ID A2C1K2_PROM1 Unreviewed; 250 AA.
AC A2C1K2;
DT 20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 20-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=ribulose-phosphate 3-epimerase {ECO:0000256|ARBA:ARBA00013188};
DE EC=5.1.3.1 {ECO:0000256|ARBA:ARBA00013188};
GN Name=rpe {ECO:0000313|EMBL:ABM75362.1};
GN OrderedLocusNames=NATL1_08041 {ECO:0000313|EMBL:ABM75362.1};
OS Prochlorococcus marinus (strain NATL1A).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=167555 {ECO:0000313|EMBL:ABM75362.1, ECO:0000313|Proteomes:UP000002592};
RN [1] {ECO:0000313|Proteomes:UP000002592}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NATL1A {ECO:0000313|Proteomes:UP000002592};
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 -!- CATALYTIC ACTIVITY:
CC Reaction=D-ribulose 5-phosphate = D-xylulose 5-phosphate;
CC Xref=Rhea:RHEA:13677, ChEBI:CHEBI:57737, ChEBI:CHEBI:58121;
CC EC=5.1.3.1; Evidence={ECO:0000256|ARBA:ARBA00001782};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|ARBA:ARBA00001941};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the ribulose-phosphate 3-epimerase family.
CC {ECO:0000256|ARBA:ARBA00009541}.
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DR EMBL; CP000553; ABM75362.1; -; Genomic_DNA.
DR RefSeq; WP_011823511.1; NC_008819.1.
DR AlphaFoldDB; A2C1K2; -.
DR KEGG; pme:NATL1_08041; -.
DR eggNOG; COG0036; Bacteria.
DR HOGENOM; CLU_054856_1_0_3; -.
DR Proteomes; UP000002592; Chromosome.
DR GO; GO:0004750; F:D-ribulose-phosphate 3-epimerase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:InterPro.
DR CDD; cd00429; RPE; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR026019; Ribul_P_3_epim.
DR InterPro; IPR000056; Ribul_P_3_epim-like.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR NCBIfam; TIGR01163; rpe; 1.
DR PANTHER; PTHR11749; RIBULOSE-5-PHOSPHATE-3-EPIMERASE; 1.
DR PANTHER; PTHR11749:SF3; RIBULOSE-PHOSPHATE 3-EPIMERASE; 1.
DR Pfam; PF00834; Ribul_P_3_epim; 1.
DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000313|EMBL:ABM75362.1}.
SQ SEQUENCE 250 AA; 27062 MW; 8EB37BEEED38D7E3 CRC64;
MIQSISSAIF TEHRPVQIIP SVLPADWANM GQCVKDLELA GVDRIQFDVM DGNFVPNLTF
GPEMISACRK YCSVPFETQL MVSQYNCETM LEGYVEASKG ANGEPGVVIA HAEANVHLHR
ILGKIRQLGG SPSVALNPHT PMDMVKDVLD MVDHVLVMTV NPGFGGQAYI PTMLNKITQL
RKTILDNGYN VDIEVDGGIK ADWSLSQCCA AGANCFIAGS GMFAYPTLKE GCDALRKVAN
DAQNGIIVEK
//
