RPIA_PLAF7
ID RPIA_PLAF7 Reviewed; 236 AA.
AC Q8I3W2;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Ribose-5-phosphate isomerase;
DE EC=5.3.1.6 {ECO:0000250|UniProtKB:P0A7Z0};
GN ORFNames=PF3D7_0514600 {ECO:0000312|EMBL:CAD51510.1};
OS Plasmodium falciparum (isolate 3D7).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=36329 {ECO:0000312|Proteomes:UP000001450};
RN [1] {ECO:0000312|Proteomes:UP000001450}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7 {ECO:0000312|Proteomes:UP000001450};
RX PubMed=12368864; DOI=10.1038/nature01097;
RA Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.D.,
RA Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A., Kyes S., Chan M.-S.,
RA Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M.,
RA Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.A.,
RA Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I.,
RA Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J.,
RA Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.G.;
RT "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL Nature 419:498-511(2002).
RN [2] {ECO:0000312|EMBL:CAD51510.1, ECO:0000312|Proteomes:UP000001450}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7 {ECO:0000312|Proteomes:UP000001450};
RX PubMed=12368867; DOI=10.1038/nature01095;
RA Hall N., Pain A., Berriman M., Churcher C.M., Harris B., Harris D.,
RA Mungall K.L., Bowman S., Atkin R., Baker S., Barron A., Brooks K.,
RA Buckee C.O., Burrows C., Cherevach I., Chillingworth C., Chillingworth T.,
RA Christodoulou Z., Clark L., Clark R., Corton C., Cronin A., Davies R.M.,
RA Davis P., Dear P., Dearden F., Doggett J., Feltwell T., Goble A.,
RA Goodhead I., Gwilliam R., Hamlin N., Hance Z., Harper D., Hauser H.,
RA Hornsby T., Holroyd S., Horrocks P., Humphray S., Jagels K., James K.D.,
RA Johnson D., Kerhornou A., Knights A., Konfortov B., Kyes S., Larke N.,
RA Lawson D., Lennard N., Line A., Maddison M., Mclean J., Mooney P.,
RA Moule S., Murphy L., Oliver K., Ormond D., Price C., Quail M.A.,
RA Rabbinowitsch E., Rajandream M.A., Rutter S., Rutherford K.M., Sanders M.,
RA Simmonds M., Seeger K., Sharp S., Smith R., Squares R., Squares S.,
RA Stevens K., Taylor K., Tivey A., Unwin L., Whitehead S., Woodward J.R.,
RA Sulston J.E., Craig A., Newbold C., Barrell B.G.;
RT "Sequence of Plasmodium falciparum chromosomes 1, 3-9 and 13.";
RL Nature 419:527-531(2002).
RN [3] {ECO:0007744|PDB:2F8M}
RP X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) IN COMPLEX WITH PHOSPHATE, AND
RP SUBUNIT.
RX PubMed=16682767; DOI=10.1107/s1744309106010876;
RA Holmes M.A., Buckner F.S., Van Voorhis W.C., Verlinde C.L., Mehlin C.,
RA Boni E., DeTitta G., Luft J., Lauricella A., Anderson L., Kalyuzhniy O.,
RA Zucker F., Schoenfeld L.W., Earnest T.N., Hol W.G., Merritt E.A.;
RT "Structure of ribose 5-phosphate isomerase from Plasmodium falciparum.";
RL Acta Crystallogr. F Struct. Biol. Commun. 62:427-431(2006).
CC -!- FUNCTION: Involved in the first step of the non-oxidative branch of the
CC pentose phosphate pathway. It catalyzes the reversible conversion of
CC ribose-5-phosphate to ribulose 5-phosphate.
CC {ECO:0000250|UniProtKB:P0A7Z0}.
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:0000250|UniProtKB:P0A7Z0};
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:0000250|UniProtKB:P0A7Z0}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16682767}.
CC -!- SIMILARITY: Belongs to the ribose 5-phosphate isomerase family.
CC {ECO:0000305}.
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DR EMBL; AL844504; CAD51510.1; -; Genomic_DNA.
DR RefSeq; XP_001351703.1; XM_001351667.1.
DR PDB; 2F8M; X-ray; 2.09 A; A/B=1-236.
DR PDBsum; 2F8M; -.
DR AlphaFoldDB; Q8I3W2; -.
DR SMR; Q8I3W2; -.
DR STRING; 5833.PFE0730c; -.
DR PRIDE; Q8I3W2; -.
DR EnsemblProtists; CAD51510; CAD51510; PF3D7_0514600.
DR GeneID; 812960; -.
DR KEGG; pfa:PF3D7_0514600; -.
DR VEuPathDB; PlasmoDB:PF3D7_0514600; -.
DR HOGENOM; CLU_056590_1_0_1; -.
DR InParanoid; Q8I3W2; -.
DR OMA; YDWDEVN; -.
DR PhylomeDB; Q8I3W2; -.
DR UniPathway; UPA00115; UER00412.
DR EvolutionaryTrace; Q8I3W2; -.
DR Proteomes; UP000001450; Chromosome 5.
DR GO; GO:0004751; F:ribose-5-phosphate isomerase activity; ISS:GeneDB.
DR GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; ISS:GeneDB.
DR CDD; cd01398; RPI_A; 1.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR InterPro; IPR004788; Ribose5P_isomerase_type_A.
DR Pfam; PF06026; Rib_5-P_isom_A; 1.
DR SUPFAM; SSF100950; SSF100950; 1.
DR TIGRFAMs; TIGR00021; rpiA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Isomerase; Reference proteome.
FT CHAIN 1..236
FT /note="Ribose-5-phosphate isomerase"
FT /id="PRO_0000438883"
FT ACT_SITE 106
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0A7Z0"
FT BINDING 27..30
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A7Z0"
FT BINDING 84..87
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A7Z0"
FT BINDING 97..100
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A7Z0"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A7Z0"
FT HELIX 1..16
FT /evidence="ECO:0007829|PDB:2F8M"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:2F8M"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:2F8M"
FT HELIX 32..43
FT /evidence="ECO:0007829|PDB:2F8M"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:2F8M"
FT HELIX 57..66
FT /evidence="ECO:0007829|PDB:2F8M"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:2F8M"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:2F8M"
FT HELIX 103..111
FT /evidence="ECO:0007829|PDB:2F8M"
FT STRAND 116..121
FT /evidence="ECO:0007829|PDB:2F8M"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:2F8M"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:2F8M"
FT HELIX 145..152
FT /evidence="ECO:0007829|PDB:2F8M"
FT TURN 156..160
FT /evidence="ECO:0007829|PDB:2F8M"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:2F8M"
FT STRAND 180..185
FT /evidence="ECO:0007829|PDB:2F8M"
FT HELIX 193..201
FT /evidence="ECO:0007829|PDB:2F8M"
FT STRAND 206..212
FT /evidence="ECO:0007829|PDB:2F8M"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:2F8M"
FT STRAND 228..232
FT /evidence="ECO:0007829|PDB:2F8M"
SQ SEQUENCE 236 AA; 26205 MW; E7C5F8F9C5C38213 CRC64;
MDSLKKIVAY KAVDEYVQSN MTIGLGTGST VFYVLERIDN LLKSGKLKDV VCIPTSIDTE
LKARKLGIPL TTLEKHSNID ITIDGTDEID LNLNLIKGRG GALVREKLVA SSSSLFIIIG
DESKLCTNGL GMTGAVPIEI LTFGYEKIIE NLLKIYTLKG CTYKIRKRNG EIFITDNKNY
IVDFFFTEPI QDLLETCTRI KMTTGVVDHG IFVNMTNVAL ISKHDGTVLT LNKKYE
