ID A0A396MFA8_9CLOT Unreviewed; 227 AA. AC A0A396MFA8; DT 05-DEC-2018, integrated into UniProtKB/TrEMBL. DT 05-DEC-2018, sequence version 1. DT 19-JAN-2022, entry version 12. 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 ECO:0000313|EMBL:RHS31415.1}; GN ORFNames=DWV55_12840 {ECO:0000313|EMBL:RHS31415.1}; OS Butyricicoccus sp. AF10-3. OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae; OC Butyricicoccus; unclassified Butyricicoccus. OX NCBI_TaxID=2292196 {ECO:0000313|EMBL:RHS31415.1, ECO:0000313|Proteomes:UP000266580}; RN [1] {ECO:0000313|EMBL:RHS31415.1, ECO:0000313|Proteomes:UP000266580} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AF10-3 {ECO:0000313|EMBL:RHS31415.1, RC ECO:0000313|Proteomes:UP000266580}; RA Zou Y., Xue W., Luo G.; RT "A genome reference for cultivated species of the human gut microbiota."; RL Submitted (AUG-2018) 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:RHS31415.1}. 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; QUHS01000048; RHS31415.1; -; Genomic_DNA. DR EnsemblBacteria; RHS31415; RHS31415; DWV55_12840. DR Proteomes; UP000266580; Unassembled WGS sequence. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0004750; F:ribulose-phosphate 3-epimerase activity; 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; -; 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 PANTHER; PTHR11749; PTHR11749; 1. DR Pfam; PF00834; Ribul_P_3_epim; 1. DR PIRSF; PIRSF001461; RPE; 1. DR SUPFAM; SSF51366; SSF51366; 1. DR TIGRFAMs; TIGR01163; rpe; 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|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}; Zinc {ECO:0000256|PIRSR:PIRSR001461-2}. FT REGION 142..145 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02227, FT ECO:0000256|PIRSR:PIRSR001461-3" FT REGION 175..177 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02227" FT REGION 197..198 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02227, FT ECO:0000256|PIRSR:PIRSR001461-3" 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 METAL 33 FT /note="Divalent metal cation" FT /evidence="ECO:0000256|PIRSR:PIRSR001461-2" FT METAL 33 FT /note="Divalent metal cation; via tele nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02227" FT METAL 35 FT /note="Divalent metal cation" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02227, FT ECO:0000256|PIRSR:PIRSR001461-2" FT METAL 66 FT /note="Divalent metal cation" FT /evidence="ECO:0000256|PIRSR:PIRSR001461-2" FT METAL 66 FT /note="Divalent metal cation; via pros nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02227" FT METAL 175 FT /note="Divalent metal cation" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02227, FT ECO:0000256|PIRSR:PIRSR001461-2" FT BINDING 8 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02227, FT ECO:0000256|PIRSR:PIRSR001461-3" FT BINDING 66 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02227, FT ECO:0000256|PIRSR:PIRSR001461-3" FT BINDING 177 FT /note="Substrate; via amide nitrogen" FT /evidence="ECO:0000256|PIRSR:PIRSR001461-3" SQ SEQUENCE 227 AA; 24201 MW; 1EC8876942A547CA CRC64; MEIKLSPSIL SADFANLARD IKIATDAGAE YVHVDVMDGH FVPNITIGAP VVKALRKATD KVLDVHLMIS DPDQYLDDFI KAGSDIITVH YESNGDTLEQ LKKIRAAGVK AACVIKPKTP AEVLFPLLPY CDMVLIMTVE PGFGGQGFIP ECMDKIKAVR AEIQKNGYKC ELEIDGGAKL NNTADIVAAG ADVIVAGSAV FGGDIAANVK GFHEVFKEGA AKAAWSK //