ALSE_ECOLI
ID ALSE_ECOLI Reviewed; 231 AA.
AC P32719; Q2M6L8;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=D-allulose-6-phosphate 3-epimerase {ECO:0000255|HAMAP-Rule:MF_02226};
DE EC=5.1.3.- {ECO:0000255|HAMAP-Rule:MF_02226, ECO:0000269|PubMed:18700786};
GN Name=alsE {ECO:0000255|HAMAP-Rule:MF_02226}; Synonyms=yjcU;
GN OrderedLocusNames=b4085, JW4046;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION.
RC STRAIN=K12;
RX PubMed=9401019; DOI=10.1128/jb.179.24.7631-7637.1997;
RA Kim C., Song S., Park C.;
RT "The D-allose operon of Escherichia coli K-12.";
RL J. Bacteriol. 179:7631-7637(1997).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS AND
RP D-GLUCITOL-6-PHOSPHATE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT,
RP MUTAGENESIS OF THR-196; SER-197 AND GLY-198, PATHWAY, AND ACTIVE SITE.
RX PubMed=18700786; DOI=10.1021/bi800821v;
RA Chan K.K., Fedorov A.A., Fedorov E.V., Almo S.C., Gerlt J.A.;
RT "Structural basis for substrate specificity in phosphate binding
RT (beta/alpha)8-barrels: D-allulose 6-phosphate 3-epimerase from Escherichia
RT coli K-12.";
RL Biochemistry 47:9608-9617(2008).
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:0000255|HAMAP-Rule:MF_02226,
CC ECO:0000269|PubMed:18700786, ECO:0000269|PubMed:9401019}.
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:0000255|HAMAP-Rule:MF_02226,
CC ECO:0000269|PubMed:18700786};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:18700786};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:18700786};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:18700786};
CC Note=Binds 1 divalent metal cation per subunit. Activity is highest
CC with Co(2+) > Mn(2+) > Zn(2+). {ECO:0000269|PubMed:18700786};
CC -!- PATHWAY: Carbohydrate degradation; D-allose degradation.
CC {ECO:0000255|HAMAP-Rule:MF_02226, ECO:0000269|PubMed:18700786}.
CC -!- SUBUNIT: Homohexamer. Trimer of dimers. {ECO:0000269|PubMed:18700786}.
CC -!- SIMILARITY: Belongs to the ribulose-phosphate 3-epimerase family. AlsE
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_02226, ECO:0000305}.
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DR EMBL; U00006; AAC43179.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77046.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78088.1; -; Genomic_DNA.
DR PIR; D65217; D65217.
DR RefSeq; NP_418509.1; NC_000913.3.
DR RefSeq; WP_001311314.1; NZ_STEB01000014.1.
DR PDB; 3CT7; X-ray; 2.50 A; A/B/C/D/E/F=1-231.
DR PDB; 3CTL; X-ray; 2.20 A; A/B/C/D/E/F=1-231.
DR PDBsum; 3CT7; -.
DR PDBsum; 3CTL; -.
DR AlphaFoldDB; P32719; -.
DR SMR; P32719; -.
DR BioGRID; 4261233; 11.
DR IntAct; P32719; 2.
DR STRING; 511145.b4085; -.
DR PaxDb; P32719; -.
DR PRIDE; P32719; -.
DR EnsemblBacteria; AAC77046; AAC77046; b4085.
DR EnsemblBacteria; BAE78088; BAE78088; BAE78088.
DR GeneID; 948595; -.
DR KEGG; ecj:JW4046; -.
DR KEGG; eco:b4085; -.
DR PATRIC; fig|1411691.4.peg.2615; -.
DR EchoBASE; EB1900; -.
DR eggNOG; COG0036; Bacteria.
DR HOGENOM; CLU_054856_2_1_6; -.
DR InParanoid; P32719; -.
DR OMA; CDLILIM; -.
DR PhylomeDB; P32719; -.
DR BioCyc; EcoCyc:EG11957-MON; -.
DR BioCyc; MetaCyc:EG11957-MON; -.
DR SABIO-RK; P32719; -.
DR UniPathway; UPA00361; -.
DR EvolutionaryTrace; P32719; -.
DR PRO; PR:P32719; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0034700; F:allulose 6-phosphate 3-epimerase activity; IDA:EcoCyc.
DR GO; GO:0004750; F:D-ribulose-phosphate 3-epimerase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IDA:UniProtKB.
DR GO; GO:0044262; P:cellular carbohydrate metabolic process; IDA:UniProtKB.
DR GO; GO:0019316; P:D-allose catabolic process; IMP:EcoCyc.
DR GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; IBA:GO_Central.
DR CDD; cd00429; RPE; 1.
DR Gene3D; 3.20.20.70; -; 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; PTHR11749; 1.
DR Pfam; PF00834; Ribul_P_3_epim; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR PROSITE; PS01085; RIBUL_P_3_EPIMER_1; 1.
DR PROSITE; PS01086; RIBUL_P_3_EPIMER_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cobalt; Isomerase; Manganese;
KW Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..231
FT /note="D-allulose-6-phosphate 3-epimerase"
FT /id="PRO_0000171585"
FT ACT_SITE 32
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02226,
FT ECO:0000269|PubMed:18700786, ECO:0007744|PDB:3CTL"
FT ACT_SITE 173
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02226,
FT ECO:0000269|PubMed:18700786, ECO:0007744|PDB:3CTL"
FT BINDING 6
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02226,
FT ECO:0000269|PubMed:18700786, ECO:0007744|PDB:3CTL"
FT BINDING 30
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02226,
FT ECO:0000269|PubMed:18700786, ECO:0007744|PDB:3CT7,
FT ECO:0007744|PDB:3CTL"
FT BINDING 32
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02226,
FT ECO:0000269|PubMed:18700786, ECO:0007744|PDB:3CT7,
FT ECO:0007744|PDB:3CTL"
FT BINDING 63
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02226,
FT ECO:0000269|PubMed:18700786, ECO:0007744|PDB:3CT7,
FT ECO:0007744|PDB:3CTL"
FT BINDING 63
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02226,
FT ECO:0000269|PubMed:18700786, ECO:0007744|PDB:3CTL"
FT BINDING 140..143
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02226,
FT ECO:0000269|PubMed:18700786, ECO:0007744|PDB:3CTL"
FT BINDING 173..175
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02226,
FT ECO:0000269|PubMed:18700786, ECO:0007744|PDB:3CTL"
FT BINDING 173
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02226,
FT ECO:0000269|PubMed:18700786, ECO:0007744|PDB:3CT7,
FT ECO:0007744|PDB:3CTL"
FT BINDING 195..197
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02226,
FT ECO:0000269|PubMed:18700786, ECO:0007744|PDB:3CTL"
FT MUTAGEN 196
FT /note="Missing: Shortens the substrate-binding pocket.
FT Slightly lower activity towards allulose 6-phosphate and
FT increased activity towards ribulose 5-phosphate."
FT /evidence="ECO:0000269|PubMed:18700786"
FT MUTAGEN 197
FT /note="Missing: Shortens the substrate-binding pocket.
FT Slightly lower activity towards allulose 6-phosphate and
FT increased activity towards ribulose 5-phosphate."
FT /evidence="ECO:0000269|PubMed:18700786"
FT MUTAGEN 198
FT /note="Missing: Shortens the substrate-binding pocket.
FT Slightly lower activity towards allulose 6-phosphate and
FT increased activity towards ribulose 5-phosphate."
FT /evidence="ECO:0000269|PubMed:18700786"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:3CTL"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:3CTL"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:3CTL"
FT HELIX 15..23
FT /evidence="ECO:0007829|PDB:3CTL"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:3CTL"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:3CTL"
FT HELIX 46..53
FT /evidence="ECO:0007829|PDB:3CTL"
FT STRAND 60..67
FT /evidence="ECO:0007829|PDB:3CTL"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:3CTL"
FT HELIX 73..79
FT /evidence="ECO:0007829|PDB:3CTL"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:3CTL"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:3CTL"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:3CTL"
FT HELIX 95..104
FT /evidence="ECO:0007829|PDB:3CTL"
FT STRAND 108..113
FT /evidence="ECO:0007829|PDB:3CTL"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:3CTL"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:3CTL"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:3CTL"
FT STRAND 130..137
FT /evidence="ECO:0007829|PDB:3CTL"
FT HELIX 150..164
FT /evidence="ECO:0007829|PDB:3CTL"
FT STRAND 169..174
FT /evidence="ECO:0007829|PDB:3CTL"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:3CTL"
FT HELIX 181..187
FT /evidence="ECO:0007829|PDB:3CTL"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:3CTL"
FT TURN 196..199
FT /evidence="ECO:0007829|PDB:3CTL"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:3CTL"
FT HELIX 206..218
FT /evidence="ECO:0007829|PDB:3CTL"
SQ SEQUENCE 231 AA; 26109 MW; 8FA92458D714D4B0 CRC64;
MKISPSLMCM DLLKFKEQIE FIDSHADYFH IDIMDGHFVP NLTLSPFFVS QVKKLATKPL
DCHLMVTRPQ DYIAQLARAG ADFITLHPET INGQAFRLID EIRRHDMKVG LILNPETPVE
AMKYYIHKAD KITVMTVDPG FAGQPFIPEM LDKLAELKAW REREGLEYEI EVDGSCNQAT
YEKLMAAGAD VFIVGTSGLF NHAENIDEAW RIMTAQILAA KSEVQPHAKT A
