KET3E_ARTGO
ID KET3E_ARTGO Reviewed; 289 AA.
AC A0A1L7NQ96;
DT 13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 1.
DT 03-AUG-2022, entry version 15.
DE RecName: Full=Ketose 3-epimerase {ECO:0000303|PubMed:30279320};
DE EC=5.1.3.- {ECO:0000269|PubMed:27713017, ECO:0000269|PubMed:30279320};
DE AltName: Full=D-allulose 3-epimerase {ECO:0000303|PubMed:27713017};
DE Short=D-AE {ECO:0000303|PubMed:27713017};
DE AltName: Full=L-ribulose 3-epimerase {ECO:0000303|PubMed:30279320};
GN Name=DAE {ECO:0000312|EMBL:BAW27657.1};
OS Arthrobacter globiformis.
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter.
OX NCBI_TaxID=1665;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR, SUBUNIT,
RP AND BIOTECHNOLOGY.
RC STRAIN=M30;
RX PubMed=27713017; DOI=10.1016/j.jbiosc.2016.09.004;
RA Yoshihara A., Kozakai T., Shintani T., Matsutani R., Ohtani K., Iida T.,
RA Akimitsu K., Izumori K., Gullapalli P.K.;
RT "Purification and characterization of D-allulose 3-epimerase derived from
RT Arthrobacter globiformis M30, a GRAS microorganism.";
RL J. Biosci. Bioeng. 123:170-176(2017).
RN [2] {ECO:0007744|PDB:5ZFS}
RP X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) IN COMPLEX WITH MANGANESE, FUNCTION,
RP CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND COFACTOR.
RC STRAIN=M30;
RX PubMed=30279320; DOI=10.1107/s2053230x18011706;
RA Yoshida H., Yoshihara A., Gullapalli P.K., Ohtani K., Akimitsu K.,
RA Izumori K., Kamitori S.;
RT "X-ray structure of Arthrobacter globiformis M30 ketose 3-epimerase for the
RT production of D-allulose from D-fructose.";
RL Acta Crystallogr. F Struct. Biol. Commun. 74:669-676(2018).
CC -!- FUNCTION: Catalyzes the reversible C-3 epimerization of several
CC ketoses. Shows the highest enzymatic activity for the epimerization of
CC L-ribulose to L-xylulose. Is also able to convert D-allulose (also
CC known as D-psicose) to D-fructose and, to a lesser extent, L-tagatose
CC to L-sorbose, D-ribulose to D-xylulose, L-allulose to L-fructose and D-
CC tagatose to D-sorbose. {ECO:0000269|PubMed:27713017,
CC ECO:0000269|PubMed:30279320}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-ribulose = L-xylulose; Xref=Rhea:RHEA:53268,
CC ChEBI:CHEBI:16880, ChEBI:CHEBI:17399;
CC Evidence={ECO:0000269|PubMed:30279320};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-allulose = keto-D-fructose; Xref=Rhea:RHEA:42360,
CC ChEBI:CHEBI:27605, ChEBI:CHEBI:48095;
CC Evidence={ECO:0000269|PubMed:27713017, ECO:0000269|PubMed:30279320};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=keto-L-tagatose = keto-L-sorbose; Xref=Rhea:RHEA:61780,
CC ChEBI:CHEBI:13172, ChEBI:CHEBI:134275;
CC Evidence={ECO:0000269|PubMed:27713017};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-ribulose = D-xylulose; Xref=Rhea:RHEA:51544,
CC ChEBI:CHEBI:17140, ChEBI:CHEBI:17173;
CC Evidence={ECO:0000269|PubMed:30279320};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-allulose = keto-L-fructose; Xref=Rhea:RHEA:61784,
CC ChEBI:CHEBI:37724, ChEBI:CHEBI:145026;
CC Evidence={ECO:0000269|PubMed:27713017};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=keto-D-tagatose = keto-D-sorbose; Xref=Rhea:RHEA:43048,
CC ChEBI:CHEBI:13022, ChEBI:CHEBI:47693;
CC Evidence={ECO:0000269|PubMed:27713017};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:27713017};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:27713017, ECO:0000269|PubMed:30279320};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:27713017};
CC Note=Binds 1 divalent metal cation per subunit. Seems able to use
CC Mg(2+), Mn(2+) or Co(2+). {ECO:0000269|PubMed:27713017,
CC ECO:0000269|PubMed:30279320};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=31.0 mM for D-allulose {ECO:0000269|PubMed:27713017};
CC KM=37.5 mM for D-fructose {ECO:0000269|PubMed:27713017};
CC Vmax=177 umol/min/mg enzyme for the epimerization of D-allulose
CC {ECO:0000269|PubMed:27713017};
CC Vmax=78.4 umol/min/mg enzyme for the epimerization of D-fructose
CC {ECO:0000269|PubMed:27713017};
CC Note=kcat is 5664 min(-1) for the epimerization of D-allulose. kcat
CC is 2509 min(-1) for the epimerization of D-fructose.
CC {ECO:0000269|PubMed:27713017};
CC pH dependence:
CC Optimum pH is 7.5-8.0. Is stable from pH 6.0-11.0.
CC {ECO:0000269|PubMed:27713017};
CC Temperature dependence:
CC Optimum temperature is 70 degrees Celsius. Is highly stable at 55
CC degrees Celsius. {ECO:0000269|PubMed:27713017};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:27713017}.
CC -!- BIOTECHNOLOGY: This enzyme is an ideal candidate for the industrial
CC production of D-allulose, which has the potential to be used not only
CC as a food ingredient but also as a growth regulator and/or agricultural
CC chemical. {ECO:0000269|PubMed:27713017}.
CC -!- SIMILARITY: Belongs to the hyi family. {ECO:0000305}.
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DR EMBL; AB981957; BAW27657.1; -; Genomic_DNA.
DR PDB; 5ZFS; X-ray; 1.96 A; A/B=1-289.
DR PDBsum; 5ZFS; -.
DR AlphaFoldDB; A0A1L7NQ96; -.
DR SMR; A0A1L7NQ96; -.
DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR GO; GO:0016857; F:racemase and epimerase activity, acting on carbohydrates and derivatives; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IDA:UniProtKB.
DR InterPro; IPR036237; Xyl_isomerase-like_sf.
DR InterPro; IPR013022; Xyl_isomerase-like_TIM-brl.
DR Pfam; PF01261; AP_endonuc_2; 1.
DR SUPFAM; SSF51658; SSF51658; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cobalt; Isomerase; Magnesium;
KW Manganese; Metal-binding.
FT CHAIN 1..289
FT /note="Ketose 3-epimerase"
FT /id="PRO_0000448614"
FT ACT_SITE 146
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9WYP7"
FT ACT_SITE 240
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9WYP7"
FT BINDING 146
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:30279320"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O50580"
FT BINDING 179..182
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O50580"
FT BINDING 179
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:30279320"
FT BINDING 205
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:30279320"
FT BINDING 211
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O50580"
FT BINDING 240
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:30279320"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:5ZFS"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:5ZFS"
FT HELIX 16..29
FT /evidence="ECO:0007829|PDB:5ZFS"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:5ZFS"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:5ZFS"
FT HELIX 46..56
FT /evidence="ECO:0007829|PDB:5ZFS"
FT STRAND 59..66
FT /evidence="ECO:0007829|PDB:5ZFS"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:5ZFS"
FT HELIX 77..97
FT /evidence="ECO:0007829|PDB:5ZFS"
FT STRAND 101..111
FT /evidence="ECO:0007829|PDB:5ZFS"
FT HELIX 119..137
FT /evidence="ECO:0007829|PDB:5ZFS"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:5ZFS"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:5ZFS"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:5ZFS"
FT HELIX 159..169
FT /evidence="ECO:0007829|PDB:5ZFS"
FT STRAND 174..179
FT /evidence="ECO:0007829|PDB:5ZFS"
FT HELIX 180..186
FT /evidence="ECO:0007829|PDB:5ZFS"
FT HELIX 192..197
FT /evidence="ECO:0007829|PDB:5ZFS"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:5ZFS"
FT STRAND 201..206
FT /evidence="ECO:0007829|PDB:5ZFS"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:5ZFS"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:5ZFS"
FT HELIX 221..231
FT /evidence="ECO:0007829|PDB:5ZFS"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:5ZFS"
FT HELIX 251..254
FT /evidence="ECO:0007829|PDB:5ZFS"
FT HELIX 265..289
FT /evidence="ECO:0007829|PDB:5ZFS"
SQ SEQUENCE 289 AA; 31406 MW; 74B66F657813AF05 CRC64;
MKIGCHGLVW TGHFDAEGIR YSVQKTREAG FDLVEFPLMD PFSFDVQTAK SALAEHGLAA
SASLGLSDAT DVSSEDPAVV KAGEELLNRA VDVLAELGAT DFCGVIYSAM KKYMEPATAA
GLANSKAAVG RVADRASDLG INVSLEVVNR YETNVLNTGR QALAYLEELN RPNLGIHLDT
YHMNIEESDM FSPILDTAEA LRYVHIGESH RGYLGTGSVD FDTFFKALGR IGYDGPVVFE
SFSSSVVAPD LSRMLGIWRN LWADNEELGA HANAFIRDKL TAIKTIELH
