyxose isomerase
RT from the hyperthermophilic archaeon Thermofilum sp.";
RL Front. Bioeng. Biotechnol. 9:711487-711487(2021).
CC -!- FUNCTION: Sugar isomerase that catalyzes the reversible isomerization
CC of D-lyxose to D-xylulose (PubMed:34422783). Is highly specific for the
CC substrate D-lyxose, showing less than 2% activity towards mannose and
CC other substrates reported for lyxose isomerases (PubMed:34422783).
CC {ECO:0000269|PubMed:34422783}.
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:34422783};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:34422783};
CC Note=Shows highest activity with Mn(2+). The Mn(2+) ions can be
CC effectively replaced by Co(2+) ions. Shows less activity with other
CC divalent metal ions such as Fe(2+), Ca(2+) and Mg(2+).
CC {ECO:0000269|PubMed:34422783};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=74 mM for D-lyxose {ECO:0000269|PubMed:34422783};
CC KM=0.4 mM for Mn(2+) {ECO:0000269|PubMed:34422783};
CC Vmax=338 umol/min/mg enzyme {ECO:0000269|PubMed:34422783};
CC Temperature dependence:
CC Optimum temperature is higher than 95 degrees Celsius. Retains 60% of
CC its activity after 60 min incubation at 80 degrees Celsius.
CC {ECO:0000269|PubMed:34422783};
CC -!- SUBUNIT: Homodimer; disulfide-linked (PubMed:34422783). Stabilized by a
CC disulfide bond between the two monomers of the dimeric enzyme and
CC increased hydrophobicity at the dimer interface (PubMed:34422783).
CC {ECO:0000269|PubMed:34422783}.
CC -!- BIOTECHNOLOGY: High substrate specificity, thermostability and solvent
CC tolerance make this lyxose isomerase enzyme a good candidate for
CC potential industrial applications. {ECO:0000269|PubMed:34422783}.
CC -!- SIMILARITY: Belongs to the D-lyxose ketol-isomerase family.
CC {ECO:0000305}.
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DR EMBL; NJDK01000115; OYT29093.1; -; Genomic_DNA.
DR PDB; 7NZO; X-ray; 1.67 A; AAA/BBB=1-180.
DR PDB; 7NZP; X-ray; 1.34 A; AAA/BBB=1-180.
DR PDB; 7NZQ; X-ray; 1.57 A; AAA=1-180.
DR PDBsum; 7NZO; -.
DR PDBsum; 7NZP; -.
DR PDBsum; 7NZQ; -.
DR SMR; A0A256XLS3; -.
DR EnsemblBacteria; OYT29093; OYT29093; B6U94_07925.
DR Proteomes; UP000216408; Unassembled WGS sequence.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
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..180
FT /note="D-lyxose ketol-isomerase"
FT /id="PRO_0000455822"
FT BINDING 62
FT /ligand="D-fructose"
FT /ligand_id="ChEBI:CHEBI:37721"
FT /evidence="ECO:0000269|PubMed:34422783,
FT ECO:0007744|PDB:7NZP"
FT BINDING 75
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:34422783,
FT ECO:0007744|PDB:7NZO, ECO:0007744|PDB:7NZP,
FT ECO:0007744|PDB:7NZQ"
FT BINDING 77
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:34422783,
FT ECO:0007744|PDB:7NZO, ECO:0007744|PDB:7NZP,
FT ECO:0007744|PDB:7NZQ"
FT BINDING 86
FT /ligand="D-fructose"
FT /ligand_id="ChEBI:CHEBI:37721"
FT /evidence="ECO:0000269|PubMed:34422783,
FT ECO:0007744|PDB:7NZP"
FT BINDING 88
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:34422783,
FT ECO:0007744|PDB:7NZO, ECO:0007744|PDB:7NZP,
FT ECO:0007744|PDB:7NZQ"
FT BINDING 143
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:34422783,
FT ECO:0007744|PDB:7NZO, ECO:0007744|PDB:7NZP,
FT ECO:0007744|PDB:7NZQ"
FT BINDING 156
FT /ligand="D-fructose"
FT /ligand_id="ChEBI:CHEBI:37721"
FT /evidence="ECO:0000269|PubMed:34422783,
FT ECO:0007744|PDB:7NZP"
FT BINDING 166
FT /ligand="D-fructose"
FT /ligand_id="ChEBI:CHEBI:37721"
FT /evidence="ECO:0000269|PubMed:34422783,
FT ECO:0007744|PDB:7NZP"
FT BINDING 175
FT /ligand="D-fructose"
FT /ligand_id="ChEBI:CHEBI:37721"
FT /evidence="ECO:0000269|PubMed:34422783,
FT ECO:0007744|PDB:7NZP"
FT DISULFID 22
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:34422783,
FT ECO:0007744|PDB:7NZO, ECO:0007744|PDB:7NZP"
SQ SEQUENCE 180 AA; 20959 MW; D2CA3B3DFDA19C95 CRC64;
MLTKELVKEA REKAIRMLEK ACIAITDEEK EKIEVTDFGL GVLYTFGLEI LVYVNNERYC
AKELVMFPRQ ICPEHRHPPI GSYLGKQETF RCRWGEVYLY VPGTPTPNPR ARIPEEKKRY
FTVWHEIVLR PGEQYTIPPN TLHWFQAGDE GAIVSEFSSQ SIDEKDIFTD PNVKRIPEIV
