ID   RPIA_KORCO              Reviewed;         225 AA.
AC   B1L7D5;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 64.
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=Kcr_0002;
OS   Korarchaeum cryptofilum (strain OPF8).
OC   Archaea; Candidatus Korarchaeota; Candidatus Korarchaeum.
OX   NCBI_TaxID=374847;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OPF8;
RX   PubMed=18535141; DOI=10.1073/pnas.0801980105;
RA   Elkins J.G., Podar M., Graham D.E., Makarova K.S., Wolf Y., Randau L.,
RA   Hedlund B.P., Brochier-Armanet C., Kunin V., Anderson I., Lapidus A.,
RA   Goltsman E., Barry K., Koonin E.V., Hugenholtz P., Kyrpides N., Wanner G.,
RA   Richardson P., Keller M., Stetter K.O.;
RT   "A korarchaeal genome reveals new insights into the evolution of the
RT   Archaea.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:8102-8107(2008).
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; CP000968; ACB06762.1; -; Genomic_DNA.
DR   RefSeq; WP_012308659.1; NC_010482.1.
DR   AlphaFoldDB; B1L7D5; -.
DR   SMR; B1L7D5; -.
DR   STRING; 374847.Kcr_0002; -.
DR   EnsemblBacteria; ACB06762; ACB06762; Kcr_0002.
DR   GeneID; 6093308; -.
DR   KEGG; kcr:Kcr_0002; -.
DR   eggNOG; arCOG01122; Archaea.
DR   HOGENOM; CLU_056590_1_0_2; -.
DR   InParanoid; B1L7D5; -.
DR   OMA; YDWDEVN; -.
DR   OrthoDB; 98657at2157; -.
DR   PhylomeDB; B1L7D5; -.
DR   UniPathway; UPA00115; UER00412.
DR   Proteomes; UP000001686; 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   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..225
FT                   /note="Ribose-5-phosphate isomerase A"
FT                   /id="PRO_1000097670"
FT   ACT_SITE        102
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT   BINDING         27..30
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT   BINDING         80..83
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT   BINDING         93..96
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT   BINDING         120
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
SQ   SEQUENCE   225 AA;  24338 MW;  4636B2799ADB26AC CRC64;
     MIEFEKRLVA REALKLIGDV KLLGLGSGST VAIFVEELAK SDKAGKIKVI PSSKQIEEVA
     RNQGLEVIYP DGERPEITVD GADEIDSNLN LLKGGGGALL REKVLAYNSS TYVIIADHTK
     LVEKLCSKRA LPVEVLPYGV SWTLGNLIKR FNCDARIRIK DLSPFITDNG NVIVDINCPP
     LEDPASMESE VKGVPGVVEV GIFVGLADLV LIARGSEVKV LRQGF