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Database: UniProt
Entry: Q1AY26_RUBXD
LinkDB: Q1AY26_RUBXD
Original site: Q1AY26_RUBXD 
ID   Q1AY26_RUBXD            Unreviewed;       231 AA.
AC   Q1AY26;
DT   11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2006, sequence version 1.
DT   27-MAR-2024, 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   OrderedLocusNames=Rxyl_0733 {ECO:0000313|EMBL:ABG03702.1};
OS   Rubrobacter xylanophilus (strain DSM 9941 / NBRC 16129 / PRD-1).
OC   Bacteria; Actinomycetota; Rubrobacteria; Rubrobacterales; Rubrobacteraceae;
OC   Rubrobacter.
OX   NCBI_TaxID=266117 {ECO:0000313|EMBL:ABG03702.1, ECO:0000313|Proteomes:UP000006637};
RN   [1] {ECO:0000313|EMBL:ABG03702.1, ECO:0000313|Proteomes:UP000006637}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9941 / NBRC 16129 / PRD-1
RC   {ECO:0000313|Proteomes:UP000006637};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., da Costa M.S.,
RA   Rainey F.A., Empadinhas N., Jolivet E., Battista J.R., Richardson P.;
RT   "Complete sequence of Rubrobacter xylanophilus DSM 9941.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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|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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00170}.
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DR   EMBL; CP000386; ABG03702.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1AY26; -.
DR   STRING; 266117.Rxyl_0733; -.
DR   KEGG; rxy:Rxyl_0733; -.
DR   eggNOG; COG0120; Bacteria.
DR   HOGENOM; CLU_056590_1_0_11; -.
DR   PhylomeDB; Q1AY26; -.
DR   UniPathway; UPA00115; UER00412.
DR   Proteomes; UP000006637; 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   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; TIGR00021; rpiA; 1.
DR   PANTHER; PTHR43748; RIBOSE-5-PHOSPHATE ISOMERASE 3, CHLOROPLASTIC-RELATED; 1.
DR   PANTHER; PTHR43748:SF3; RIBOSE-5-PHOSPHATE ISOMERASE 3, CHLOROPLASTIC-RELATED; 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:UP000006637}.
FT   ACT_SITE        110
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         88..91
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00170"
FT   BINDING         101..104
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00170"
SQ   SEQUENCE   231 AA;  24192 MW;  288B312F8468536A CRC64;
     MSPDGMERLK RAAAREAVDR YVESGMVVGL GTGTTASWAV RRIGERLLEG SLSGVRGVPT
     SEYTAALARE CGVPLVSLSE RRPELTIDGA DEIAPDLSVI KGRGGALLRE KIVAAASRRG
     VVIVADGSKQ VSLLGNGPLP VEVEPFGWEA TAEALAALGC EPELRRVKTQ PFVTDGGHYT
     LDCRFPGIPD PPGLACKIKR VPGALECGLF VGLARAAVIA RPEGVEVLEA A
//
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