ID A0A0R1V6W8_9LACO Unreviewed; 238 AA.
AC A0A0R1V6W8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=FD50_GL000549 {ECO:0000313|EMBL:KRL98741.1};
OS Liquorilactobacillus satsumensis DSM 16230 = JCM 12392.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Liquorilactobacillus.
OX NCBI_TaxID=1423801 {ECO:0000313|EMBL:KRL98741.1, ECO:0000313|Proteomes:UP000051166};
RN [1] {ECO:0000313|EMBL:KRL98741.1, ECO:0000313|Proteomes:UP000051166}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16230 {ECO:0000313|EMBL:KRL98741.1,
RC ECO:0000313|Proteomes:UP000051166};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:KRL98741.1}.
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DR EMBL; AZFQ01000036; KRL98741.1; -; Genomic_DNA.
DR RefSeq; WP_056960696.1; NZ_AZFQ01000036.1.
DR AlphaFoldDB; A0A0R1V6W8; -.
DR STRING; 1423801.FD50_GL000549; -.
DR PATRIC; fig|1423801.4.peg.558; -.
DR OrthoDB; 1645589at2; -.
DR UniPathway; UPA00361; -.
DR Proteomes; UP000051166; 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};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_02226}.
FT ACT_SITE 36
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02226"
FT ACT_SITE 177
FT /note="Proton donor"
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 36
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02226"
FT BINDING 67
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02226"
FT BINDING 67
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02226"
FT BINDING 144..147
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02226"
FT BINDING 177..179
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02226"
FT BINDING 177
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02226"
SQ SEQUENCE 238 AA; 27135 MW; 3E5D5C167B6A2BEB CRC64;
MTESIQVSPS LMTMDLDHFK EQIKFLNGKV SFYHIDIMDG HFVPNITLSP WFIEQVRKIS
DVPMSAHLMV TNPSFWVQQL IASKCEMICM HAEVINGVAF RLIDQIHEAG LKVGVVLNPE
TSIETLLPYI DLLDKVTVMT VDPGFAGQRF LKICLNKIVE LRRLRENNNY KYSIEIDGST
NLKHWKMLAD VKPDIYIIGR SGLFGLADNI EDCWNQMIKE YEESTGLFFS NSANATNS
//
