RPE_METJA
ID RPE_METJA Reviewed; 234 AA.
AC Q58093;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 109.
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}; OrderedLocusNames=MJ0680;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
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; L77117; AAB98675.1; -; Genomic_DNA.
DR PIR; H64384; H64384.
DR RefSeq; WP_010870185.1; NC_000909.1.
DR AlphaFoldDB; Q58093; -.
DR SMR; Q58093; -.
DR STRING; 243232.MJ_0680; -.
DR EnsemblBacteria; AAB98675; AAB98675; MJ_0680.
DR GeneID; 1451546; -.
DR KEGG; mja:MJ_0680; -.
DR eggNOG; arCOG05046; Archaea.
DR HOGENOM; CLU_054856_2_1_2; -.
DR InParanoid; Q58093; -.
DR OMA; WLQVDGG; -.
DR OrthoDB; 78990at2157; -.
DR PhylomeDB; Q58093; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004750; F:D-ribulose-phosphate 3-epimerase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IBA:GO_Central.
DR GO; GO:0044262; P:cellular carbohydrate metabolic process; IBA:GO_Central.
DR GO; GO:0019323; P:pentose catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; IBA:GO_Central.
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; Reference proteome.
FT CHAIN 1..234
FT /note="Ribulose-phosphate 3-epimerase"
FT /id="PRO_0000171584"
FT ACT_SITE 34
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT ACT_SITE 172
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT BINDING 7
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT BINDING 32
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
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 65
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT BINDING 65
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT BINDING 139..142
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT BINDING 172..174
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT BINDING 172
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT BINDING 194..195
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
SQ SEQUENCE 234 AA; 25838 MW; 070E2CF7A2BC9D7F CRC64;
MIKIGASILS ADFGHLREEI KKAEEAGVDF FHVDMMDGHF VPNISMGIGI AKHVKKLTEL
PVEVHLMVEN VDLFVNEFEE MDYITFHIEA VKFPFRIINR IKSIGAKPIV ALNPATPLDA
IEYILGDVYA VLVMTVEPGF SGQKFIPVMT KKIRKLKSMI VENGYDTKIF VDGGINVETA
PLAVKAGADV LVAASAIFGK DDVKTAVKNL REAALEALNK DFLTKSFNSN EEKQ
