ID   RPIA_AZOSB              Reviewed;         222 AA.
AC   A1K9D7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 74.
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=azo2826;
OS   Azoarcus sp. (strain BH72).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC   Azoarcus.
OX   NCBI_TaxID=418699;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BH72;
RX   PubMed=17057704; DOI=10.1038/nbt1243;
RA   Krause A., Ramakumar A., Bartels D., Battistoni F., Bekel T., Boch J.,
RA   Boehm M., Friedrich F., Hurek T., Krause L., Linke B., McHardy A.C.,
RA   Sarkar A., Schneiker S., Syed A.A., Thauer R., Vorhoelter F.-J.,
RA   Weidner S., Puehler A., Reinhold-Hurek B., Kaiser O., Goesmann A.;
RT   "Complete genome of the mutualistic, N2-fixing grass endophyte Azoarcus sp.
RT   strain BH72.";
RL   Nat. Biotechnol. 24:1385-1391(2006).
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; AM406670; CAL95442.1; -; Genomic_DNA.
DR   RefSeq; WP_011766552.1; NC_008702.1.
DR   AlphaFoldDB; A1K9D7; -.
DR   SMR; A1K9D7; -.
DR   STRING; 62928.azo2826; -.
DR   PRIDE; A1K9D7; -.
DR   EnsemblBacteria; CAL95442; CAL95442; azo2826.
DR   KEGG; aoa:dqs_2965; -.
DR   KEGG; azo:azo2826; -.
DR   eggNOG; COG0120; Bacteria.
DR   HOGENOM; CLU_056590_1_1_4; -.
DR   OMA; YDWDEVN; -.
DR   OrthoDB; 1681738at2; -.
DR   UniPathway; UPA00115; UER00412.
DR   Proteomes; UP000002588; 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..222
FT                   /note="Ribose-5-phosphate isomerase A"
FT                   /id="PRO_1000016901"
FT   ACT_SITE        103
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT   BINDING         28..31
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT   BINDING         81..84
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT   BINDING         94..97
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT   BINDING         121
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
SQ   SEQUENCE   222 AA;  23290 MW;  BEEC6B70377339C0 CRC64;
     MTQDELKKAA ALAALDYVED GMIVGVGTGS TVNHFIDGLA GIKHRIRGAV SSSEASSKRL
     AAHGIALLDL NDVDELPVYI DGADEIDHGF AMIKGGGGAL TREKIVAAVA RRFVCICDES
     KRVDVLGRFP LPIEVIPMAR SQVMRAAAAL GATPRLREGF VTDNGNLIID LHGLSITDPC
     ATEQALNAVV GVVTNGLFAA RGADTLLLAS AQGVRRFERS AT