LR3E_RHILO
ID LR3E_RHILO Reviewed; 297 AA.
AC Q98FW0;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=L-ribulose 3-epimerase {ECO:0000303|PubMed:23470755};
DE Short=L-RE {ECO:0000303|PubMed:23470755};
DE AltName: Full=D-tagatose 3-epimerase {ECO:0000303|PubMed:23470755};
DE Short=DTE {ECO:0000303|PubMed:23470755};
DE EC=5.1.3.31 {ECO:0000269|PubMed:23470755};
DE AltName: Full=Ketose 3-epimerase {ECO:0000303|PubMed:23470755};
GN OrderedLocusNames=mll3595;
OS Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS (Mesorhizobium loti (strain MAFF 303099)).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=266835;
RN [1]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, COFACTOR, SUBSTRATE SPECIFICITY, AND SUBUNIT.
RC STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX PubMed=23470755; DOI=10.1271/bbb.120745;
RA Uechi K., Takata G., Fukai Y., Yoshihara A., Morimoto K.;
RT "Gene cloning and characterization of L-ribulose 3-epimerase from
RT Mesorhizobium loti and its application to rare sugar production.";
RL Biosci. Biotechnol. Biochem. 77:511-515(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT Mesorhizobium loti.";
RL DNA Res. 7:331-338(2000).
CC -!- FUNCTION: Catalyzes the epimerization of various ketoses at the C(3)
CC position. It is able to interconvert L-ribulose with high efficiency.
CC The enzyme can also accept other ketopentoses such as D-psicose and D-
CC tagatose with lower efficiency. {ECO:0000269|PubMed:23470755}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-ribulose = L-xylulose; Xref=Rhea:RHEA:53268,
CC ChEBI:CHEBI:16880, ChEBI:CHEBI:17399; EC=5.1.3.31;
CC Evidence={ECO:0000269|PubMed:23470755};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=keto-D-tagatose = keto-D-sorbose; Xref=Rhea:RHEA:43048,
CC ChEBI:CHEBI:13022, ChEBI:CHEBI:47693; EC=5.1.3.31;
CC Evidence={ECO:0000269|PubMed:23470755};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-allulose = keto-D-fructose; Xref=Rhea:RHEA:42360,
CC ChEBI:CHEBI:27605, ChEBI:CHEBI:48095; EC=5.1.3.31;
CC Evidence={ECO:0000269|PubMed:23470755};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:23470755};
CC Note=It can also use Fe(2+). {ECO:0000269|PubMed:23470755};
CC -!- ACTIVITY REGULATION: Strongly inhibited by Co(2+) and Ni(2+), and
CC slightly inhibited by EDTA. {ECO:0000269|PubMed:23470755}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=58 mM for D-psicose {ECO:0000269|PubMed:23470755};
CC KM=140 mM for D-tagatose {ECO:0000269|PubMed:23470755};
CC KM=230 mM for L-xylulose {ECO:0000269|PubMed:23470755};
CC KM=291 mM for L-ribulose {ECO:0000269|PubMed:23470755};
CC Vmax=416 umol/min/mg enzyme with L-ribulose as substrate
CC {ECO:0000269|PubMed:23470755};
CC Vmax=290 umol/min/mg enzyme with L-xylulose as substrate
CC {ECO:0000269|PubMed:23470755};
CC Vmax=50 umol/min/mg enzyme with D-tagatose as substrate
CC {ECO:0000269|PubMed:23470755};
CC Vmax=10 umol/min/mg enzyme with D-psicose as substrate
CC {ECO:0000269|PubMed:23470755};
CC Note=kcat is 0.34 min(-1) for epimerase activity with D-psicose as
CC substrate. kcat is 3.4 min(-1) for epimerase activity with D-tagatose
CC as substrate. kcat is 8.5 min(-1) for epimerase activity with L-
CC xylulose as substrate. kcat is 13 min(-1) for epimerase activity with
CC L-ribulose as substrate. {ECO:0000269|PubMed:23470755};
CC pH dependence:
CC Optimum pH is 8. The enzyme is stable between 7 and 10.
CC {ECO:0000269|PubMed:23470755};
CC Temperature dependence:
CC Optimum temperature is around 60 degrees Celsius. The enzyme is
CC stable below 60 degrees Celsius. {ECO:0000269|PubMed:23470755};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:23470755}.
CC -!- SIMILARITY: Belongs to the hyi family. {ECO:0000305}.
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DR EMBL; BA000012; BAB50456.1; -; Genomic_DNA.
DR RefSeq; WP_010911802.1; NC_002678.2.
DR AlphaFoldDB; Q98FW0; -.
DR SMR; Q98FW0; -.
DR STRING; 266835.14023851; -.
DR EnsemblBacteria; BAB50456; BAB50456; BAB50456.
DR KEGG; mlo:mll3595; -.
DR PATRIC; fig|266835.9.peg.2866; -.
DR eggNOG; COG1082; Bacteria.
DR HOGENOM; CLU_050006_8_2_5; -.
DR OMA; NMALAKH; -.
DR OrthoDB; 1007505at2; -.
DR Proteomes; UP000000552; Chromosome.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 Isomerase; Manganese; Metal-binding.
FT CHAIN 1..297
FT /note="L-ribulose 3-epimerase"
FT /id="PRO_0000435307"
FT ACT_SITE 147
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9WYP7"
FT ACT_SITE 241
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9WYP7"
FT BINDING 147
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:O50580"
FT BINDING 153
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O50580"
FT BINDING 180..183
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O50580"
FT BINDING 180
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:O50580"
FT BINDING 206
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:O50580"
FT BINDING 212
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O50580"
FT BINDING 241
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:O50580"
SQ SEQUENCE 297 AA; 31623 MW; 5D9E97AECC274DF8 CRC64;
MARIGIHSFV WSASSAQSEL ERTLANTREA GFDLIEFSYL DPADVDIGGL AKRIADLGLG
VAISIGLPGD GDISSADKAV AARGVEILNE TVALTRDLGG RKVAGILSAG HGLQLEAPTR
DQWSRSTAAL AKVAETAKAA GVTLNLEIVN RFESNLLNTA AQGLAFIEDT GSDNIFLHLD
TFHMNIEEAD VGLAIRHAAG KIGYVHIGES HRGFLGTGNI DFAAIFDALT AVGYADDLSF
ESFSSEIVDE NLSKKTAIWR NLWADNMALA KHARAFIGLG LETARRKAEL VSARHKP
