FUCA_HAEIN
ID FUCA_HAEIN Reviewed; 216 AA.
AC P44777;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 129.
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}; OrderedLocusNames=HI_0611;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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; L42023; AAC22270.1; -; Genomic_DNA.
DR PIR; C64081; C64081.
DR RefSeq; NP_438769.1; NC_000907.1.
DR RefSeq; WP_005694545.1; NC_000907.1.
DR AlphaFoldDB; P44777; -.
DR SMR; P44777; -.
DR STRING; 71421.HI_0611; -.
DR EnsemblBacteria; AAC22270; AAC22270; HI_0611.
DR KEGG; hin:HI_0611; -.
DR PATRIC; fig|71421.8.peg.635; -.
DR eggNOG; COG0235; Bacteria.
DR HOGENOM; CLU_006033_3_0_6; -.
DR OMA; YATFGTH; -.
DR PhylomeDB; P44777; -.
DR BioCyc; HINF71421:G1GJ1-632-MON; -.
DR UniPathway; UPA00563; UER00626.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016832; F:aldehyde-lyase activity; IBA:GO_Central.
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 GO; GO:0019323; P:pentose catabolic process; IBA:GO_Central.
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..216
FT /note="L-fuculose phosphate aldolase"
FT /id="PRO_0000162928"
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 216 AA; 23944 MW; 4DBEEE21ED8EA6C6 CRC64;
MNRAELSQKI IDTCLEMTKL GLNQGTAGNV SVRYKDGMLI TPTGMPYHLM KTENIVYVDG
NGKHEENKLP SSEWQFHLSV YHTRPEANAV VHNHSIHCAG LSILEKPIPA IHYMVAVSGT
DHIPCVPYAT FGSHKLASYV ATGIKESKAI LLAHHGLITC GENLDKALWL AQEVEVLASW
YLKLLSTGLE IPLLSKEQMQ VVLGKFHTYG LRIEES
