ID   RPIA_BORPE              Reviewed;         226 AA.
AC   Q7VWC1;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 89.
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}; OrderedLocusNames=BP2339;
OS   Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257313;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA   Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA   Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA   Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA   Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA   Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
CC   -!- FUNCTION: Catalyzes the reversible conversion of ribose-5-phosphate to
CC       ribulose 5-phosphate. {ECO:0000255|HAMAP-Rule:MF_00170}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosphate;
CC         Xref=Rhea:RHEA:14657, ChEBI:CHEBI:58121, ChEBI:CHEBI:58273;
CC         EC=5.3.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00170};
CC   -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-ribose
CC       5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step
CC       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}.
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DR   EMBL; BX640418; CAE42612.1; -; Genomic_DNA.
DR   RefSeq; NP_880977.1; NC_002929.2.
DR   RefSeq; WP_010930882.1; NZ_CP039022.1.
DR   AlphaFoldDB; Q7VWC1; -.
DR   SMR; Q7VWC1; -.
DR   STRING; 257313.BP2339; -.
DR   GeneID; 45389608; -.
DR   KEGG; bpe:BP2339; -.
DR   PATRIC; fig|257313.5.peg.2521; -.
DR   eggNOG; COG0120; Bacteria.
DR   HOGENOM; CLU_056590_1_1_4; -.
DR   OMA; YDWDEVN; -.
DR   UniPathway; UPA00115; UER00412.
DR   Proteomes; UP000002676; Chromosome.
DR   GO; GO:0004751; F:ribose-5-phosphate isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; IEA:UniProtKB-UniRule.
DR   CDD; cd01398; RPI_A; 1.
DR   HAMAP; MF_00170; Rib_5P_isom_A; 1.
DR   InterPro; IPR037171; NagB/RpiA_transferase-like.
DR   InterPro; IPR020672; Ribose5P_isomerase_typA_subgr.
DR   InterPro; IPR004788; Ribose5P_isomerase_type_A.
DR   PANTHER; PTHR11934; PTHR11934; 1.
DR   Pfam; PF06026; Rib_5-P_isom_A; 1.
DR   SUPFAM; SSF100950; SSF100950; 1.
DR   TIGRFAMs; TIGR00021; rpiA; 1.
PE   3: Inferred from homology;
KW   Isomerase; Reference proteome.
FT   CHAIN           1..226
FT                   /note="Ribose-5-phosphate isomerase A"
FT                   /id="PRO_0000158394"
FT   ACT_SITE        108
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT   BINDING         33..36
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT   BINDING         86..89
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT   BINDING         99..102
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT   BINDING         126
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
SQ   SEQUENCE   226 AA;  23632 MW;  F38296F5C7DBD882 CRC64;
     MLTQQELKQQ AADAALELVE QVAGPDVIIG VGTGSTADLF IDGLACFKGR LRGTVASSER
     SAARLAGHGL AVLDLNDVQS MPIYVDGADE IDPNLHMIKG GGGALTREKI VASVARRYIC
     IADESKLVER LGRFPLPVEV IPMARNAVAR GLSRLGGQPA LREGFVTDNG NIILDVAGLS
     IADAPGLEKT INDIPGVVTC GLFALAGADV ALLATQDGIR RLERRG