ID A0A1B1Y8D6_9FLAO Unreviewed; 218 AA.
AC A0A1B1Y8D6;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=AXE80_12485 {ECO:0000313|EMBL:ANW97052.1};
OS Wenyingzhuangia fucanilytica.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Wenyingzhuangia.
OX NCBI_TaxID=1790137 {ECO:0000313|EMBL:ANW97052.1, ECO:0000313|Proteomes:UP000092967};
RN [1] {ECO:0000313|EMBL:ANW97052.1, ECO:0000313|Proteomes:UP000092967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CZ1127 {ECO:0000313|EMBL:ANW97052.1,
RC ECO:0000313|Proteomes:UP000092967};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP014224; ANW97052.1; -; Genomic_DNA.
DR RefSeq; WP_068827856.1; NZ_CP014224.1.
DR AlphaFoldDB; A0A1B1Y8D6; -.
DR STRING; 1790137.AXE80_12485; -.
DR KEGG; wfu:AXE80_12485; -.
DR OrthoDB; 1645589at2; -.
DR Proteomes; UP000092967; Chromosome.
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; PS01085; RIBUL_P_3_EPIMER_1; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000092967};
KW Zinc {ECO:0000256|PIRSR:PIRSR001461-2}.
FT ACT_SITE 35
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02227,
FT ECO:0000256|PIRSR:PIRSR001461-1"
FT ACT_SITE 175
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02227,
FT ECO:0000256|PIRSR:PIRSR001461-1"
FT BINDING 8
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02227,
FT ECO:0000256|PIRSR:PIRSR001461-3"
FT BINDING 33
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 35
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 66
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 66
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02227,
FT ECO:0000256|PIRSR:PIRSR001461-3"
FT BINDING 142..145
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02227,
FT ECO:0000256|PIRSR:PIRSR001461-3"
FT BINDING 175..177
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02227"
FT BINDING 175
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 177
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001461-3"
FT BINDING 197..198
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02227,
FT ECO:0000256|PIRSR:PIRSR001461-3"
SQ SEQUENCE 218 AA; 23881 MW; 1569ED20479D153A CRC64;
MSKLVAPSVL AADFANIQRD VEMINSSDAD WFHIDIMDGV FVPNISFGMP VMQAIKKHAT
KPLDVHLMIV NPDQYIKTFK EIGADILTVH YEACTHLHRT IQSIKAEGMQ AGVALNPHTP
ISVLEDIIQD LDLVCIMSVN PGFGGQSFIE NTYTKVQQLK NLITFKGCDT KIEIDGGVTS
KNANNLIEVG ADVLVAGSFV FGAEDPIQTV KELKELIN
//