ID A8YVV7_LACH4 Unreviewed; 216 AA.
AC A8YVV7;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=ribulose-phosphate 3-epimerase {ECO:0000256|ARBA:ARBA00013188};
DE EC=5.1.3.1 {ECO:0000256|ARBA:ARBA00013188};
GN OrderedLocusNames=lhv_1400 {ECO:0000313|EMBL:ABX27387.1};
OS Lactobacillus helveticus (strain DPC 4571).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=405566 {ECO:0000313|EMBL:ABX27387.1, ECO:0000313|Proteomes:UP000000790};
RN [1] {ECO:0000313|EMBL:ABX27387.1, ECO:0000313|Proteomes:UP000000790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DPC 4571 {ECO:0000313|EMBL:ABX27387.1,
RC ECO:0000313|Proteomes:UP000000790};
RX PubMed=17993529; DOI=10.1128/JB.01295-07;
RA Callanan M., Kaleta P., O'Callaghan J., O'Sullivan O., Jordan K.,
RA McAuliffe O., Sangrador-Vegas A., Slattery L., Fitzgerald G.F.,
RA Beresford T., Ross R.P.;
RT "Genome sequence of Lactobacillus helveticus: an organism distinguished by
RT selective gene loss and IS element expansion.";
RL J. Bacteriol. 190:727-735(2008).
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; CP000517; ABX27387.1; -; Genomic_DNA.
DR RefSeq; WP_012212023.1; NC_010080.1.
DR AlphaFoldDB; A8YVV7; -.
DR KEGG; lhe:lhv_1400; -.
DR eggNOG; COG0036; Bacteria.
DR HOGENOM; CLU_054856_2_2_9; -.
DR Proteomes; UP000000790; 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.
DR PROSITE; PS01085; RIBUL_P_3_EPIMER_1; 1.
DR PROSITE; PS01086; RIBUL_P_3_EPIMER_2; 1.
PE 3: Inferred from homology;
SQ SEQUENCE 216 AA; 23829 MW; B9B36FC73594CADE CRC64;
MIIAPSILNA DNLNLKENIK EAVAVGIDRF HIDIMDGHFV PNLSFGPQLI SDFKREFPMI
DAEIHFMSNN PDDLIPAFVA AGADIMELHY GAMSESKLNY WLDYLASNGV EAVLAIKPDV
QADVIEKFLP KIKQVLVMTV NPGFGGQSFI ADSAEKIKQV REIVGPNMPI EVDGGINERT
IKIAKDAGAD VFVVGSYLYK NGNITNQVRK LEKIIK
//
