ID   RPIA_BIFLS              Reviewed;         232 AA.
AC   B7GN96; E8MN40;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 66.
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=Blon_2191, BLIJ_2266;
OS   Bifidobacterium longum subsp. infantis (strain ATCC 15697 / DSM 20088 / JCM
OS   1222 / NCTC 11817 / S12).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=391904;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12;
RX   PubMed=19033196; DOI=10.1073/pnas.0809584105;
RA   Sela D.A., Chapman J., Adeuya A., Kim J.H., Chen F., Whitehead T.R.,
RA   Lapidus A., Rokhsar D.S., Lebrilla C.B., German J.B., Price N.P.,
RA   Richardson P.M., Mills D.A.;
RT   "The genome sequence of Bifidobacterium longum subsp. infantis reveals
RT   adaptations for milk utilization within the infant microbiome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:18964-18969(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12;
RX   PubMed=21270894; DOI=10.1038/nature09646;
RA   Fukuda S., Toh H., Hase K., Oshima K., Nakanishi Y., Yoshimura K., Tobe T.,
RA   Clarke J.M., Topping D.L., Suzuki T., Taylor T.D., Itoh K., Kikuchi J.,
RA   Morita H., Hattori M., Ohno H.;
RT   "Bifidobacteria can protect from enteropathogenic infection through
RT   production of acetate.";
RL   Nature 469:543-547(2011).
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; CP001095; ACJ53252.1; -; Genomic_DNA.
DR   EMBL; AP010889; BAJ69843.1; -; Genomic_DNA.
DR   RefSeq; WP_012578451.1; NZ_JDTT01000049.1.
DR   AlphaFoldDB; B7GN96; -.
DR   SMR; B7GN96; -.
DR   PRIDE; B7GN96; -.
DR   EnsemblBacteria; ACJ53252; ACJ53252; Blon_2191.
DR   KEGG; bln:Blon_2191; -.
DR   KEGG; blon:BLIJ_2266; -.
DR   PATRIC; fig|391904.8.peg.2267; -.
DR   HOGENOM; CLU_056590_1_0_11; -.
DR   OMA; YDWDEVN; -.
DR   UniPathway; UPA00115; UER00412.
DR   Proteomes; UP000001360; 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   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.
FT   CHAIN           1..232
FT                   /note="Ribose-5-phosphate isomerase A"
FT                   /id="PRO_1000194690"
FT   ACT_SITE        109
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT   BINDING         31..34
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT   BINDING         87..90
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT   BINDING         100..103
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT   BINDING         127
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
SQ   SEQUENCE   232 AA;  25225 MW;  0FC13A126D7DD423 CRC64;
     MDKAQQDALK KAAGIEAAKL VENGMIAGLG TGSTVKFLVD ELGRRHQEEG LEFTGVTTSR
     RTQAQAESYG IKIVDIDDVD HIDVTIDGAD EVDKNFNGIK GGGAALLWEK IVATNSNQIV
     WIVDESKVVD TIGKFPLPVE VIPFGAGHVI KKFEACGYKP VLRLDADGKE VRTDENNFVV
     DLHLERIDHP QELAEDLINT VGVVEHGLFL NMVDKVIVGD PNGPRVMTNA NK