RPIA_PROM1
ID RPIA_PROM1 Reviewed; 236 AA.
AC A2C4N6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=NATL1_18901;
OS Prochlorococcus marinus (strain NATL1A).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=167555;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NATL1A;
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(2007).
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; CP000553; ABM76446.1; -; Genomic_DNA.
DR RefSeq; WP_011824423.1; NC_008819.1.
DR AlphaFoldDB; A2C4N6; -.
DR SMR; A2C4N6; -.
DR STRING; 167555.NATL1_18901; -.
DR EnsemblBacteria; ABM76446; ABM76446; NATL1_18901.
DR KEGG; pme:NATL1_18901; -.
DR eggNOG; COG0120; Bacteria.
DR HOGENOM; CLU_056590_1_1_3; -.
DR OMA; YDWDEVN; -.
DR UniPathway; UPA00115; UER00412.
DR Proteomes; UP000002592; 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 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_1000194714"
FT ACT_SITE 108
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT BINDING 29..32
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT BINDING 86..89
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT BINDING 99..102
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT BINDING 126
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
SQ SEQUENCE 236 AA; 25092 MW; D02934273135A20B CRC64;
MDLQNQMKKA VAQAAVDQIQ NGMILGLGSG STAALMIEAL AIKIKSGEIK DVVGVTTSFQ
GEVLASELGI PLKSLSSVSE IDLAIDGADE VDPKFQLIKG GGACHVQEKL VAALAKKFIV
VVDSTKLVEK LNLDFKLPVE VLPSAWKQVQ KTLINLGGEG NLRMAQKKAG PIVTDQGNLI
LDLTFRNGID QPELLETQIN NIPGVLENGL FVNLTDEVLV GKVESDVVGV ESLKKI
