RPE_SERMA
ID RPE_SERMA Reviewed; 210 AA.
AC P45455;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Ribulose-phosphate 3-epimerase {ECO:0000255|HAMAP-Rule:MF_02227};
DE EC=5.1.3.1 {ECO:0000255|HAMAP-Rule:MF_02227};
GN Name=rpe {ECO:0000255|HAMAP-Rule:MF_02227}; Synonyms=dod;
OS Serratia marcescens.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=615;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sr41;
RA Ostendorf T., Cherepanov P., Jekel M., de Vries J., Wackernagel W.;
RL Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reversible epimerization of D-ribulose 5-
CC phosphate to D-xylulose 5-phosphate. {ECO:0000255|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:0000255|HAMAP-Rule:MF_02227};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02227};
CC Note=Binds 1 divalent metal cation per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_02227};
CC -!- PATHWAY: Carbohydrate degradation. {ECO:0000255|HAMAP-Rule:MF_02227}.
CC -!- SIMILARITY: Belongs to the ribulose-phosphate 3-epimerase family.
CC {ECO:0000255|HAMAP-Rule:MF_02227}.
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DR EMBL; X78412; CAA55178.1; -; Genomic_DNA.
DR PIR; S47100; S47100.
DR AlphaFoldDB; P45455; -.
DR SMR; P45455; -.
DR STRING; 273526.SMDB11_3847; -.
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; -; 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 PANTHER; PTHR11749; PTHR11749; 1.
DR Pfam; PF00834; Ribul_P_3_epim; 1.
DR PIRSF; PIRSF001461; RPE; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR TIGRFAMs; TIGR01163; rpe; 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; Isomerase; Metal-binding.
FT CHAIN 1..210
FT /note="Ribulose-phosphate 3-epimerase"
FT /id="PRO_0000171579"
FT ACT_SITE 36
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT ACT_SITE 177
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT BINDING 9
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT BINDING 34
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT BINDING 36
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT BINDING 68
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT BINDING 68
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT BINDING 144..147
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT BINDING 177..179
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT BINDING 177
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT BINDING 199..200
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
SQ SEQUENCE 210 AA; 22781 MW; D67805D72E2FFBE5 CRC64;
MKKFLIAPSI LSADFARLGE DTANVLAAGG DVVHFDVMDN HYVPNLTIGP MVCEALRNYG
ITAPIDVHLM VKPVDRIVPD FAKAGASYIS FHPEASEHVD RTIQLIKEHG CKAGLVFNPA
TPLSYLDYVM DKIDVILLMS VNPGFGGQSF IHGTLDKLRQ VRKLIDDSGR DIRLEVDGGV
KVDNIAEIAA AGADMFVAGS AIFGQPDYRK
