ID U3U2A6_9ENTR Unreviewed; 226 AA.
AC U3U2A6;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=D-allulose-6-phosphate 3-epimerase {ECO:0000256|HAMAP-Rule:MF_02226};
DE EC=5.1.3.- {ECO:0000256|HAMAP-Rule:MF_02226};
GN Name=alsE {ECO:0000256|HAMAP-Rule:MF_02226};
GN ORFNames=E05_27610 {ECO:0000313|EMBL:BAN97527.1};
OS Plautia stali symbiont.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae.
OX NCBI_TaxID=891974 {ECO:0000313|EMBL:BAN97527.1, ECO:0000313|Proteomes:UP000016901};
RN [1] {ECO:0000313|EMBL:BAN97527.1, ECO:0000313|Proteomes:UP000016901}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21470838; DOI=10.1016/j.micres.2011.03.001;
RA Kobayashi H., Kawasaki K., Takeishi K., Noda H.;
RT "Symbiont of the stink bug Plautia stali synthesizes rough-type
RT lipopolysaccharide.";
RL Microbiol. Res. 167:48-54(2011).
CC -!- FUNCTION: Catalyzes the reversible epimerization of D-allulose 6-
CC phosphate to D-fructose 6-phosphate. Can also catalyze with lower
CC efficiency the reversible epimerization of D-ribulose 5-phosphate to D-
CC xylulose 5-phosphate. {ECO:0000256|HAMAP-Rule:MF_02226}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-allulose 6-phosphate = keto-D-fructose 6-phosphate;
CC Xref=Rhea:RHEA:28426, ChEBI:CHEBI:57579, ChEBI:CHEBI:61519;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02226};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02226};
CC -!- PATHWAY: Carbohydrate degradation; D-allose degradation.
CC {ECO:0000256|HAMAP-Rule:MF_02226}.
CC -!- SIMILARITY: Belongs to the ribulose-phosphate 3-epimerase family. AlsE
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_02226}.
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DR EMBL; AP012551; BAN97527.1; -; Genomic_DNA.
DR AlphaFoldDB; U3U2A6; -.
DR KEGG; psts:E05_27610; -.
DR eggNOG; COG0036; Bacteria.
DR HOGENOM; CLU_054856_2_1_6; -.
DR UniPathway; UPA00361; -.
DR Proteomes; UP000016901; Chromosome.
DR GO; GO:0034700; F:allulose 6-phosphate 3-epimerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019316; P:D-allose catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd00429; RPE; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR HAMAP; MF_02226; AlluloseP_3_epimer; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR043677; AlluloseP_3_epimer_AlsE.
DR InterPro; IPR000056; Ribul_P_3_epim-like.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
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; PS01086; RIBUL_P_3_EPIMER_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_02226};
KW Isomerase {ECO:0000256|HAMAP-Rule:MF_02226};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_02226};
KW Reference proteome {ECO:0000313|Proteomes:UP000016901}.
FT ACT_SITE 34
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02226"
FT ACT_SITE 175
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02226"
FT BINDING 32
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02226"
FT BINDING 34
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02226"
FT BINDING 65
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02226"
FT BINDING 65
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02226"
FT BINDING 142..145
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02226"
FT BINDING 175..177
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02226"
FT BINDING 175
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02226"
FT BINDING 197..199
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02226"
SQ SEQUENCE 226 AA; 25246 MW; 361D5303BFF04D9E CRC64;
MNARFSPSLM CMDLTRFREQ IEAMNASASF YHVDIMDGSY VKNITLSPFF IENLRKITDV
PIDLHLMVNH PEDIIPMCID AGADIISFHP ETANNKNFRL LTQIKEAGRR CGVVLNPATP
ADSIREYAHL LDKVTVMSVD PGFAGQTFIP ETLNKIRQLI AMRESHGYHY LTEIDGSCNA
RTFKQIAASG VDVFIVGTSG LFNLDDDVAQ AWQKMEQIFA QETAAA
//
