RPIA_POLNS
ID RPIA_POLNS Reviewed; 236 AA.
AC B1XU95;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 67.
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=Pnec_0686;
OS Polynucleobacter necessarius subsp. necessarius (strain STIR1).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Polynucleobacter.
OX NCBI_TaxID=452638;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=STIR1;
RX PubMed=24167248; DOI=10.1073/pnas.1316687110;
RA Boscaro V., Felletti M., Vannini C., Ackerman M.S., Chain P.S.,
RA Malfatti S., Vergez L.M., Shin M., Doak T.G., Lynch M., Petroni G.;
RT "Polynucleobacter necessarius, a model for genome reduction in both free-
RT living and symbiotic bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:18590-18595(2013).
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; CP001010; ACB43922.1; -; Genomic_DNA.
DR RefSeq; WP_012357689.1; NC_010531.1.
DR AlphaFoldDB; B1XU95; -.
DR SMR; B1XU95; -.
DR STRING; 452638.Pnec_0686; -.
DR EnsemblBacteria; ACB43922; ACB43922; Pnec_0686.
DR KEGG; pne:Pnec_0686; -.
DR eggNOG; COG0120; Bacteria.
DR HOGENOM; CLU_056590_1_1_4; -.
DR OMA; YDWDEVN; -.
DR OrthoDB; 1681738at2; -.
DR UniPathway; UPA00115; UER00412.
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 PANTHER; PTHR11934; PTHR11934; 1.
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.
FT CHAIN 1..236
FT /note="Ribose-5-phosphate isomerase A"
FT /id="PRO_1000097680"
FT ACT_SITE 106
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT BINDING 31..34
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT BINDING 84..87
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT BINDING 97..100
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
SQ SEQUENCE 236 AA; 24940 MW; FE179A7FF3197449 CRC64;
MNQDQLKQMV GEAARDEVLK LPAGQVLGVG TGSTANYFID ALALHKGHFA GTVSSSNATT
ERLLKHGFKV LDPNDVQGLP AYVDGADEID PAGHMIKGGG GVLTGEKIIA SMAKQFICIC
DSSKQVPVLG NFALPVEIIP LSQGVVSREL EKFGGRVTLR LAKHTRADLN QTPSEPFVTD
NGGWILDVAG LRIASPAQME AQINQIAGVI TVGLFAKEKA NILLVSNAAG VERIQF
