ID   RPIA_ALBFT              Reviewed;         234 AA.
AC   Q21WC3;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, 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=Rfer_2206;
OS   Albidiferax ferrireducens (strain ATCC BAA-621 / DSM 15236 / T118)
OS   (Rhodoferax ferrireducens).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Rhodoferax.
OX   NCBI_TaxID=338969;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-621 / DSM 15236 / T118;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of chromosome of Rhodoferax ferrireducens DSM 15236.";
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000267; ABD69930.1; -; Genomic_DNA.
DR   RefSeq; WP_011464498.1; NC_007908.1.
DR   AlphaFoldDB; Q21WC3; -.
DR   SMR; Q21WC3; -.
DR   STRING; 338969.Rfer_2206; -.
DR   EnsemblBacteria; ABD69930; ABD69930; Rfer_2206.
DR   KEGG; rfr:Rfer_2206; -.
DR   eggNOG; COG0120; Bacteria.
DR   HOGENOM; CLU_056590_1_1_4; -.
DR   OMA; GHYIVDL; -.
DR   OrthoDB; 1681738at2; -.
DR   UniPathway; UPA00115; UER00412.
DR   Proteomes; UP000008332; 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..234
FT                   /note="Ribose-5-phosphate isomerase A"
FT                   /id="PRO_1000097688"
FT   ACT_SITE        114
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT   BINDING         39..42
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT   BINDING         92..95
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT   BINDING         105..108
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT   BINDING         132
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
SQ   SEQUENCE   234 AA;  24483 MW;  BC724B95F9561F0A CRC64;
     MTNPISQAAG ALSQDELKTL VGQAALQYVA PGEIVGVGTG STVNKFIDAL ASIRHLIKGA
     VSSSEASTLR LKALGIPVFD ANEVAELSVY IDGADEIDGH GNMIKGGGAA LTREKIVAAL
     ANQFVCIADE SKLVQTLGRY PLPVEIIPMA AQRITQQFAA LGGRAQVRLK GDQPLVTDNG
     QILLDVTGLQ ISDPLAFETL VSQWPGVVTV GVFAYQKAQV CLLGTARGVK TLTF