ID FUCA_ECOLI Reviewed; 215 AA.
AC P0AB87; P11550; Q2MA34;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 24-JAN-2024, entry version 126.
DE RecName: Full=L-fuculose phosphate aldolase {ECO:0000255|HAMAP-Rule:MF_00987, ECO:0000303|PubMed:13898172};
DE EC=4.1.2.17 {ECO:0000255|HAMAP-Rule:MF_00987, ECO:0000269|PubMed:10821675, ECO:0000269|PubMed:11054289, ECO:0000269|PubMed:13898172, ECO:0000269|Ref.8, ECO:0000269|Ref.9};
DE AltName: Full=D-ribulose-phosphate aldolase {ECO:0000255|HAMAP-Rule:MF_00987, ECO:0000303|PubMed:13898172};
DE AltName: Full=L-fuculose-1-phosphate aldolase {ECO:0000255|HAMAP-Rule:MF_00987, ECO:0000303|PubMed:13898172};
GN Name=fucA {ECO:0000255|HAMAP-Rule:MF_00987, ECO:0000303|PubMed:2664711};
GN Synonyms=fucC, prd; OrderedLocusNames=b2800, JW2771;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2664711; DOI=10.1093/nar/17.12.4883;
RA Lu Z., Lin E.C.C.;
RT "The nucleotide sequence of Escherichia coli genes for L-fucose
RT dissimilation.";
RL Nucleic Acids Res. 17:4883-4884(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2553671; DOI=10.1128/jb.171.11.6097-6105.1989;
RA Chen Y.M., Lu Z., Lin E.C.C.;
RT "Constitutive activation of the fucAO operon and silencing of the
RT divergently transcribed fucPIK operon by an IS5 element in Escherichia coli
RT mutants selected for growth on L-1,2-propanediol.";
RL J. Bacteriol. 171:6097-6105(1989).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 108-215.
RC STRAIN=K12;
RX PubMed=2661535; DOI=10.1128/jb.171.7.3754-3759.1989;
RA Conway T., Ingram L.O.;
RT "Similarity of Escherichia coli propanediol oxidoreductase (fucO product)
RT and an unusual alcohol dehydrogenase from Zymomonas mobilis and
RT Saccharomyces cerevisiae.";
RL J. Bacteriol. 171:3754-3759(1989).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR,
RP PATHWAY, AND SUBSTRATE SPECIFICITY.
RC STRAIN=O111:B4;
RX PubMed=13898172;
RA Ghalambor M.A., Heath E.C.;
RT "The metabolism of L-fucose. II. The enzymatic cleavage of L-fuculose 1-
RT phosphate.";
RL J. Biol. Chem. 237:2427-2433(1962).
RN [7]
RP FUNCTION, AND INDUCTION BY L-FUCOSE.
RC STRAIN=K12;
RX PubMed=4928018; DOI=10.1128/jb.106.1.90-96.1971;
RA LeBlanc D.J., Mortlock R.P.;
RT "Metabolism of D-arabinose: a new pathway in Escherichia coli.";
RL J. Bacteriol. 106:90-96(1971).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RA Fessner W.-D., Sinerius G., Schneider A., Dreyer M., Schulz G.E., Badia J.,
RA Aguilar J.;
RT "Diastereoselective enzymatic aldol additions: L-rhamnulose and L-fuculose
RT 1-phosphate aldolases from E. coli.";
RL Angew. Chem. Int. Ed. 30:555-558(1991).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP REGULATION.
RA Fessner W.-D., Schneider A., Held H., Sinerius G., Walter C., Hixon M.,
RA Schloss J.V.;
RT "The mechanism of class II, metal-dependent aldolases.";
RL Angew. Chem. Int. Ed. 50:2219-2221(1996).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.13 ANGSTROMS), COFACTOR, AND SUBUNIT.
RX PubMed=8515438; DOI=10.1006/jmbi.1993.1307;
RA Dreyer M.K., Schulz G.E.;
RT "The spatial structure of the class II L-fuculose-1-phosphate aldolase from
RT Escherichia coli.";
RL J. Mol. Biol. 231:549-553(1993).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) IN COMPLEX WITH ZINC ION, COFACTOR,
RP AND SUBUNIT.
RX PubMed=15299567; DOI=10.1107/s0907444996009146;
RA Dreyer M.K., Schulz G.E.;
RT "Refined high-resolution structure of the metal-ion dependent L-fuculose-1-
RT phosphate aldolase (class II) from Escherichia coli.";
RL Acta Crystallogr. D 52:1082-1091(1996).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.43 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG AND
RP ZINC ION, COFACTOR, AND SUBUNIT.
RX PubMed=8676381; DOI=10.1006/jmbi.1996.0332;
RA Dreyer M.K., Schulz G.E.;
RT "Catalytic mechanism of the metal-dependent fuculose aldolase from
RT Escherichia coli as derived from the structure.";
RL J. Mol. Biol. 259:458-466(1996).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF WILD TYPE AND MUTANTS IN COMPLEX
RP WITH ZINC ION, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP MUTAGENESIS OF THR-26; GLU-73; TYR-113; PHE-131; PHE-206; 207-LYS--GLU-215;
RP TYR-209 AND 211-LEU--GLU-215, COFACTOR, ACTIVE SITE, REACTION MECHANISM,
RP SUBSTRATE SPECIFICITY, AND SUBUNIT.
RX PubMed=10821675; DOI=10.1021/bi9927686;
RA Joerger A.C., Gosse C., Fessner W.-D., Schulz G.E.;
RT "Catalytic action of fuculose 1-phosphate aldolase (class II) as derived
RT from structure-directed mutagenesis.";
RL Biochemistry 39:6033-6041(2000).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) OF WILD TYPE AND MUTANTS IN COMPLEX
RP WITH SUBSTRATE ANALOG AND ZINC ION, FUNCTION, CATALYTIC ACTIVITY,
RP MUTAGENESIS OF ALA-27; ASN-29; SER-71; GLU-73; TYR-113 AND TYR-209,
RP COFACTOR, REACTION MECHANISM, ACTIVE SITE, AND SUBUNIT.
RX PubMed=11054289; DOI=10.1006/jmbi.2000.4153;
RA Joerger A.C., Mueller-Dieckmann C., Schulz G.E.;
RT "Structures of L-fuculose-1-phosphate aldolase mutants outlining motions
RT during catalysis.";
RL J. Mol. Biol. 303:531-543(2000).
CC -!- FUNCTION: Involved in the degradation of L-fucose and D-arabinose
CC (PubMed:13898172). Catalyzes the reversible cleavage of L-fuculose 1-
CC phosphate (Fuc1P) to yield dihydroxyacetone phosphate (DHAP) and L-
CC lactaldehyde (PubMed:13898172, Ref.8, Ref.9, PubMed:10821675,
CC PubMed:11054289). Also able to catalyze the reversible cleavage of D-
CC ribulose 1-phosphate, but FucA has a higher affinity for L-fuculose 1-
CC phosphate and L-lactaldehyde than for D-ribulose 1-phosphate and
CC glycolaldehyde, respectively (PubMed:4928018). FucA possesses a high
CC specificity for the dihydroxyacetone phosphate (DHAP), but accepts a
CC great variety of different aldehydes and has a strong preference for L-
CC configurated alpha-hydroxy aldehydes (PubMed:13898172, Ref.8,
CC PubMed:10821675). FucA generates a vicinal diol unit having the
CC absolute (3R,4R)-cis configuration (D-erythro) (Ref.8,
CC PubMed:10821675). {ECO:0000269|PubMed:10821675,
CC ECO:0000269|PubMed:11054289, ECO:0000269|PubMed:13898172,
CC ECO:0000269|PubMed:4928018, ECO:0000269|Ref.8, ECO:0000269|Ref.9}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-fuculose 1-phosphate = (S)-lactaldehyde + dihydroxyacetone
CC phosphate; Xref=Rhea:RHEA:12933, ChEBI:CHEBI:18041,
CC ChEBI:CHEBI:57642, ChEBI:CHEBI:57846; EC=4.1.2.17;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00987,
CC ECO:0000269|PubMed:10821675, ECO:0000269|PubMed:11054289,
CC ECO:0000269|PubMed:13898172, ECO:0000269|Ref.8, ECO:0000269|Ref.9};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00987,
CC ECO:0000269|PubMed:10821675, ECO:0000269|PubMed:11054289,
CC ECO:0000269|PubMed:13898172, ECO:0000269|PubMed:15299567,
CC ECO:0000269|PubMed:8515438, ECO:0000269|PubMed:8676381};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00987,
CC ECO:0000269|PubMed:10821675, ECO:0000269|PubMed:11054289,
CC ECO:0000269|PubMed:15299567, ECO:0000269|PubMed:8515438,
CC ECO:0000269|PubMed:8676381};
CC -!- ACTIVITY REGULATION: Inhibited by phosphoglycolohydroxamate (PGH).
CC {ECO:0000269|Ref.9}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.7 mM for L-fuculose 1-phosphate (Fuc1P)
CC {ECO:0000269|PubMed:13898172};
CC KM=1.5 mM for L-fuculose 1-phosphate (Fuc1P) {ECO:0000269|Ref.9};
CC KM=2.2 mM for L-fuculose 1-phosphate (Fuc1P)
CC {ECO:0000269|PubMed:10821675};
CC Note=kcat is 19.3 sec(-1) for L-fuculose 1-phosphate (Fuc1P) as
CC substrate. {ECO:0000269|PubMed:10821675};
CC pH dependence:
CC Optimum pH is 7.2. {ECO:0000269|PubMed:13898172};
CC -!- PATHWAY: Carbohydrate degradation; L-fucose degradation; L-lactaldehyde
CC and glycerone phosphate from L-fucose: step 3/3. {ECO:0000255|HAMAP-
CC Rule:MF_00987, ECO:0000269|PubMed:13898172}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00987,
CC ECO:0000269|PubMed:10821675, ECO:0000269|PubMed:11054289,
CC ECO:0000269|PubMed:15299567, ECO:0000269|PubMed:8515438,
CC ECO:0000269|PubMed:8676381}.
CC -!- INDUCTION: By L-fucose. {ECO:0000269|PubMed:4928018}.
CC -!- MISCELLANEOUS: During catalysis the binding of dihydroxyacetone
CC phosphate (DHAP) frees Glu-73 residue from its interaction with zinc
CC ion (PubMed:10821675, PubMed:11054289). Then Glu-73 residue abstracts a
CC proton from the C3 atom of dihydroxyacetone phosphate (DHAP) (or from
CC the O4 atom of L-fuculose 1-phosphate (Fuc1P) in the backward
CC reaction), and moves to transfer its proton to the aldehyde oxygen atom
CC (or to the C3 atom of dihydroxyacetone phosphate (DHAP))
CC (PubMed:10821675, PubMed:11054289). {ECO:0000269|PubMed:10821675,
CC ECO:0000269|PubMed:11054289}.
CC -!- SIMILARITY: Belongs to the aldolase class II family. AraD/FucA
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00987, ECO:0000305}.
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DR EMBL; M31059; AAA23823.1; -; Genomic_DNA.
DR EMBL; X15025; CAA33125.1; -; Genomic_DNA.
DR EMBL; U29581; AAB40450.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75842.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76872.1; -; Genomic_DNA.
DR EMBL; M27177; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; B33495; ADECFP.
DR RefSeq; NP_417280.1; NC_000913.3.
DR RefSeq; WP_000440781.1; NZ_LN832404.1.
DR PDB; 1DZU; X-ray; 2.09 A; P=1-215.
DR PDB; 1DZV; X-ray; 1.86 A; P=1-215.
DR PDB; 1DZW; X-ray; 2.17 A; P=1-215.
DR PDB; 1DZX; X-ray; 2.18 A; P=1-215.
DR PDB; 1DZY; X-ray; 2.44 A; P=1-213.
DR PDB; 1DZZ; X-ray; 1.92 A; P=1-215.
DR PDB; 1E46; X-ray; 2.55 A; P=1-215.
DR PDB; 1E47; X-ray; 2.15 A; P=1-215.
DR PDB; 1E48; X-ray; 1.97 A; P=1-215.
DR PDB; 1E49; X-ray; 2.53 A; P=1-215.
DR PDB; 1E4A; X-ray; 2.15 A; P=1-215.
DR PDB; 1E4B; X-ray; 1.84 A; P=1-215.
DR PDB; 1E4C; X-ray; 1.66 A; P=1-215.
DR PDB; 1FUA; X-ray; 1.92 A; A=1-215.
DR PDB; 2FUA; X-ray; 2.00 A; A=1-215.
DR PDB; 3FUA; X-ray; 2.67 A; A=1-215.
DR PDB; 4FUA; X-ray; 2.43 A; A=1-215.
DR PDBsum; 1DZU; -.
DR PDBsum; 1DZV; -.
DR PDBsum; 1DZW; -.
DR PDBsum; 1DZX; -.
DR PDBsum; 1DZY; -.
DR PDBsum; 1DZZ; -.
DR PDBsum; 1E46; -.
DR PDBsum; 1E47; -.
DR PDBsum; 1E48; -.
DR PDBsum; 1E49; -.
DR PDBsum; 1E4A; -.
DR PDBsum; 1E4B; -.
DR PDBsum; 1E4C; -.
DR PDBsum; 1FUA; -.
DR PDBsum; 2FUA; -.
DR PDBsum; 3FUA; -.
DR PDBsum; 4FUA; -.
DR AlphaFoldDB; P0AB87; -.
DR SMR; P0AB87; -.
DR BioGRID; 4259224; 20.
DR DIP; DIP-9710N; -.
DR IntAct; P0AB87; 1.
DR STRING; 511145.b2800; -.
DR DrugBank; DB04326; Dihydroxyacetone phosphate.
DR DrugBank; DB03026; Phosphoglycolohydroxamic Acid.
DR jPOST; P0AB87; -.
DR PaxDb; 511145-b2800; -.
DR EnsemblBacteria; AAC75842; AAC75842; b2800.
DR GeneID; 75172884; -.
DR GeneID; 947282; -.
DR KEGG; ecj:JW2771; -.
DR KEGG; eco:b2800; -.
DR PATRIC; fig|1411691.4.peg.3933; -.
DR EchoBASE; EB0344; -.
DR eggNOG; COG0235; Bacteria.
DR HOGENOM; CLU_006033_3_0_6; -.
DR InParanoid; P0AB87; -.
DR OMA; YATFGTH; -.
DR OrthoDB; 5500703at2; -.
DR PhylomeDB; P0AB87; -.
DR BioCyc; EcoCyc:FUCPALDOL-MONOMER; -.
DR BioCyc; MetaCyc:FUCPALDOL-MONOMER; -.
DR BRENDA; 4.1.2.17; 2026.
DR SABIO-RK; P0AB87; -.
DR UniPathway; UPA00563; UER00626.
DR EvolutionaryTrace; P0AB87; -.
DR PRO; PR:P0AB87; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016832; F:aldehyde-lyase activity; IDA:EcoCyc.
DR GO; GO:0008738; F:L-fuculose-phosphate aldolase activity; IDA:EcoCyc.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0019571; P:D-arabinose catabolic process; IMP:EcoCyc.
DR GO; GO:0042355; P:L-fucose catabolic process; IMP:EcoCyc.
DR GO; GO:0019323; P:pentose catabolic process; IBA:GO_Central.
DR CDD; cd00398; Aldolase_II; 1.
DR Gene3D; 3.40.225.10; Class II aldolase/adducin N-terminal domain; 1.
DR HAMAP; MF_00987; FucA; 1.
DR InterPro; IPR001303; Aldolase_II/adducin_N.
DR InterPro; IPR036409; Aldolase_II/adducin_N_sf.
DR InterPro; IPR004782; FucA.
DR NCBIfam; TIGR01086; fucA; 1.
DR PANTHER; PTHR22789:SF0; 3-OXO-TETRONATE 4-PHOSPHATE DECARBOXYLASE-RELATED; 1.
DR PANTHER; PTHR22789; FUCULOSE PHOSPHATE ALDOLASE; 1.
DR Pfam; PF00596; Aldolase_II; 1.
DR SMART; SM01007; Aldolase_II; 1.
DR SUPFAM; SSF53639; AraD/HMP-PK domain-like; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Arabinose catabolism; Carbohydrate metabolism;
KW Fucose metabolism; Lyase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..215
FT /note="L-fuculose phosphate aldolase"
FT /id="PRO_0000162925"
FT ACT_SITE 73
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000269|PubMed:10821675,
FT ECO:0000269|PubMed:11054289"
FT BINDING 28..29
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11054289,
FT ECO:0000269|PubMed:8676381, ECO:0007744|PDB:1E47,
FT ECO:0007744|PDB:1E48, ECO:0007744|PDB:4FUA"
FT BINDING 43..44
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11054289,
FT ECO:0000269|PubMed:8676381, ECO:0007744|PDB:1E47,
FT ECO:0007744|PDB:1E48, ECO:0007744|PDB:4FUA"
FT BINDING 71..72
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11054289,
FT ECO:0000269|PubMed:8676381, ECO:0007744|PDB:1E47,
FT ECO:0007744|PDB:1E48, ECO:0007744|PDB:4FUA"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00987,
FT ECO:0000269|PubMed:10821675, ECO:0000269|PubMed:11054289,
FT ECO:0000269|PubMed:15299567, ECO:0000269|PubMed:8676381,
FT ECO:0007744|PDB:1DZU, ECO:0007744|PDB:1DZV,
FT ECO:0007744|PDB:1DZW, ECO:0007744|PDB:1DZX,
FT ECO:0007744|PDB:1DZY, ECO:0007744|PDB:1DZZ,
FT ECO:0007744|PDB:1E48, ECO:0007744|PDB:1E49,
FT ECO:0007744|PDB:1E4A, ECO:0007744|PDB:1E4B,
FT ECO:0007744|PDB:1E4C, ECO:0007744|PDB:1FUA,
FT ECO:0007744|PDB:2FUA, ECO:0007744|PDB:3FUA,
FT ECO:0007744|PDB:4FUA"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00987,
FT ECO:0000269|PubMed:10821675, ECO:0000269|PubMed:11054289,
FT ECO:0000269|PubMed:15299567, ECO:0000269|PubMed:8676381,
FT ECO:0007744|PDB:1DZU, ECO:0007744|PDB:1DZV,
FT ECO:0007744|PDB:1DZW, ECO:0007744|PDB:1DZX,
FT ECO:0007744|PDB:1DZY, ECO:0007744|PDB:1DZZ,
FT ECO:0007744|PDB:1E46, ECO:0007744|PDB:1E47,
FT ECO:0007744|PDB:1E48, ECO:0007744|PDB:1E49,
FT ECO:0007744|PDB:1E4A, ECO:0007744|PDB:1E4B,
FT ECO:0007744|PDB:1E4C, ECO:0007744|PDB:1FUA,
FT ECO:0007744|PDB:2FUA, ECO:0007744|PDB:3FUA,
FT ECO:0007744|PDB:4FUA"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00987,
FT ECO:0000269|PubMed:10821675, ECO:0000269|PubMed:11054289,
FT ECO:0000269|PubMed:15299567, ECO:0000269|PubMed:8676381,
FT ECO:0007744|PDB:1DZU, ECO:0007744|PDB:1DZV,
FT ECO:0007744|PDB:1DZW, ECO:0007744|PDB:1DZX,
FT ECO:0007744|PDB:1DZY, ECO:0007744|PDB:1DZZ,
FT ECO:0007744|PDB:1E46, ECO:0007744|PDB:1E47,
FT ECO:0007744|PDB:1E48, ECO:0007744|PDB:1E49,
FT ECO:0007744|PDB:1E4A, ECO:0007744|PDB:1E4B,
FT ECO:0007744|PDB:1E4C, ECO:0007744|PDB:1FUA,
FT ECO:0007744|PDB:2FUA, ECO:0007744|PDB:3FUA,
FT ECO:0007744|PDB:4FUA"
FT BINDING 155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00987,
FT ECO:0000269|PubMed:10821675, ECO:0000269|PubMed:11054289,
FT ECO:0000269|PubMed:15299567, ECO:0000269|PubMed:8676381,
FT ECO:0007744|PDB:1DZU, ECO:0007744|PDB:1DZV,
FT ECO:0007744|PDB:1DZW, ECO:0007744|PDB:1DZX,
FT ECO:0007744|PDB:1DZY, ECO:0007744|PDB:1DZZ,
FT ECO:0007744|PDB:1E46, ECO:0007744|PDB:1E47,
FT ECO:0007744|PDB:1E48, ECO:0007744|PDB:1E49,
FT ECO:0007744|PDB:1E4A, ECO:0007744|PDB:1E4B,
FT ECO:0007744|PDB:1E4C, ECO:0007744|PDB:1FUA,
FT ECO:0007744|PDB:2FUA, ECO:0007744|PDB:3FUA,
FT ECO:0007744|PDB:4FUA"
FT SITE 113
FT /note="Plays a key role in the stabilization of the
FT transition state and positioning the aldehyde component"
FT /evidence="ECO:0000269|PubMed:10821675"
FT SITE 131
FT /note="Plays a key role in the stabilization of the
FT transition state and positioning the aldehyde component"
FT /evidence="ECO:0000269|PubMed:10821675"
FT SITE 209
FT /note="Plays a key role in the stabilization of the
FT transition state and positioning the aldehyde component"
FT /evidence="ECO:0000269|PubMed:10821675"
FT MUTAGEN 26
FT /note="T->A: Decrease of the aldolase activity mostly due
FT to a decrease of the affinity for L-fuculose 1-phosphate
FT (Fuc1P)."
FT /evidence="ECO:0000269|PubMed:10821675"
FT MUTAGEN 27
FT /note="Missing: Strong decrease of the aldolase activity."
FT /evidence="ECO:0000269|PubMed:11054289"
FT MUTAGEN 29
FT /note="N->L: Loss of aldolase activity; when associated
FT with A-71."
FT /evidence="ECO:0000269|PubMed:11054289"
FT MUTAGEN 29
FT /note="N->Q: Strong decrease of the aldolase activity
FT mostly due to a decrease of the affinity for L-fuculose 1-
FT phosphate (Fuc1P)."
FT /evidence="ECO:0000269|PubMed:11054289"
FT MUTAGEN 71
FT /note="S->A: Loss of aldolase activity; when associated
FT with L-29."
FT /evidence="ECO:0000269|PubMed:11054289"
FT MUTAGEN 71
FT /note="S->Q: Loss of aldolase activity."
FT /evidence="ECO:0000269|PubMed:11054289"
FT MUTAGEN 73
FT /note="E->Q: Loss of aldolase activity; when associated
FT with F-113 and F-209."
FT /evidence="ECO:0000269|PubMed:11054289"
FT MUTAGEN 73
FT /note="E->S: Loss of aldolase activity."
FT /evidence="ECO:0000269|PubMed:10821675,
FT ECO:0000269|PubMed:11054289"
FT MUTAGEN 113
FT /note="Y->F: Slowly inactivated. Has a preference for the
FT D-aldehyde and shows an inversion of the
FT diastereoselectivity. Loss of aldolase activity; when
FT associated with Q-73 and F-209."
FT /evidence="ECO:0000269|PubMed:10821675,
FT ECO:0000269|PubMed:11054289"
FT MUTAGEN 131
FT /note="F->A: Has a slight preference for the D-aldehyde and
FT shows an inversion of the diastereoselectivity. Loss of
FT aldolase activity; when associated with W-206."
FT /evidence="ECO:0000269|PubMed:10821675"
FT MUTAGEN 206
FT /note="F->W: Decrease of aldolase activity mostly due to a
FT decrease of the affinity for L-fuculose 1-phosphate
FT (Fuc1P). Loss of aldolase activity; when associated with A-
FT 131."
FT /evidence="ECO:0000269|PubMed:10821675"
FT MUTAGEN 207..215
FT /note="Missing: Loss of aldolase activity. Has a slight
FT preference for the D-aldehyde."
FT /evidence="ECO:0000269|PubMed:10821675"
FT MUTAGEN 209
FT /note="Y->F: Slowly inactivated and unable to discriminate
FT between the enantiomers. Shows an inversion of the
FT diastereoselectivity. Loss of aldolase activity; when
FT associated with Q-73 and F-113."
FT /evidence="ECO:0000269|PubMed:10821675,
FT ECO:0000269|PubMed:11054289"
FT MUTAGEN 211..215
FT /note="Missing: Decrease of aldolase activity mostly due to
FT a decrease of the affinity for L-fuculose 1-phosphate
FT (Fuc1P)."
FT /evidence="ECO:0000269|PubMed:10821675"
FT HELIX 3..19
FT /evidence="ECO:0007829|PDB:1E4C"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:2FUA"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:1E4C"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:1E4C"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:1E4B"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:1E4C"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:1E4C"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:1E4C"
FT HELIX 74..83
FT /evidence="ECO:0007829|PDB:1E4C"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:1E4C"
FT HELIX 96..104
FT /evidence="ECO:0007829|PDB:1E4C"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:1E4C"
FT HELIX 113..118
FT /evidence="ECO:0007829|PDB:1E4C"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:1E47"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:1E46"
FT HELIX 134..143
FT /evidence="ECO:0007829|PDB:1E4C"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:2FUA"
FT STRAND 148..152
FT /evidence="ECO:0007829|PDB:1E4C"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:1E4C"
FT STRAND 156..163
FT /evidence="ECO:0007829|PDB:1E4C"
FT HELIX 164..185
FT /evidence="ECO:0007829|PDB:1E4C"
FT HELIX 196..205
FT /evidence="ECO:0007829|PDB:1E4C"
SQ SEQUENCE 215 AA; 23775 MW; BA9897E13ABE4A22 CRC64;
MERNKLARQI IDTCLEMTRL GLNQGTAGNV SVRYQDGMLI TPTGIPYEKL TESHIVFIDG
NGKHEEGKLP SSEWRFHMAA YQSRPDANAV VHNHAVHCTA VSILNRSIPA IHYMIAAAGG
NSIPCAPYAT FGTRELSEHV ALALKNRKAT LLQHHGLIAC EVNLEKALWL AHEVEVLAQL
YLTTLAITDP VPVLSDEEIA VVLEKFKTYG LRIEE
//
