FUCA_ECO57
ID FUCA_ECO57 Reviewed; 215 AA.
AC Q8X6R8; Q7AB69;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=L-fuculose phosphate aldolase {ECO:0000255|HAMAP-Rule:MF_00987};
DE EC=4.1.2.17 {ECO:0000255|HAMAP-Rule:MF_00987};
DE AltName: Full=L-fuculose-1-phosphate aldolase {ECO:0000255|HAMAP-Rule:MF_00987};
GN Name=fucA {ECO:0000255|HAMAP-Rule:MF_00987};
GN OrderedLocusNames=Z4117, ECs3660;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: Involved in the degradation of L-fucose and D-arabinose.
CC Catalyzes the reversible cleavage of L-fuculose 1-phosphate (Fuc1P) to
CC yield dihydroxyacetone phosphate (DHAP) and L-lactaldehyde.
CC {ECO:0000255|HAMAP-Rule:MF_00987}.
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00987};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00987};
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}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00987}.
CC -!- SIMILARITY: Belongs to the aldolase class II family. AraD/FucA
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00987}.
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DR EMBL; AE005174; AAG57914.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB37083.1; -; Genomic_DNA.
DR PIR; D91086; D91086.
DR PIR; F85931; F85931.
DR RefSeq; NP_311687.1; NC_002695.1.
DR RefSeq; WP_000440775.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; Q8X6R8; -.
DR SMR; Q8X6R8; -.
DR STRING; 155864.EDL933_3981; -.
DR EnsemblBacteria; AAG57914; AAG57914; Z4117.
DR EnsemblBacteria; BAB37083; BAB37083; ECs_3660.
DR GeneID; 916460; -.
DR KEGG; ece:Z4117; -.
DR KEGG; ecs:ECs_3660; -.
DR PATRIC; fig|386585.9.peg.3826; -.
DR eggNOG; COG0235; Bacteria.
DR HOGENOM; CLU_006033_3_0_6; -.
DR OMA; YATFGTH; -.
DR UniPathway; UPA00563; UER00626.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0008738; F:L-fuculose-phosphate aldolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019568; P:arabinose catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0042355; P:L-fucose catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.225.10; -; 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 Pfam; PF00596; Aldolase_II; 1.
DR SMART; SM01007; Aldolase_II; 1.
DR SUPFAM; SSF53639; SSF53639; 1.
DR TIGRFAMs; TIGR01086; fucA; 1.
PE 3: Inferred from homology;
KW Arabinose catabolism; Carbohydrate metabolism; Fucose metabolism; Lyase;
KW Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..215
FT /note="L-fuculose phosphate aldolase"
FT /id="PRO_0000162926"
FT ACT_SITE 73
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00987"
FT BINDING 28..29
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00987"
FT BINDING 43..44
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00987"
FT BINDING 71..72
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00987"
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 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 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 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 SITE 113
FT /note="Plays a key role in the stabilization of the
FT transition state and positioning the aldehyde component"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00987"
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:0000255|HAMAP-Rule:MF_00987"
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:0000255|HAMAP-Rule:MF_00987"
SQ SEQUENCE 215 AA; 23785 MW; 072E4EC5A94E76D1 CRC64;
MERNKLARQI IDTCLEMTRL GLNQGTAGNV SVRYQDGMLI TPTGIPYEKL TESHIVFIDG
NGKHEEGKLP SSEWRFHMAA YQSRPDANAV VHNHAVHCTA VSILNRPIPA IHYMIAAAGG
NSIPCAPYAT FGTRELSEHV ALALKNRKAT LLQHHGLIAC EVNLEKALWL AHEVEVLAQL
YLTTLAITDP VPVLSDEEIA VVLEKFKTYG LRIEE
