ID RPE1_CUPNH Reviewed; 241 AA. AC P40117; Q0K1E4; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 27-MAR-2024, entry version 120. DE RecName: Full=Ribulose-phosphate 3-epimerase 1 {ECO:0000255|HAMAP-Rule:MF_02227}; DE EC=5.1.3.1 {ECO:0000255|HAMAP-Rule:MF_02227}; GN Name=rpe1 {ECO:0000255|HAMAP-Rule:MF_02227}; GN Synonyms=cbbE2, cbbEC, cfxE; OrderedLocusNames=H16_B1391; OS Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 OS / H16 / Stanier 337) (Ralstonia eutropha). 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=16964242; DOI=10.1038/nbt1244; RA Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R., RA Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I., RA Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.; RT "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia RT eutropha H16."; RL Nat. Biotechnol. 24:1257-1262(2006). 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; M64173; AAA21962.1; -; Genomic_DNA. DR EMBL; AM260480; CAJ96180.1; -; Genomic_DNA. DR PIR; C47019; C47019. DR RefSeq; WP_011617203.1; NZ_CP039288.1. DR AlphaFoldDB; P40117; -. DR SMR; P40117; -. DR STRING; 381666.H16_B1391; -. DR GeneID; 57647289; -. DR KEGG; reh:H16_B1391; -. DR eggNOG; COG0036; Bacteria. DR HOGENOM; CLU_054856_2_1_4; -. DR OrthoDB; 1645589at2; -. DR Proteomes; UP000008210; Chromosome 2. 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; KW Reference proteome. FT CHAIN 1..241 FT /note="Ribulose-phosphate 3-epimerase 1" FT /id="PRO_0000171556" 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; 25501 MW; 9B6CC244FD1215CC CRC64; MHATELNTGH GSQRAIRLAP SILSADFARL GEEVCAIEAG GADLVHFDVM DNHYVPNLTI GPLVCEAIRP LVSIPIDVHL MVEPVDALIP LFAKAGANII SFHPEASRHV DRTIGLIRDH GCKAGLVLNP ATPLGWLDHT LDQLDLVLLM SVNPGFGGQA FIPGVLDKVR QARARIDRQV DAGGRPVWLE IDGGVKADNI AAIARAGADT FVAGSAVFGA PDADGGYSSI LYRLREAATV T //