ID Q7XYJ3_BIGNA Unreviewed; 321 AA.
AC Q7XYJ3;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=ribulose-phosphate 3-epimerase {ECO:0000256|ARBA:ARBA00013188};
DE EC=5.1.3.1 {ECO:0000256|ARBA:ARBA00013188};
DE Flags: Fragment;
OS Bigelowiella natans (Pedinomonas minutissima) (Chlorarachnion sp. (strain
OS CCMP621)).
OC Eukaryota; Sar; Rhizaria; Cercozoa; Chlorarachniophyceae; Bigelowiella.
OX NCBI_TaxID=227086 {ECO:0000313|EMBL:AAP79201.1};
RN [1] {ECO:0000313|EMBL:AAP79201.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP 621 {ECO:0000313|EMBL:AAP79201.1};
RX PubMed=12777624; DOI=10.1073/pnas.1230951100;
RA Archibald J.M., Rogers M.B., Toop M., Ishida K., Keeling P.J.;
RT "Lateral gene transfer and the evolution of plastid-targeted proteins in
RT the secondary plastid-containing alga Bigelowiella natans.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7678-7683(2003).
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; AY267687; AAP79201.1; -; mRNA.
DR AlphaFoldDB; Q7XYJ3; -.
DR HOGENOM; CLU_054856_1_0_1; -.
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 HAMAP; MF_02227; RPE; 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.
DR PROSITE; PS01085; RIBUL_P_3_EPIMER_1; 1.
PE 2: Evidence at transcript level;
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..321
FT /note="ribulose-phosphate 3-epimerase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004294083"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAP79201.1"
SQ SEQUENCE 321 AA; 34469 MW; ADEA3B81A4A8F9B2 CRC64;
ALTRPLYASL AVSAVLLTAL VALRSRTNNV ALGIRTRAAA SSLVSPALAR VQARQFIKQS
IPPSFQCPRG ATRPLRSYAE LQQIANEAHE GNKMLIAPSI LSANFAKLGE DVDRVLADGA
DVVHFDVMDN HYVPNLTIGP MVCKALRDHG VTAPIDVHLM VSPVDRIIPD FIAAGASYIT
FHPEASLHVD RSLQMIKDAG LKCGLVFNPA TPLDILEYVI DKVDIVLLMS VNPGFGGQKF
IPNTLEKAKK ARALIDAEMA RSGRKIRLEI DGGVSPANIK EVAAAGVDMF VAGSAIFNTP
DYKETIDTMR AELAQVEPVS A
//
