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Database: UniProt
Entry: B1X447_PAUCH
LinkDB: B1X447_PAUCH
Original site: B1X447_PAUCH 
ID   B1X447_PAUCH            Unreviewed;       222 AA.
AC   B1X447;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   24-JAN-2024, entry version 64.
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=cfxE {ECO:0000313|EMBL:ACB42716.1};
GN   OrderedLocusNames=PCC_0267 {ECO:0000313|EMBL:ACB42716.1};
OS   Paulinella chromatophora.
OG   Plastid; Organellar chromatophore {ECO:0000313|EMBL:ACB42716.1}.
OC   Eukaryota; Sar; Rhizaria; Cercozoa; Imbricatea; Silicofilosea; Euglyphida;
OC   Paulinellidae; Paulinella.
OX   NCBI_TaxID=39717 {ECO:0000313|EMBL:ACB42716.1};
RN   [1] {ECO:0000313|EMBL:ACB42716.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Gloeckner G., Nowack E., Melkonian M.;
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACB42716.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18356055; DOI=10.1016/j.cub.2008.02.051;
RA   Nowack E.C.M., Melkonian M., Gloeckner G.;
RT   "Chromatophore genome sequence of Paulinella sheds light on acquisition of
RT   photosynthesis by eukaryotes.";
RL   Curr. Biol. 18:410-418(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}.
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DR   EMBL; CP000815; ACB42716.1; -; Genomic_DNA.
DR   RefSeq; YP_002048926.1; NC_011087.1.
DR   AlphaFoldDB; B1X447; -.
DR   GeneID; 6481196; -.
DR   GO; GO:0009536; C:plastid; IEA:UniProtKB-KW.
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-RELATED; 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|ARBA:ARBA00023235, ECO:0000256|PIRNR:PIRNR001461};
KW   Manganese {ECO:0000256|PIRSR:PIRSR001461-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR001461-2}; Plastid {ECO:0000313|EMBL:ACB42716.1};
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        178
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         69
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001461-2"
FT   BINDING         69
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001461-3"
FT   BINDING         145..148
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001461-3"
FT   BINDING         178
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001461-2"
FT   BINDING         180
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001461-3"
FT   BINDING         200..201
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001461-3"
SQ   SEQUENCE   222 AA;  23984 MW;  3B62197F30362CAD CRC64;
     MSTKSLMISP SILSADFSRL GEDVVAVDKA GADWIHVDVM DGRFVPNITI GPLIVEALRP
     VTKKPLDVHL MIIEPERYVA DFAKAGADII SVQVEACPHL HRNLAQIKDL GKMAGAVLNP
     STSLSSLDYC LELCDLVLIM SVNPGFGGQS FIDSQVNKIR ELRRICDERG LDPWIEVDGG
     VKGSNAWKVI EAGANAIVSG SGIFSQSNYA EAIQGIRNSR KP
//
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