ID F0YNL6_AURAN Unreviewed; 241 AA.
AC F0YNL6;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
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 Name=RPE {ECO:0000313|EMBL:EGB03298.1};
GN ORFNames=AURANDRAFT_34246 {ECO:0000313|EMBL:EGB03298.1};
OS Aureococcus anophagefferens (Harmful bloom alga).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Pelagophyceae; Pelagomonadales;
OC Aureococcus.
OX NCBI_TaxID=44056 {ECO:0000313|Proteomes:UP000002729};
RN [1] {ECO:0000313|EMBL:EGB03298.1, ECO:0000313|Proteomes:UP000002729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP 1984 {ECO:0000313|Proteomes:UP000002729};
RX PubMed=21368207; DOI=10.1073/pnas.1016106108;
RA Gobler C.J., Berry D.L., Dyhrman S.T., Wilhelm S.W., Salamov A.,
RA Lobanov A.V., Zhang Y., Collier J.L., Wurch L.L., Kustka A.B., Dill B.D.,
RA Shah M., VerBerkmoes N.C., Kuo A., Terry A., Pangilinan J., Lindquist E.A.,
RA Lucas S., Paulsen I.T., Hattenrath-Lehmann T.K., Talmage S.C., Walker E.A.,
RA Koch F., Burson A.M., Marcoval M.A., Tang Y.Z., Lecleir G.R., Coyne K.J.,
RA Berg G.M., Bertrand E.M., Saito M.A., Gladyshev V.N., Grigoriev I.V.;
RT "Niche of harmful alga Aureococcus anophagefferens revealed through
RT ecogenomics.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:4352-4357(2011).
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}.
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DR EMBL; GL833178; EGB03298.1; -; Genomic_DNA.
DR RefSeq; XP_009042015.1; XM_009043767.1.
DR AlphaFoldDB; F0YNL6; -.
DR EnsemblProtists; EGB03298; EGB03298; AURANDRAFT_34246.
DR GeneID; 20221405; -.
DR KEGG; aaf:AURANDRAFT_34246; -.
DR InParanoid; F0YNL6; -.
DR OrthoDB; 101513at2759; -.
DR Proteomes; UP000002729; Unassembled WGS sequence.
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 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.
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};
KW Manganese {ECO:0000256|PIRSR:PIRSR001461-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001461-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000002729};
KW Zinc {ECO:0000256|PIRSR:PIRSR001461-2}.
FT ACT_SITE 42
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001461-1"
FT ACT_SITE 183
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001461-1"
FT BINDING 15
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001461-3"
FT BINDING 40
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR001461-2"
FT BINDING 42
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR001461-2"
FT BINDING 74
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR001461-2"
FT BINDING 74
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 183
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR001461-2"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001461-3"
FT BINDING 205..206
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001461-3"
SQ SEQUENCE 241 AA; 25849 MW; 04910E0B9B13CA37 CRC64;
MELIEPDKDF LIAPSILSAD FARLGEEVVN SLSAGADVVH FDVMDNHYVP NLTIGPMVCS
ALRKHGVTAP IDVHLMVSPV DRIVGDFADA GASYITFHPE ASPHVDRTLQ LIRGAGCKAG
LVFNPATPLD ILKYVMDKVD IILLMSVNPG FGGQSFIPAT LDKAREARKL IDASGYDIRL
EIDGGVSGAN IKEVAEAGVD MFVAGSAIFR DPRTEEDYKV TIDAMRDELA AAKVPANLVE
S
//
