DPES_RUMCH
ID DPES_RUMCH Reviewed; 293 AA.
AC B8I944;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=D-psicose 3-epimerase {ECO:0000303|PubMed:21663329};
DE Short=DPEase {ECO:0000303|PubMed:21663329};
DE EC=5.1.3.30 {ECO:0000269|PubMed:21663329};
GN OrderedLocusNames=Ccel_0941;
OS Ruminiclostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 /
OS H10) (Clostridium cellulolyticum).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminiclostridium.
OX NCBI_TaxID=394503;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35319 / DSM 5812 / JCM 6584 / H10;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Saunders E., Brettin T.,
RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Zhou J., Richardson P.;
RT "Complete sequence of Clostridium cellulolyticum H10.";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP SPECIFICITY, COFACTOR, AND SUBUNIT.
RC STRAIN=ATCC 35319 / DSM 5812 / JCM 6584 / H10;
RX PubMed=21663329; DOI=10.1021/jf201356q;
RA Mu W., Chu F., Xing Q., Yu S., Zhou L., Jiang B.;
RT "Cloning, expression, and characterization of a D-psicose 3-epimerase from
RT Clostridium cellulolyticum H10.";
RL J. Agric. Food Chem. 59:7785-7792(2011).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) IN COMPLEX WITH SUBSTRATE; SUBSTRATE
RP ANALOGS AND MANGANESE ION, COFACTOR, AND SUBUNIT.
RC STRAIN=ATCC 35319 / DSM 5812 / JCM 6584 / H10;
RX PubMed=22426981; DOI=10.1007/s13238-012-2026-5;
RA Chan H.C., Zhu Y., Hu Y., Ko T.P., Huang C.H., Ren F., Chen C.C., Ma Y.,
RA Guo R.T., Sun Y.;
RT "Crystal structures of D-psicose 3-epimerase from Clostridium
RT cellulolyticum H10 and its complex with ketohexose sugars.";
RL Protein Cell 3:123-131(2012).
CC -!- FUNCTION: Involved in the biosynthesis of D-psicose. Catalyzes the
CC reversible epimerization of D-fructose at the C3 position to yield D-
CC psicose. The enzyme is highly specific for D-psicose and shows very low
CC activity with D-tagatose. {ECO:0000269|PubMed:21663329}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-allulose = keto-D-fructose; Xref=Rhea:RHEA:42360,
CC ChEBI:CHEBI:27605, ChEBI:CHEBI:48095; EC=5.1.3.30;
CC Evidence={ECO:0000269|PubMed:21663329};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:21663329, ECO:0000269|PubMed:22426981};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:21663329};
CC Note=Binds 1 Mn(2+) or Co(2+) ion per subunit. Can also use Mg(2+),
CC Fe(2+) and Ni(2+) ions to a lesser extent.
CC {ECO:0000269|PubMed:21663329, ECO:0000269|PubMed:22426981};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=17.4 mM for D-psicose (at pH 8 and 55 degrees Celsius)
CC {ECO:0000269|PubMed:21663329};
CC KM=244 mM for D-tagatose (at pH 8 and 55 degrees Celsius)
CC {ECO:0000269|PubMed:21663329};
CC Note=kcat is 3243.4 min(-1) for epimerase activity with D-psicose as
CC substrate (at pH 8 and 55 degrees Celsius). kcat is 184.8 min(-1) for
CC epimerase activity with D-tagatose as substrate (at pH 8 and 55
CC degrees Celsius). {ECO:0000269|PubMed:21663329};
CC pH dependence:
CC Optimum pH is 8. {ECO:0000269|PubMed:21663329};
CC Temperature dependence:
CC Optimum temperature is 55 degrees Celsius.
CC {ECO:0000269|PubMed:21663329};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:21663329,
CC ECO:0000269|PubMed:22426981}.
CC -!- SIMILARITY: Belongs to the hyi family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001348; ACL75304.1; -; Genomic_DNA.
DR RefSeq; WP_015924461.1; NC_011898.1.
DR PDB; 3VNI; X-ray; 1.98 A; A/B/C/D=1-293.
DR PDB; 3VNJ; X-ray; 2.08 A; A/B/C/D=1-293.
DR PDB; 3VNK; X-ray; 2.02 A; A/B/C/D=1-293.
DR PDB; 3VNL; X-ray; 2.15 A; A/B/C/D=1-293.
DR PDB; 3VNM; X-ray; 2.12 A; A/B/C/D=1-293.
DR PDB; 7E9W; X-ray; 2.10 A; A/B/C/D=1-293.
DR PDBsum; 3VNI; -.
DR PDBsum; 3VNJ; -.
DR PDBsum; 3VNK; -.
DR PDBsum; 3VNL; -.
DR PDBsum; 3VNM; -.
DR PDBsum; 7E9W; -.
DR AlphaFoldDB; B8I944; -.
DR SMR; B8I944; -.
DR STRING; 394503.Ccel_0941; -.
DR EnsemblBacteria; ACL75304; ACL75304; Ccel_0941.
DR KEGG; cce:Ccel_0941; -.
DR eggNOG; COG1082; Bacteria.
DR HOGENOM; CLU_050006_8_2_9; -.
DR OMA; GLAMESF; -.
DR OrthoDB; 1007505at2; -.
DR BRENDA; 5.1.3.30; 1468.
DR Proteomes; UP000001349; Chromosome.
DR GO; GO:0050897; F:cobalt ion binding; IDA:UniProtKB.
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 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; Cobalt; Isomerase; Manganese; Metal-binding;
KW Reference proteome.
FT CHAIN 1..293
FT /note="D-psicose 3-epimerase"
FT /id="PRO_0000435452"
FT ACT_SITE 150
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9WYP7"
FT ACT_SITE 244
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9WYP7"
FT BINDING 6
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22426981"
FT BINDING 107
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A9CH28"
FT BINDING 150
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:22426981"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22426981"
FT BINDING 183..186
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22426981"
FT BINDING 183
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:22426981"
FT BINDING 209
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:22426981"
FT BINDING 215
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22426981"
FT BINDING 244
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:22426981"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:3VNI"
FT HELIX 7..10
FT /evidence="ECO:0007829|PDB:3VNI"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:3VNI"
FT HELIX 18..28
FT /evidence="ECO:0007829|PDB:3VNI"
FT STRAND 31..37
FT /evidence="ECO:0007829|PDB:3VNI"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:3VNI"
FT HELIX 45..57
FT /evidence="ECO:0007829|PDB:3VNI"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:3VNI"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:3VNI"
FT HELIX 79..99
FT /evidence="ECO:0007829|PDB:3VNI"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:3VNI"
FT HELIX 122..142
FT /evidence="ECO:0007829|PDB:3VNI"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:3VNI"
FT TURN 154..156
FT /evidence="ECO:0007829|PDB:3VNI"
FT HELIX 163..173
FT /evidence="ECO:0007829|PDB:3VNI"
FT STRAND 178..183
FT /evidence="ECO:0007829|PDB:3VNI"
FT HELIX 184..190
FT /evidence="ECO:0007829|PDB:3VNI"
FT HELIX 194..201
FT /evidence="ECO:0007829|PDB:3VNI"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:3VNI"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:3VNI"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:3VNI"
FT HELIX 225..234
FT /evidence="ECO:0007829|PDB:3VNI"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:3VNI"
FT HELIX 251..257
FT /evidence="ECO:0007829|PDB:3VNI"
FT TURN 263..266
FT /evidence="ECO:0007829|PDB:3VNK"
FT HELIX 269..287
FT /evidence="ECO:0007829|PDB:3VNI"
SQ SEQUENCE 293 AA; 33034 MW; AC42BF378C03B426 CRC64;
MKHGIYYAYW EQEWEADYKY YIEKVAKLGF DILEIAASPL PFYSDIQINE LKACAHGNGI
TLTVGHGPSA EQNLSSPDPD IRKNAKAFYT DLLKRLYKLD VHLIGGALYS YWPIDYTKTI
DKKGDWERSV ESVREVAKVA EACGVDFCLE VLNRFENYLI NTAQEGVDFV KQVDHNNVKV
MLDTFHMNIE EDSIGGAIRT AGSYLGHLHT GECNRKVPGR GRIPWVEIGE ALADIGYNGS
VVMEPFVRMG GTVGSNIKVW RDISNGADEK MLDREAQAAL DFSRYVLECH KHS
