ID A0A3P1W3W1_9FUSO Unreviewed; 226 AA.
AC A0A3P1W3W1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Putative D-allulose-6-phosphate 3-epimerase {ECO:0000256|HAMAP-Rule:MF_02226};
DE EC=5.1.3.- {ECO:0000256|HAMAP-Rule:MF_02226};
GN ORFNames=EII29_08145 {ECO:0000313|EMBL:RRD39203.1};
OS Leptotrichia sp. OH3620_COT-345.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC Leptotrichia.
OX NCBI_TaxID=2491048 {ECO:0000313|EMBL:RRD39203.1, ECO:0000313|Proteomes:UP000280115};
RN [1] {ECO:0000313|EMBL:RRD39203.1, ECO:0000313|Proteomes:UP000280115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OH3620_COT-345 {ECO:0000313|EMBL:RRD39203.1,
RC ECO:0000313|Proteomes:UP000280115};
RA Coil D.A., Jospin G., Darling A.E., Wallis C., Davis I.J., Harris S.,
RA Eisen J.A., Holcombe L.J., O'Flynn C.;
RT "Genomes From Bacteria Associated with the Canine Oral Cavity: a Test Case
RT for Automated Genome-Based Taxonomic Assignment.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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:RRD39203.1}.
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DR EMBL; RQYW01000012; RRD39203.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P1W3W1; -.
DR OrthoDB; 1645589at2; -.
DR UniPathway; UPA00361; -.
DR Proteomes; UP000280115; Unassembled WGS sequence.
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, ECO:0000313|EMBL:RRD39203.1};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_02226}.
FT ACT_SITE 35
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02226"
FT ACT_SITE 176
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02226"
FT BINDING 33
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02226"
FT BINDING 35
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02226"
FT BINDING 66
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02226"
FT BINDING 66
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02226"
FT BINDING 143..146
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02226"
FT BINDING 176..178
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02226"
FT BINDING 176
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02226"
FT BINDING 198..200
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02226"
SQ SEQUENCE 226 AA; 25719 MW; ABA403A785F02C55 CRC64;
MEKVRFSPSL MCMDLTRFKE QVDILNERAD FYHVDIMDGH FVKNITLSPF FVEQLNKISK
LPIDVHLMTE FPGDYIDVLG KVGAAYISPH AETINKDAFR IINKIKNVGC KVGVVLNPAT
PVEWIKYYIH LVDKITVMTV DPGFAGQPFI PEMLEKIKEL KTLKEENGYS YIIEIDGSCN
EKTFRKLVKA GGEVFIVGSS GLFNLDNSLT DAWDKMIEIF NRETSE
//
