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,
GN   ECO:0000303|PubMed:2664711}; Synonyms=fucC, prd;
GN   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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00987, ECO:0000269|PubMed:10821675,
CC         ECO:0000269|PubMed:11054289, ECO:0000269|PubMed:13898172,
CC         ECO:0000269|PubMed:15299567, ECO:0000269|PubMed:8515438,
CC         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
FT                   1-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
FT                   A-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
//