RPE_SCHPO
ID RPE_SCHPO Reviewed; 228 AA.
AC O14105;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Ribulose-phosphate 3-epimerase;
DE EC=5.1.3.1 {ECO:0000250|UniProtKB:Q96AT9};
DE AltName: Full=Pentose-5-phosphate 3-epimerase;
DE Short=PPE;
DE AltName: Full=RPE;
GN ORFNames=SPAC31G5.05c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- FUNCTION: Catalyzes the reversible epimerization of D-ribulose 5-
CC phosphate to D-xylulose 5-phosphate. {ECO:0000250|UniProtKB:Q96AT9}.
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:0000250|UniProtKB:Q96AT9};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000250|UniProtKB:Q96AT9};
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:Q96AT9};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q96AT9};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q96AT9};
CC Note=Binds 1 divalent metal cation per subunit. Active with Co(2+),
CC Fe(2+), Mn(2+) and Zn(2+). {ECO:0000250|UniProtKB:Q96AT9};
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC xylulose 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage):
CC step 1/1.
CC -!- SIMILARITY: Belongs to the ribulose-phosphate 3-epimerase family.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAB11689.1; -; Genomic_DNA.
DR PIR; T38622; T38622.
DR RefSeq; NP_594005.1; NM_001019431.2.
DR AlphaFoldDB; O14105; -.
DR SMR; O14105; -.
DR STRING; 4896.SPAC31G5.05c.1; -.
DR iPTMnet; O14105; -.
DR MaxQB; O14105; -.
DR PaxDb; O14105; -.
DR PRIDE; O14105; -.
DR EnsemblFungi; SPAC31G5.05c.1; SPAC31G5.05c.1:pep; SPAC31G5.05c.
DR GeneID; 2543174; -.
DR KEGG; spo:SPAC31G5.05c; -.
DR PomBase; SPAC31G5.05c; -.
DR VEuPathDB; FungiDB:SPAC31G5.05c; -.
DR eggNOG; KOG3111; Eukaryota.
DR HOGENOM; CLU_054856_0_1_1; -.
DR InParanoid; O14105; -.
DR OMA; WLQVDGG; -.
DR PhylomeDB; O14105; -.
DR Reactome; R-SPO-71336; Pentose phosphate pathway.
DR UniPathway; UPA00115; UER00411.
DR PRO; PR:O14105; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0004750; F:D-ribulose-phosphate 3-epimerase activity; IDA:PomBase.
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:0009052; P:pentose-phosphate shunt, non-oxidative branch; EXP:PomBase.
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; Cobalt; Iron; Isomerase; Manganese; Metal-binding;
KW Reference proteome; Zinc.
FT CHAIN 1..228
FT /note="Ribulose-phosphate 3-epimerase"
FT /id="PRO_0000171594"
FT ACT_SITE 36
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P32719"
FT ACT_SITE 175
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P32719"
FT BINDING 9
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32719"
FT BINDING 34
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P32719"
FT BINDING 36
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P32719"
FT BINDING 70
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P32719"
FT BINDING 70
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32719"
FT BINDING 146..149
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32719"
FT BINDING 175..177
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32719"
FT BINDING 175
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P32719"
FT BINDING 197..198
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32719"
SQ SEQUENCE 228 AA; 25205 MW; A537B544C0E5E1E9 CRC64;
MVQAKIAPSL LAGDFANLEK EVGRMLKYGS DWLHVDVMDA QFVPNLTIGP IVVKAMRNHY
TKEEAFFDCH LMVIEPERYI DQLADAGASL FCFHYEATEK HEEIISRAHE KGMLVGCALK
PKTPVEVILP FVEKLDMVLV MTVEPGKGGQ SFMPECLPKV EFLRKKYPTL NVEVDGGLSL
KTVDAAADAG ANVIVAGTAV FHAQSPEEVI SGLRNSVMKA QETKPWFK
