ID A0A384L6B3_PLAKH Unreviewed; 227 AA. AC A0A384L6B3; A0A1A7VFN5; B3LCI8; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 13-FEB-2019, entry version 3. DE RecName: Full=Ribulose-phosphate 3-epimerase {ECO:0000256|PIRNR:PIRNR001461}; DE EC=5.1.3.1 {ECO:0000256|PIRNR:PIRNR001461}; GN ORFNames=PKH_143650 {ECO:0000313|EMBL:CAQ42147.1}, PKNA1_C2_1439100 GN {ECO:0000313|EMBL:SBO20755.1}, PKNA1_H1_1439100 GN {ECO:0000313|EMBL:SBO21212.1}; OS Plasmodium knowlesi (strain H). OC Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium). OX NCBI_TaxID=5851 {ECO:0000313|EMBL:SBO20755.1}; RN [1] {ECO:0000313|EMBL:CAQ42147.1, ECO:0000313|Proteomes:UP000031513} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=H {ECO:0000313|EMBL:CAQ42147.1, RC ECO:0000313|Proteomes:UP000031513}; RA Pain A., Boehme U., Berry A.E., Mungall K., Finn R., Jackson A.P., RA Mourier T., Mistry J., Pasini E.M., Aslett M., Balasubrammaniam S., RA Borgwardt K., Brooks K., Carret C., Carver T.J., Cherevach I., RA Chillingworth T., Clarke T.G., Galinski M.R., Hall N., Harper D., RA Harris D., Hauser H., Ivens A., Janssen C.S., Keane T., Larke N., RA Lapp S., Marti M., Moule S., Meyer I.M., Ormond D., Peters N., RA Sanders M., Sanders S., Sergeant T.J., Simmonds M., Smith F., RA Squares R., Thurston S., Tivey A.R., Walker D., White B., RA Zuiderwijk E., Churcher C., Quail M.A., Cowman A.F., Turner C.M.R., RA Rajandream M.A., Kocken C.H.M., Thomas A.W., Newbold C.I., RA Barrell B.G., Berriman M.; RT "The genome of Plasmodium knowlesi strain H, a zoonotic malaria RT parasite with host range from monkey to man."; RL Nature 455:799-803(2008). RN [2] {ECO:0000313|EMBL:SBO20755.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Lavstsen T., Jespersen J.S.; RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases. 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|PIRNR:PIRNR001461}; CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000256|PIRSR:PIRSR001461-2}; CC Note=Binds 1 divalent metal cation per subunit. CC {ECO:0000256|PIRSR:PIRSR001461-2}; CC -!- SIMILARITY: Belongs to the ribulose-phosphate 3-epimerase family. CC {ECO:0000256|PIRNR:PIRNR001461}. 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; AM910996; CAQ42147.1; -; Genomic_DNA. DR EMBL; CWHQ02000003; SBO20755.1; -; Genomic_DNA. DR EMBL; CWHR02000002; SBO21212.1; -; Genomic_DNA. DR RefSeq; XP_002262269.1; XM_002262233.1. DR STRING; 5850.PKH_143650; -. DR GeneID; 7323288; -. DR KEGG; pkn:PKH_143650; -. DR HOGENOM; HOG000259349; -. DR KO; K01783; -. DR Proteomes; UP000031513; Chromosome 14. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004750; F:ribulose-phosphate 3-epimerase activity; IEA:UniProtKB-EC. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW. DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:InterPro. DR CDD; cd00429; RPE; 1. DR Gene3D; 3.20.20.70; -; 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 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|PIRNR:PIRNR001461}; KW Cobalt {ECO:0000256|PIRSR:PIRSR001461-2}; KW Complete proteome {ECO:0000313|Proteomes:UP000031513}; KW Isomerase {ECO:0000256|PIRNR:PIRNR001461}; KW Manganese {ECO:0000256|PIRSR:PIRSR001461-2}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR001461-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000031513}; KW Zinc {ECO:0000256|PIRSR:PIRSR001461-2}. FT REGION 150 153 Substrate binding. {ECO:0000256|PIRSR: FT PIRSR001461-3}. FT REGION 201 202 Substrate binding. {ECO:0000256|PIRSR: FT PIRSR001461-3}. FT ACT_SITE 38 38 Proton acceptor. {ECO:0000256|PIRSR: FT PIRSR001461-1}. FT ACT_SITE 179 179 Proton donor. {ECO:0000256|PIRSR: FT PIRSR001461-1}. FT METAL 36 36 Divalent metal cation. FT {ECO:0000256|PIRSR:PIRSR001461-2}. FT METAL 38 38 Divalent metal cation. FT {ECO:0000256|PIRSR:PIRSR001461-2}. FT METAL 70 70 Divalent metal cation. FT {ECO:0000256|PIRSR:PIRSR001461-2}. FT METAL 179 179 Divalent metal cation. FT {ECO:0000256|PIRSR:PIRSR001461-2}. FT BINDING 11 11 Substrate. {ECO:0000256|PIRSR: FT PIRSR001461-3}. FT BINDING 70 70 Substrate. {ECO:0000256|PIRSR: FT PIRSR001461-3}. FT BINDING 181 181 Substrate; via amide nitrogen. FT {ECO:0000256|PIRSR:PIRSR001461-3}. SQ SEQUENCE 227 AA; 25566 MW; 6CFE0AD317630927 CRC64; MSSLKAIIAP SVLASNISKL AEETQRMEEL GAEWIHLDVM DMHFVPNLSF GPPVINDLKK YTKDIFFDVH LMVENPEKYV DLLKTSDQLT FHFEALNEDT DKCVKLAQQI RNNNQWCGVS IKPKTNVEKI VPLLDTNLIN TVLVMTVEPG FGGQSFMHDM MSKVAFLRKK YTDLNIQVDG GLNIETTEIS ASHGANVIVA GTSIFKADNP KFVIDTMRES VRKHLQK //