ID   A3PEX8_PROM0            Unreviewed;       231 AA.
AC   A3PEX8;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   18-JUN-2025, entry version 109.
DE   RecName: Full=Ribose-5-phosphate isomerase A {ECO:0000256|HAMAP-Rule:MF_00170};
DE            EC=5.3.1.6 {ECO:0000256|HAMAP-Rule:MF_00170};
DE   AltName: Full=Phosphoriboisomerase A {ECO:0000256|HAMAP-Rule:MF_00170};
DE            Short=PRI {ECO:0000256|HAMAP-Rule:MF_00170};
GN   Name=rpiA {ECO:0000256|HAMAP-Rule:MF_00170,
GN   ECO:0000313|EMBL:ABO18303.1};
GN   OrderedLocusNames=P9301_16801 {ECO:0000313|EMBL:ABO18303.1};
OS   Prochlorococcus marinus (strain MIT 9301).
OC   Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Prochlorococcaceae; Prochlorococcus.
OX   NCBI_TaxID=167546 {ECO:0000313|EMBL:ABO18303.1, ECO:0000313|Proteomes:UP000001430};
RN   [1] {ECO:0000313|EMBL:ABO18303.1, ECO:0000313|Proteomes:UP000001430}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9301 {ECO:0000313|EMBL:ABO18303.1,
RC   ECO:0000313|Proteomes:UP000001430};
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
CC   -!- FUNCTION: Catalyzes the reversible conversion of ribose-5-phosphate to
CC       ribulose 5-phosphate. {ECO:0000256|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:0000256|ARBA:ARBA00001713,
CC         ECO:0000256|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:0000256|HAMAP-Rule:MF_00170}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00170}.
CC   -!- SIMILARITY: Belongs to the ribose 5-phosphate isomerase family.
CC       {ECO:0000256|ARBA:ARBA00008088, ECO:0000256|HAMAP-Rule:MF_00170}.
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DR   EMBL; CP000576; ABO18303.1; -; Genomic_DNA.
DR   RefSeq; WP_011863600.1; NC_009091.1.
DR   AlphaFoldDB; A3PEX8; -.
DR   STRING; 167546.P9301_16801; -.
DR   KEGG; pmg:P9301_16801; -.
DR   eggNOG; COG0120; Bacteria.
DR   HOGENOM; CLU_056590_1_1_3; -.
DR   OrthoDB; 5870696at2; -.
DR   UniPathway; UPA00115; UER00412.
DR   Proteomes; UP000001430; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0004751; F:ribose-5-phosphate isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006014; P:D-ribose metabolic process; IEA:TreeGrafter.
DR   GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; IEA:UniProtKB-UniRule.
DR   CDD; cd01398; RPI_A; 1.
DR   FunFam; 3.30.70.260:FF:000018; Ribose-5-phosphate isomerase A; 1.
DR   FunFam; 3.40.50.1360:FF:000001; Ribose-5-phosphate isomerase A; 1.
DR   Gene3D; 3.30.70.260; -; 1.
DR   Gene3D; 3.40.50.1360; -; 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   NCBIfam; NF001924; PRK00702.1; 1.
DR   NCBIfam; TIGR00021; rpiA; 1.
DR   PANTHER; PTHR11934; RIBOSE-5-PHOSPHATE ISOMERASE; 1.
DR   PANTHER; PTHR11934:SF0; RIBOSE-5-PHOSPHATE ISOMERASE; 1.
DR   Pfam; PF06026; Rib_5-P_isom_A; 1.
DR   SUPFAM; SSF75445; D-ribose-5-phosphate isomerase (RpiA), lid domain; 1.
DR   SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001430}.
FT   ACT_SITE        102
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00170"
FT   BINDING         23..26
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00170"
FT   BINDING         80..83
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00170"
FT   BINDING         93..96
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00170"
FT   BINDING         120
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00170"
SQ   SEQUENCE   231 AA;  24702 MW;  0B1C691260374B2B CRC64;
     MKQVVADAAI REVKSDMILG LGSGSTAALM IKSLADEMRS GKLQNIKGVA TSFQSEVLAL
     ELNIPLIDLA SVSQIDLAID GADEVDPGFQ LIKGGGACHV REKLVASKAD QLLIVVDETK
     LVQNLNLSFP LPVEVLPNAW KQVQEVISEM KGSSTLRMAT KKAGPVVTDQ GNLILDVLFD
     DGINNPKDIE MKINNIPGVL ENGLFVDLTD KVLVGKIENN TPVVYSPSRA S
//