(data stored in ACNUC7421 zone)

SWISSPROT: RPIA_PSEAB

ID   RPIA_PSEAB              Reviewed;         223 AA.
AC   Q02U86;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   07-JUN-2017, entry version 54.
DE   RecName: Full=Ribose-5-phosphate isomerase A {ECO:0000255|HAMAP-Rule:MF_00170};
DE            EC=5.3.1.6 {ECO:0000255|HAMAP-Rule:MF_00170};
DE   AltName: Full=Phosphoriboisomerase A {ECO:0000255|HAMAP-Rule:MF_00170};
DE            Short=PRI {ECO:0000255|HAMAP-Rule:MF_00170};
GN   Name=rpiA {ECO:0000255|HAMAP-Rule:MF_00170};
GN   OrderedLocusNames=PA14_04310;
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14;
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   -!- FUNCTION: Catalyzes the reversible conversion of ribose-5-
CC       phosphate to ribulose 5-phosphate. {ECO:0000255|HAMAP-
CC       Rule:MF_00170}.
CC   -!- CATALYTIC ACTIVITY: D-ribose 5-phosphate = D-ribulose 5-phosphate.
CC       {ECO:0000255|HAMAP-Rule:MF_00170}.
CC   -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC       ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative
CC       stage): step 1/1. {ECO:0000255|HAMAP-Rule:MF_00170}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00170}.
CC   -!- SIMILARITY: Belongs to the ribose 5-phosphate isomerase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00170}.
DR   EMBL; CP000438; ABJ15293.1; -; Genomic_DNA.
DR   RefSeq; WP_003084386.1; NC_008463.1.
DR   ProteinModelPortal; Q02U86; -.
DR   SMR; Q02U86; -.
DR   PRIDE; Q02U86; -.
DR   EnsemblBacteria; ABJ15293; ABJ15293; PA14_04310.
DR   KEGG; pau:PA14_04310; -.
DR   HOGENOM; HOG000276368; -.
DR   KO; K01807; -.
DR   OMA; VAPMAYV; -.
DR   UniPathway; UPA00115; UER00412.
DR   Proteomes; UP000000653; Chromosome.
DR   GO; GO:0004751; F:ribose-5-phosphate isomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; IEA:InterPro.
DR   CDD; cd01398; RPI_A; 1.
DR   HAMAP; MF_00170; Rib_5P_isom_A; 1.
DR   InterPro; IPR004788; Ribose5P_isomerase_typA.
DR   InterPro; IPR020672; Ribose5P_isomerase_typA_subgr.
DR   Pfam; PF06026; Rib_5-P_isom_A; 1.
DR   TIGRFAMs; TIGR00021; rpiA; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q02U86.
DR   SWISS-2DPAGE; Q02U86.
KW   Complete proteome; Isomerase.
FT   CHAIN         1    223       Ribose-5-phosphate isomerase A.
FT                                /FTId=PRO_1000016963.
FT   REGION       32     35       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00170}.
FT   REGION       85     88       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00170}.
FT   REGION       98    101       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00170}.
FT   ACT_SITE    107    107       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00170}.
FT   BINDING     125    125       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00170}.
SQ   SEQUENCE   223 AA;  23721 MW;  ED096E8EB6AF5E37 CRC64;
     MNQDQLKQAV AQAAVDHILP HLDSKSIVGV GTGSTANFFI DALARHKAEF DGAVASSEAT
     AKRLKEHGIP VYELNTVSEL EFYVDGADES NERLELIKGG GAALTREKIV AAVAKTFICI
     ADASKLVPIL GQFPLPVEVI PMARSHVARQ LVKLGGDPVY REGVLTDNGN IILDVHNLRI
     DSPVELEEKI NAIVGVVTNG LFAARPADLL LLGTADGVKT LKA
//

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