ID RPE2_CUPNH Reviewed; 241 AA. AC Q04539; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 27-MAR-2024, entry version 132. DE RecName: Full=Ribulose-phosphate 3-epimerase 2 {ECO:0000255|HAMAP-Rule:MF_02227}; DE EC=5.1.3.1 {ECO:0000255|HAMAP-Rule:MF_02227}; GN Name=rpe2 {ECO:0000255|HAMAP-Rule:MF_02227}; Synonyms=cbbEP, cfxE; GN OrderedLocusNames=PHG423; OS Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 OS / H16 / Stanier 337) (Ralstonia eutropha). OG Plasmid megaplasmid pHG1. OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Cupriavidus. OX NCBI_TaxID=381666; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1429456; DOI=10.1128/jb.174.22.7337-7344.1992; RA Kusian B., Yoo J.-G., Bednarski R., Bowien B.; RT "The Calvin cycle enzyme pentose-5-phosphate 3-epimerase is encoded within RT the cfx operons of the chemoautotroph Alcaligenes eutrophus."; RL J. Bacteriol. 174:7337-7344(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier RC 337; RX PubMed=12948488; DOI=10.1016/s0022-2836(03)00894-5; RA Schwartz E., Henne A., Cramm R., Eitinger T., Friedrich B., Gottschalk G.; RT "Complete nucleotide sequence of pHG1: a Ralstonia eutropha H16 megaplasmid RT encoding key enzymes of H(2)-based lithoautotrophy and anaerobiosis."; RL J. Mol. Biol. 332:369-383(2003). CC -!- FUNCTION: Catalyzes the reversible epimerization of D-ribulose 5- CC phosphate to D-xylulose 5-phosphate. {ECO:0000255|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:0000255|HAMAP-Rule:MF_02227}; CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000255|HAMAP-Rule:MF_02227}; CC Note=Binds 1 divalent metal cation per subunit. {ECO:0000255|HAMAP- CC Rule:MF_02227}; CC -!- PATHWAY: Carbohydrate degradation. {ECO:0000255|HAMAP-Rule:MF_02227}. CC -!- SIMILARITY: Belongs to the ribulose-phosphate 3-epimerase family. CC {ECO:0000255|HAMAP-Rule:MF_02227}. 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; M64172; AAA98231.1; -; Genomic_DNA. DR EMBL; AY305378; AAP86172.1; -; Genomic_DNA. DR RefSeq; WP_011154335.1; NZ_CP039289.1. DR AlphaFoldDB; Q04539; -. DR SMR; Q04539; -. DR GeneID; 39976486; -. DR KEGG; reh:PHG423; -. DR PATRIC; fig|381666.6.peg.351; -. DR eggNOG; COG0036; Bacteria. DR HOGENOM; CLU_054856_1_0_4; -. DR OrthoDB; 1645589at2; -. DR Proteomes; UP000008210; Plasmid megaplasmid pHG1. 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 GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW. 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 Calvin cycle; Carbohydrate metabolism; Isomerase; Metal-binding; Plasmid; KW Reference proteome. FT CHAIN 1..241 FT /note="Ribulose-phosphate 3-epimerase 2" FT /id="PRO_0000171557" FT ACT_SITE 48 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227" FT ACT_SITE 192 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227" FT BINDING 21 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227" FT BINDING 46 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227" FT BINDING 48 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227" FT BINDING 79 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227" FT BINDING 79 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227" FT BINDING 155..158 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227" FT BINDING 192..194 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227" FT BINDING 192 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227" FT BINDING 214..215 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227" SQ SEQUENCE 241 AA; 25594 MW; 6FACA5B81D6734CD CRC64; MHATEPNTGH GSQRAIRLAP SILSADFARL GEEVCAIEAG GADLVHFDVM DNHYVSNLTI GPLVCEAIRP LVSIPIDVHL MVEPVDALIP MFAKAGANLI SFHPEASRHV DRTIGLIRDH GCKAGLVLNP ATPLSWLDHT LDKLDLVLLM SVNPGFGGQA FIPGVLDKVR QARARIDRQV AAGGRPVWLE IDGGVKADNI TEIARAGADT FVAGSAVFGA PDADGGYRGI LHRLREAATI T //