RPIA_GLOC7
ID RPIA_GLOC7 Reviewed; 237 AA.
AC B7KIR2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 62.
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};
GN OrderedLocusNames=PCC7424_1014;
OS Gloeothece citriformis (strain PCC 7424) (Cyanothece sp. (strain PCC
OS 7424)).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC Aphanothecaceae; Gloeothece; Gloeothece citriformis.
OX NCBI_TaxID=65393;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7424;
RX PubMed=21972240; DOI=10.1128/mbio.00214-11;
RA Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H.,
RA Sherman L.A., Pakrasi H.B.;
RT "Novel metabolic attributes of the genus Cyanothece, comprising a group of
RT unicellular nitrogen-fixing Cyanobacteria.";
RL MBio 2:E214-E214(2011).
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; CP001291; ACK69468.1; -; Genomic_DNA.
DR RefSeq; WP_012598415.1; NC_011729.1.
DR AlphaFoldDB; B7KIR2; -.
DR SMR; B7KIR2; -.
DR STRING; 65393.PCC7424_1014; -.
DR EnsemblBacteria; ACK69468; ACK69468; PCC7424_1014.
DR KEGG; cyc:PCC7424_1014; -.
DR eggNOG; COG0120; Bacteria.
DR HOGENOM; CLU_056590_1_1_3; -.
DR OMA; YDWDEVN; -.
DR OrthoDB; 1681738at2; -.
DR UniPathway; UPA00115; UER00412.
DR Proteomes; UP000002384; 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; Reference proteome.
FT CHAIN 1..237
FT /note="Ribose-5-phosphate isomerase A"
FT /id="PRO_1000194698"
FT ACT_SITE 112
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT BINDING 33..36
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT BINDING 90..93
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT BINDING 103..106
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
FT BINDING 130
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00170"
SQ SEQUENCE 237 AA; 25090 MW; 4CFFF7FD17527108 CRC64;
MTVTNDPVVL MKQEVGKAAA QRVHSDTIIG LGTGSTTAYA IQYIGERIQT GELKNVVGVP
TSFGAEVLAR KYGVPLTTLD VIDKMDLAID GADEVDPQKN LIKGGGAAHT REKIVDSLAD
VFIVVVDSGK LVDKLGSTFL LPVEVIPMAV TPVIKALEKL GGKTDLRMGV KKAGPVVTDQ
GNLVIDVKFD NIEDPANLEK TINNIPGVLE NGLFVGVADL ILVGEIIDGK PRVREIS
