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Database: UniProt
Entry: U6F2H8_LACHE
LinkDB: U6F2H8_LACHE
Original site: U6F2H8_LACHE 
ID   U6F2H8_LACHE            Unreviewed;       216 AA.
AC   U6F2H8;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=ribulose-phosphate 3-epimerase {ECO:0000256|ARBA:ARBA00013188};
DE            EC=5.1.3.1 {ECO:0000256|ARBA:ARBA00013188};
GN   ORFNames=LHCIRMBIA951_00065 {ECO:0000313|EMBL:CDI58126.1};
OS   Lactobacillus helveticus CIRM-BIA 951.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=1226334 {ECO:0000313|EMBL:CDI58126.1, ECO:0000313|Proteomes:UP000017248};
RN   [1] {ECO:0000313|EMBL:CDI58126.1, ECO:0000313|Proteomes:UP000017248}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIRM-BIA 951 {ECO:0000313|EMBL:CDI58126.1,
RC   ECO:0000313|Proteomes:UP000017248};
RA   Valence F., Chuat V., Ma L., Creno S., Falentin H., Lortal S., Bizet C.,
RA   Clermont D., Loux V., Bouchier C., Cousin S.;
RT   "Draft Genome Sequence of five Lactobacillus helveticus strains CIRM-BIA
RT   101T, 103, 104, 951 and 953 isolated from milk product.";
RL   Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CDI58126.1}.
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DR   EMBL; CBUK010000051; CDI58126.1; -; Genomic_DNA.
DR   RefSeq; WP_012212023.1; NZ_HG530809.1.
DR   AlphaFoldDB; U6F2H8; -.
DR   STRING; 1587.ALV80_04255; -.
DR   HOGENOM; CLU_054856_2_2_9; -.
DR   Proteomes; UP000017248; Unassembled WGS sequence.
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;
KW   Isomerase {ECO:0000313|EMBL:CDI58126.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017248}.
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
//
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