ID M0EBB7_9EURY Unreviewed; 244 AA. AC M0EBB7; DT 03-APR-2013, integrated into UniProtKB/TrEMBL. DT 03-APR-2013, sequence version 1. DT 29-MAY-2024, entry version 49. 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 ORFNames=C465_15712 {ECO:0000313|EMBL:ELZ45081.1}; OS Halorubrum distributum JCM 9100. OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales; OC Halorubraceae; Halorubrum; Halorubrum distributum group. OX NCBI_TaxID=1227467 {ECO:0000313|EMBL:ELZ45081.1, ECO:0000313|Proteomes:UP000011526}; RN [1] {ECO:0000313|EMBL:ELZ45081.1, ECO:0000313|Proteomes:UP000011526} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 9100 {ECO:0000313|EMBL:ELZ45081.1, RC ECO:0000313|Proteomes:UP000011526}; RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784; RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D., RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.; RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals RT strategies for static and dynamic osmo-response."; RL PLoS Genet. 10:E1004784-E1004784(2014). 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: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:ELZ45081.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AOJM01000081; ELZ45081.1; -; Genomic_DNA. DR RefSeq; WP_004599351.1; NZ_AOJM01000081.1. DR AlphaFoldDB; M0EBB7; -. DR PATRIC; fig|1227467.4.peg.3090; -. DR UniPathway; UPA00115; UER00412. DR Proteomes; UP000011526; Unassembled WGS sequence. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; 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 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; 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}. FT REGION 1..22 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..19 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 124 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 92..95 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00170" FT BINDING 115..118 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00170" FT BINDING 142 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00170" SQ SEQUENCE 244 AA; 24488 MW; 197AA2D8AB8A797A CRC64; MKTSGGSDAM KRRAGESAAE AVTDGDVVGL GTGSTAAHAI RRLGDRVDAG LDIRGVPTSF ASRELAAEEG ILCLDLPEAV GPDGPGIDLA IDGADQVATG SDGADDPVSG GALIKGGGAA HAREKLVDAA ADRFLVVADP SKESPRLDRP VPVEVLPAGR TAVAAAVREA GGEPTLRRAE RKDGPVVTDN GNLVLDCEFG EVADPAALSA TLSSIPGAVE NGLFVGLADE IHVGTESGVR VDEV //