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 27-MAR-2024, entry version 28. DE RecName: Full=Ribulose-phosphate 3-epimerase {ECO:0000256|ARBA:ARBA00013188, ECO:0000256|PIRNR:PIRNR001461}; DE EC=5.1.3.1 {ECO:0000256|ARBA:ARBA00013188, ECO:0000256|PIRNR:PIRNR001461}; GN ORFNames=PKNH_1439100 {ECO:0000313|EMBL:CAA9990987.1}; OS Plasmodium knowlesi (strain H). OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium). OX NCBI_TaxID=5851 {ECO:0000313|EMBL:CAA9990987.1, ECO:0000313|Proteomes:UP000031513}; RN [1] {ECO:0000313|EMBL:CAA9990987.1, ECO:0000313|Proteomes:UP000031513} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=H {ECO:0000313|EMBL:CAA9990987.1, 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., Lapp S., RA Marti M., Moule S., Meyer I.M., Ormond D., Peters N., Sanders M., RA Sanders S., Sergeant T.J., Simmonds M., Smith F., Squares R., Thurston S., RA Tivey A.R., Walker D., White B., Zuiderwijk E., Churcher C., Quail M.A., RA Cowman A.F., Turner C.M.R., Rajandream M.A., Kocken C.H.M., Thomas A.W., RA Newbold C.I., Barrell B.G., Berriman M.; RT "The genome of Plasmodium knowlesi strain H, a zoonotic malaria parasite RT with host range from monkey to man."; RL Nature 455:799-803(2008). 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|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|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|ARBA:ARBA00009541, 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; CAA9990987.1; -; Genomic_DNA. DR RefSeq; XP_002262269.1; XM_002262233.1. DR AlphaFoldDB; A0A384L6B3; -. DR STRING; 5851.A0A384L6B3; -. DR GeneID; 7323288; -. DR KEGG; pkn:PKNH_1439100; -. DR VEuPathDB; PlasmoDB:PKNH_1439100; -. DR InParanoid; A0A384L6B3; -. DR OMA; CHLMIED; -. DR OrthoDB; 101513at2759; -. DR Proteomes; UP000031513; Chromosome 14. DR GO; GO:0004750; F:D-ribulose-phosphate 3-epimerase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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; Aldolase class I; 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; 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 Carbohydrate metabolism {ECO:0000256|PIRNR:PIRNR001461}; KW Cobalt {ECO:0000256|PIRSR:PIRSR001461-2}; KW Isomerase {ECO:0000256|PIRNR:PIRNR001461, ECO:0000313|EMBL:CAA9990987.1}; 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 ACT_SITE 38 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR001461-1" FT ACT_SITE 179 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR001461-1" FT BINDING 11 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001461-3" FT BINDING 36 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000256|PIRSR:PIRSR001461-2" FT BINDING 38 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000256|PIRSR:PIRSR001461-2" FT BINDING 70 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000256|PIRSR:PIRSR001461-2" FT BINDING 70 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001461-3" FT BINDING 150..153 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001461-3" FT BINDING 179 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000256|PIRSR:PIRSR001461-2" FT BINDING 181 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001461-3" FT BINDING 201..202 FT /ligand="substrate" FT /evidence="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 //