ID M0EBB7_9EURY Unreviewed; 244 AA. AC M0EBB7; DT 03-APR-2013, integrated into UniProtKB/TrEMBL. DT 03-APR-2013, sequence version 1. DT 27-SEP-2017, entry version 25. 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; Halobacteria; Haloferacales; Halorubraceae; OC Halorubrum. 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; RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., RA Wu D., Madern D., Eisen J.A., Darling A.E., Facciotti M.T.; RT "Phylogenetically driven sequencing of extremely halophilic archaea RT reveals strategies for static and dynamic osmo-response."; RL PLoS Genet. 10:E1004784-E1004784(2014). CC -!- FUNCTION: Catalyzes the reversible conversion of ribose-5- CC phosphate to ribulose 5-phosphate. {ECO:0000256|HAMAP- CC Rule:MF_00170}. CC -!- CATALYTIC ACTIVITY: D-ribose 5-phosphate = D-ribulose 5-phosphate. CC {ECO:0000256|HAMAP-Rule:MF_00170}. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribose 5-phosphate from D-ribulose 5-phosphate (non-oxidative CC stage): step 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 CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 EnsemblBacteria; ELZ45081; ELZ45081; C465_15712. DR PATRIC; fig|1227467.4.peg.3090; -. DR OrthoDB; POG093Z0F8P; -. DR UniPathway; UPA00115; UER00412. DR Proteomes; UP000011526; Unassembled WGS sequence. 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; IPR004788; Ribose5P_isomerase_typA. DR InterPro; IPR020672; Ribose5P_isomerase_typA_subgr. DR Pfam; PF06026; Rib_5-P_isom_A; 1. DR TIGRFAMs; TIGR00021; rpiA; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000011526}; KW Isomerase {ECO:0000256|HAMAP-Rule:MF_00170, KW ECO:0000313|EMBL:ELZ45081.1}. FT REGION 32 35 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00170}. FT REGION 92 95 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00170}. FT REGION 115 118 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00170}. FT ACT_SITE 124 124 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_00170}. FT BINDING 142 142 Substrate. {ECO:0000256|HAMAP-Rule: FT 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 //