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Database: UniProt
Entry: J0KS22_9BURK
LinkDB: J0KS22_9BURK
Original site: J0KS22_9BURK 
ID   J0KS22_9BURK            Unreviewed;       226 AA.
AC   J0KS22;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=Ribulose-phosphate 3-epimerase {ECO:0000256|ARBA:ARBA00013188, ECO:0000256|HAMAP-Rule:MF_02227};
DE            EC=5.1.3.1 {ECO:0000256|ARBA:ARBA00013188, ECO:0000256|HAMAP-Rule:MF_02227};
GN   Name=rpe {ECO:0000256|HAMAP-Rule:MF_02227};
GN   ORFNames=PMI14_01165 {ECO:0000313|EMBL:EJE53953.1};
OS   Acidovorax sp. CF316.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=1144317 {ECO:0000313|EMBL:EJE53953.1, ECO:0000313|Proteomes:UP000004811};
RN   [1] {ECO:0000313|EMBL:EJE53953.1, ECO:0000313|Proteomes:UP000004811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF316 {ECO:0000313|EMBL:EJE53953.1,
RC   ECO:0000313|Proteomes:UP000004811};
RX   PubMed=23045501; DOI=10.1128/JB.01243-12;
RA   Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA   Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT   "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT   sequences from diverse bacteria isolated from the rhizosphere and
RT   endosphere of Populus deltoides.";
RL   J. Bacteriol. 194:5991-5993(2012).
CC   -!- FUNCTION: Catalyzes the reversible epimerization of D-ribulose 5-
CC       phosphate to D-xylulose 5-phosphate. {ECO:0000256|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:0000256|ARBA:ARBA00001782,
CC         ECO:0000256|HAMAP-Rule:MF_02227, 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|HAMAP-Rule:MF_02227,
CC         ECO:0000256|PIRSR:PIRSR001461-2};
CC       Note=Binds 1 divalent metal cation per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_02227, ECO:0000256|PIRSR:PIRSR001461-2};
CC   -!- PATHWAY: Carbohydrate degradation. {ECO:0000256|HAMAP-Rule:MF_02227}.
CC   -!- SIMILARITY: Belongs to the ribulose-phosphate 3-epimerase family.
CC       {ECO:0000256|ARBA:ARBA00009541, ECO:0000256|HAMAP-Rule:MF_02227,
CC       ECO:0000256|PIRNR:PIRNR001461}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EJE53953.1}.
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DR   EMBL; AKJX01000047; EJE53953.1; -; Genomic_DNA.
DR   RefSeq; WP_007850948.1; NZ_AKJX01000047.1.
DR   AlphaFoldDB; J0KS22; -.
DR   PATRIC; fig|1144317.3.peg.1101; -.
DR   Proteomes; UP000004811; Unassembled WGS sequence.
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   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|HAMAP-Rule:MF_02227,
KW   ECO:0000256|PIRNR:PIRNR001461}; Cobalt {ECO:0000256|PIRSR:PIRSR001461-2};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_02227};
KW   Manganese {ECO:0000256|PIRSR:PIRSR001461-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_02227}; Reference proteome {ECO:0000313|Proteomes:UP000004811};
KW   Zinc {ECO:0000256|PIRSR:PIRSR001461-2}.
FT   ACT_SITE        37
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02227,
FT                   ECO:0000256|PIRSR:PIRSR001461-1"
FT   ACT_SITE        183
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02227,
FT                   ECO:0000256|PIRSR:PIRSR001461-1"
FT   BINDING         10
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02227,
FT                   ECO:0000256|PIRSR:PIRSR001461-3"
FT   BINDING         35
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02227,
FT                   ECO:0000256|PIRSR:PIRSR001461-2"
FT   BINDING         37
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02227,
FT                   ECO:0000256|PIRSR:PIRSR001461-2"
FT   BINDING         74
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02227,
FT                   ECO:0000256|PIRSR:PIRSR001461-2"
FT   BINDING         74
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02227,
FT                   ECO:0000256|PIRSR:PIRSR001461-3"
FT   BINDING         150..153
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02227,
FT                   ECO:0000256|PIRSR:PIRSR001461-3"
FT   BINDING         183..185
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02227"
FT   BINDING         183
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02227,
FT                   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|HAMAP-Rule:MF_02227,
FT                   ECO:0000256|PIRSR:PIRSR001461-3"
SQ   SEQUENCE   226 AA;  24340 MW;  5E167DB4779B493D CRC64;
     MSRPFRIAPS ILSADFARLG EEVRNVIAAG ADWIHFDVMD NHYVPNLTFG PMVCQALKPH
     AKTADGTAIP VDVHLMIQPV DALAAAFADA GADYISFHPD ASGHVHRSIQ AIRSKGVKPG
     LVFNPASPLD VLDWVIDDID LILIMSVNPG FGGQSFIDSA LRKIEDVRRR IDASGKDIRL
     EVDGGIKTDN IRRVADAGAD TFVAGSAIFG KPDYKGVIDA MRLQLG
//
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