ID   B0JM55_MICAN            Unreviewed;       236 AA.
AC   B0JM55;
DT   18-MAR-2008, integrated into UniProtKB/TrEMBL.
DT   18-MAR-2008, sequence version 1.
DT   04-NOV-2026, entry version 103.
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:BAG00072.1};
GN   OrderedLocusNames=MAE_02500 {ECO:0000313|EMBL:BAG00072.1};
OS   Microcystis aeruginosa (strain NIES-843 / IAM M-2473).
OC   Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Microcystaceae; Microcystis.
OX   NCBI_TaxID=449447 {ECO:0000313|EMBL:BAG00072.1, ECO:0000313|Proteomes:UP000001510};
RN   [1] {ECO:0000313|EMBL:BAG00072.1, ECO:0000313|Proteomes:UP000001510}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-843 / IAM M-247 {ECO:0000313|Proteomes:UP000001510};
RX   PubMed=18192279; DOI=10.1093/dnares/dsm026;
RA   Kaneko T., Nakajima N., Okamoto S., Suzuki I., Tanabe Y., Tamaoki M.,
RA   Nakamura Y., Kasai F., Watanabe A., Kawashima K., Kishida Y., Ono A.,
RA   Shimizu Y., Takahashi C., Minami C., Fujishiro T., Kohara M., Katoh M.,
RA   Nakazaki N., Nakayama S., Yamada M., Tabata S., Watanabe M.M.;
RT   "Complete genomic structure of the bloom-forming toxic cyanobacterium
RT   Microcystis aeruginosa NIES-843.";
RL   DNA Res. 14:247-256(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|HAMAP-Rule:MF_00170}.
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DR   EMBL; AP009552; BAG00072.1; -; Genomic_DNA.
DR   RefSeq; WP_012263957.1; NC_010296.1.
DR   AlphaFoldDB; B0JM55; -.
DR   STRING; 449447.MAE_02500; -.
DR   PaxDb; 449447-MAE_02500; -.
DR   EnsemblBacteria; BAG00072; BAG00072; MAE_02500.
DR   KEGG; mar:MAE_02500; -.
DR   PATRIC; fig|449447.4.peg.231; -.
DR   eggNOG; COG0120; Bacteria.
DR   HOGENOM; CLU_056590_1_1_3; -.
DR   OMA; AACGKKM; -.
DR   BioCyc; MAER449447:MAE_RS01125-MONOMER; -.
DR   UniPathway; UPA00115; UER00412.
DR   Proteomes; UP000001510; 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; 3.40.50.1360: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; rpiA; 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:UP000001510}.
FT   ACT_SITE        111
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00170"
FT   BINDING         32..35
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00170"
FT   BINDING         89..92
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00170"
FT   BINDING         102..105
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00170"
FT   BINDING         129
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00170"
SQ   SEQUENCE   236 AA;  24870 MW;  A372BA205F69EFE1 CRC64;
     MTAIDPVIIM KQEVGKAAAN LVQSNSVVGL GTGSTTAYAI EYLGARLQSG EISNIVGVPT
     SFQAQVLARK YGIPLTTLDV IAKMDIAIDG ADEVDPQKNL IKGGGAAHTQ EKIVDSLADI
     FVVVVDGNKL VDKLGSTFLL PVEVLPMAMT PVMRKLEALG GKPSLRMGVK KAGPVVTDQG
     NLVIDVKFDS IDDPADLERT INNMPGVLEN GLFVGVADLI LVGEIIDGKP VVREIR
//