ID E6QMR8_9ZZZZ Unreviewed; 222 AA.
AC E6QMR8;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, 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 Name=rpe {ECO:0000313|EMBL:CBI08539.1};
GN ORFNames=CARN6_2016 {ECO:0000313|EMBL:CBI08539.1};
OS mine drainage metagenome.
OC unclassified sequences; metagenomes; ecological metagenomes.
OX NCBI_TaxID=410659 {ECO:0000313|EMBL:CBI08539.1};
RN [1] {ECO:0000313|EMBL:CBI08539.1}
RP NUCLEOTIDE SEQUENCE.
RA Bertin P.N., Heinrich-Salmeron A., Pelletier E., Goulhen-Chollet F.,
RA Arsene-Ploetze F., Gallien S., Calteau A., Vallenet D., Casiot C.,
RA Chane-Woon-Ming B., Giloteaux L., Barakat M., Bonnefoy V., Bruneel O.,
RA Chandler M., Cleiss J., Duran R., Elbaz-Poulichet F., Fonknechten N.,
RA Lauga B., Mornico D., Ortet P., Schaeffer C., Siguier P.,
RA Alexander Thil Smith A., Van Dorsselaer A., Weissenbach J., Medigue C.,
RA Le Paslier D.;
RT "Diversity of trophic interactions inside an arsenic-rich microbial
RT ecosystem.";
RL Submitted (OCT-2009) 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:CBI08539.1}.
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DR EMBL; CABQ01000236; CBI08539.1; -; Genomic_DNA.
DR AlphaFoldDB; E6QMR8; -.
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 PIRSF; PIRSF001461; RPE; 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:CBI08539.1}.
SQ SEQUENCE 222 AA; 23771 MW; 111697082957DAF9 CRC64;
MVELLPSILS ADFANLARDV AAAERGGGTV IHVDVMDGHF VPNITLGPPV VSSLRKATRL
PLDCHLMIEN PDEFIPAFAD AGANWVSVHY EACRHLHRTL ELIADHGMEP AVVLNPATRA
DLILDILPML HHVLIMTVNP GFGGQKFIPF TLEKVRFLAR IRQERGLTFR IEVDGGVAHD
TIAAVVQAGA DLLVAGNAVF GSGDAAQNAA SLLEAARRAA VE
//
