ID A0A0R1K109_9LACO Unreviewed; 217 AA.
AC A0A0R1K109;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Ribulose-phosphate 3-epimerase {ECO:0000256|ARBA:ARBA00013188, ECO:0000256|HAMAP-Rule:MF_02227};
DE EC=5.1.3.1 {ECO:0000256|ARBA:ARBA00013188, ECO:0000256|HAMAP-Rule:MF_02227};
GN Name=rpe {ECO:0000256|HAMAP-Rule:MF_02227};
GN ORFNames=FD30_GL000528 {ECO:0000313|EMBL:KRK77167.1};
OS Levilactobacillus namurensis DSM 19117.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Levilactobacillus.
OX NCBI_TaxID=1423773 {ECO:0000313|EMBL:KRK77167.1, ECO:0000313|Proteomes:UP000051162};
RN [1] {ECO:0000313|EMBL:KRK77167.1, ECO:0000313|Proteomes:UP000051162}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19117 {ECO:0000313|EMBL:KRK77167.1,
RC ECO:0000313|Proteomes:UP000051162};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
CC -!- FUNCTION: Catalyzes the reversible epimerization of D-ribulose 5-
CC phosphate to D-xylulose 5-phosphate. {ECO:0000256|HAMAP-Rule:MF_02227}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-ribulose 5-phosphate = D-xylulose 5-phosphate;
CC Xref=Rhea:RHEA:13677, ChEBI:CHEBI:57737, ChEBI:CHEBI:58121;
CC EC=5.1.3.1; Evidence={ECO:0000256|ARBA:ARBA00001782,
CC ECO:0000256|HAMAP-Rule:MF_02227, ECO:0000256|PIRNR:PIRNR001461};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|ARBA:ARBA00001941};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02227,
CC ECO:0000256|PIRSR:PIRSR001461-2};
CC Note=Binds 1 divalent metal cation per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_02227, ECO:0000256|PIRSR:PIRSR001461-2};
CC -!- PATHWAY: Carbohydrate degradation. {ECO:0000256|HAMAP-Rule:MF_02227}.
CC -!- SIMILARITY: Belongs to the ribulose-phosphate 3-epimerase family.
CC {ECO:0000256|ARBA:ARBA00009541, ECO:0000256|HAMAP-Rule:MF_02227,
CC ECO:0000256|PIRNR:PIRNR001461}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRK77167.1}.
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DR EMBL; AZDT01000010; KRK77167.1; -; Genomic_DNA.
DR RefSeq; WP_024746461.1; NZ_AZDT01000010.1.
DR AlphaFoldDB; A0A0R1K109; -.
DR STRING; 1423773.FD30_GL000528; -.
DR GeneID; 84781652; -.
DR PATRIC; fig|1423773.3.peg.540; -.
DR OrthoDB; 1645589at2; -.
DR Proteomes; UP000051162; Unassembled WGS sequence.
DR GO; GO:0004750; F:D-ribulose-phosphate 3-epimerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019323; P:pentose catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:InterPro.
DR CDD; cd00429; RPE; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR HAMAP; MF_02227; RPE; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR026019; Ribul_P_3_epim.
DR InterPro; IPR000056; Ribul_P_3_epim-like.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR NCBIfam; TIGR01163; rpe; 1.
DR PANTHER; PTHR11749; RIBULOSE-5-PHOSPHATE-3-EPIMERASE; 1.
DR PANTHER; PTHR11749:SF3; RIBULOSE-PHOSPHATE 3-EPIMERASE; 1.
DR Pfam; PF00834; Ribul_P_3_epim; 1.
DR PIRSF; PIRSF001461; RPE; 1.
DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
DR PROSITE; PS01086; RIBUL_P_3_EPIMER_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_02227,
KW ECO:0000256|PIRNR:PIRNR001461}; Cobalt {ECO:0000256|PIRSR:PIRSR001461-2};
KW Isomerase {ECO:0000256|HAMAP-Rule:MF_02227, ECO:0000256|PIRNR:PIRNR001461};
KW Manganese {ECO:0000256|PIRSR:PIRSR001461-2};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_02227,
KW ECO:0000256|PIRSR:PIRSR001461-2}; Zinc {ECO:0000256|PIRSR:PIRSR001461-2}.
FT ACT_SITE 34
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02227,
FT ECO:0000256|PIRSR:PIRSR001461-1"
FT ACT_SITE 174
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02227,
FT ECO:0000256|PIRSR:PIRSR001461-1"
FT BINDING 7
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02227,
FT ECO:0000256|PIRSR:PIRSR001461-3"
FT BINDING 32
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02227,
FT ECO:0000256|PIRSR:PIRSR001461-2"
FT BINDING 34
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02227,
FT ECO:0000256|PIRSR:PIRSR001461-2"
FT BINDING 65
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02227,
FT ECO:0000256|PIRSR:PIRSR001461-2"
FT BINDING 65
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02227,
FT ECO:0000256|PIRSR:PIRSR001461-3"
FT BINDING 141..144
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02227,
FT ECO:0000256|PIRSR:PIRSR001461-3"
FT BINDING 174..176
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02227"
FT BINDING 174
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02227,
FT ECO:0000256|PIRSR:PIRSR001461-2"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001461-3"
FT BINDING 196..197
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02227,
FT ECO:0000256|PIRSR:PIRSR001461-3"
SQ SEQUENCE 217 AA; 23286 MW; 25F1B1F73F339C5B CRC64;
MIKVAPSILS ADYVNLQPDI EKVDRGGAEV LHIDIMDGQF VPALSYGPGW VKAIRPITKM
VLDVHMMVQN PERYVDDFAK AGADIIGVHV EATPHIHRAL QMIQNAGVTP EVVINPGTPV
SQIEPVLDMV GQVLVMTVNP GFGGQKFLQS TVQKIAQLDA IKKEKGYNFD IEVDGGVNDK
TVVECANAGA TVAVAGSYVF NADDPVARIN ALKDATK
//
