ID A0A5C7EPA8_9ACTN Unreviewed; 226 AA. AC A0A5C7EPA8; DT 13-NOV-2019, integrated into UniProtKB/TrEMBL. DT 13-NOV-2019, sequence version 1. DT 13-SEP-2023, entry version 18. 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=E4J93_04465 {ECO:0000313|EMBL:TXF36660.1}; OS Collinsella sp. BA40. OC Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales; OC Coriobacteriaceae; Collinsella. OX NCBI_TaxID=2560852 {ECO:0000313|EMBL:TXF36660.1, ECO:0000313|Proteomes:UP000321063}; RN [1] {ECO:0000313|EMBL:TXF36660.1, ECO:0000313|Proteomes:UP000321063} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BA40 {ECO:0000313|EMBL:TXF36660.1, RC ECO:0000313|Proteomes:UP000321063}; RA Park J.-K.; RT "Collinsella canisensis sp. nov., a novel bacterium isolated from canine RT feces."; RL Submitted (AUG-2019) 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}. 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:TXF36660.1}. 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; VOWY01000010; TXF36660.1; -; Genomic_DNA. DR AlphaFoldDB; A0A5C7EPA8; -. DR OrthoDB; 1645589at2; -. DR Proteomes; UP000321063; 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-RELATED; 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|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_02227}; KW Manganese {ECO:0000256|PIRSR:PIRSR001461-2}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_02227}; Reference proteome {ECO:0000313|Proteomes:UP000321063}; 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 10 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 226 AA; 23793 MW; 0990466D4D980FE8 CRC64; MHDSVLVSPS ILSADMAHLA DDLDKIAGAD YIHIDVMDGH FTKNLTFGAG IVGACKRSTD VPLDVHMMVT NPDDTVDWYI DAGADLITIH FEASTHLHGT LKHIQSRGVK AGVVLNPATP VSLLENIIED VDAVLLMSVN PGFGGQSFIE GTFAKIRELR ALCERHGVSP LIEVDGGVSR KNVEAVCAAG ANMVVAGSAV FGADDPASEI DVIRELGTRG LASARG //