(data stored in SCRATCH zone)

SWISSPROT: A0A0H2ZKY8_PSEAB

ID   A0A0H2ZKY8_PSEAB        Unreviewed;       224 AA.
AC   A0A0H2ZKY8;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   07-JUN-2017, entry version 10.
DE   RecName: Full=Ribulose-phosphate 3-epimerase {ECO:0000256|PIRNR:PIRNR001461};
DE            EC=5.1.3.1 {ECO:0000256|PIRNR:PIRNR001461};
GN   Name=rpe {ECO:0000313|EMBL:ABJ15571.1};
GN   OrderedLocusNames=PA14_07910 {ECO:0000313|EMBL:ABJ15571.1};
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963 {ECO:0000313|EMBL:ABJ15571.1, ECO:0000313|Proteomes:UP000000653};
RN   [1] {ECO:0000313|EMBL:ABJ15571.1, ECO:0000313|Proteomes:UP000000653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14 {ECO:0000313|EMBL:ABJ15571.1,
RC   ECO:0000313|Proteomes:UP000000653};
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
CC   -!- CATALYTIC ACTIVITY: D-ribulose 5-phosphate = D-xylulose 5-
CC       phosphate. {ECO:0000256|PIRNR:PIRNR001461}.
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|PIRNR:PIRNR001461}.
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DR   EMBL; CP000438; ABJ15571.1; -; Genomic_DNA.
DR   RefSeq; WP_003085122.1; NC_008463.1.
DR   ProteinModelPortal; A0A0H2ZKY8; -.
DR   SMR; A0A0H2ZKY8; -.
DR   EnsemblBacteria; ABJ15571; ABJ15571; PA14_07910.
DR   KEGG; pau:PA14_07910; -.
DR   KO; K01783; -.
DR   OMA; CHLMIED; -.
DR   Proteomes; UP000000653; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004750; F:ribulose-phosphate 3-epimerase activity; IEA:UniProtKB-EC.
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; -; 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;
DR   PRODOM; A0A0H2ZKY8.
DR   SWISS-2DPAGE; A0A0H2ZKY8.
KW   Carbohydrate metabolism {ECO:0000256|PIRNR:PIRNR001461};
KW   Cobalt {ECO:0000256|PIRSR:PIRSR001461-2};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000653};
KW   Isomerase {ECO:0000256|PIRNR:PIRNR001461};
KW   Manganese {ECO:0000256|PIRSR:PIRSR001461-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001461-2};
KW   Zinc {ECO:0000256|PIRSR:PIRSR001461-2}.
FT   REGION      144    147       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR001461-3}.
FT   REGION      199    200       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR001461-3}.
FT   ACT_SITE     36     36       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR001461-1}.
FT   ACT_SITE    177    177       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR001461-1}.
FT   METAL        34     34       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR001461-2}.
FT   METAL        36     36       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR001461-2}.
FT   METAL        68     68       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR001461-2}.
FT   METAL       177    177       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR001461-2}.
FT   BINDING       9      9       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001461-3}.
FT   BINDING      68     68       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001461-3}.
FT   BINDING     179    179       Substrate; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001461-3}.
SQ   SEQUENCE   224 AA;  24096 MW;  F2172994DEF4C2C0 CRC64;
     MQPFAIAPSI LSADFARLGE DVDKVLAAGA DIVHFDVMDN HYVPNLTIGP MVCSALRKYG
     VSAPIDVHLM VSPVDRIIGD FIEAGATYIT FHPEASQHID RSLQLIRDGG CKAGLVFNPA
     TPLEVLKYVM DKVDMVLLMS VNPGFGGQKF IPGTLDKLRE ARALIDASGR EIRLEIDGGV
     NVKNIREIAA AGADTFVAGS AIFNAPDYAE VIRAMHAELA QAHQ
//

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