ALF_EDWI9
ID ALF_EDWI9 Reviewed; 358 AA.
AC O52402; C5BAU5;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Fructose-bisphosphate aldolase;
DE Short=FBP aldolase;
DE Short=FBPA;
DE EC=4.1.2.13;
DE AltName: Full=Fructose-1,6-bisphosphate aldolase;
GN Name=fba; Synonyms=fda; OrderedLocusNames=NT01EI_3367;
OS Edwardsiella ictaluri (strain 93-146).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Hafniaceae; Edwardsiella.
OX NCBI_TaxID=634503;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12542086; DOI=10.3354/dao052093;
RA Moore M.M., Fernandez D.L., Thune R.L.;
RT "Cloning and characterization of Edwardsiella ictaluri proteins expressed
RT and recognized by the channel catfish Ictalurus punctatus immune response
RT during infection.";
RL Dis. Aquat. Organ. 52:93-107(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-146;
RA Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the aldol condensation of dihydroxyacetone
CC phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate
CC (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and
CC the reverse reaction in glycolysis. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-
CC phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729,
CC ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. One is catalytic and the other
CC provides a structural contribution. {ECO:0000250};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 4/4.
CC -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase
CC family. {ECO:0000305}.
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DR EMBL; AF037440; AAB92572.1; -; Genomic_DNA.
DR EMBL; CP001600; ACR70504.1; -; Genomic_DNA.
DR RefSeq; WP_015872577.1; NC_012779.2.
DR AlphaFoldDB; O52402; -.
DR SMR; O52402; -.
DR STRING; 67780.B6E78_08520; -.
DR PRIDE; O52402; -.
DR EnsemblBacteria; ACR70504; ACR70504; NT01EI_3367.
DR GeneID; 7959666; -.
DR KEGG; eic:NT01EI_3367; -.
DR PATRIC; fig|634503.3.peg.2993; -.
DR HOGENOM; CLU_036923_0_0_6; -.
DR OMA; QAYCAEK; -.
DR OrthoDB; 827430at2; -.
DR SABIO-RK; O52402; -.
DR UniPathway; UPA00109; UER00183.
DR Proteomes; UP000001485; Chromosome.
DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00946; FBP_aldolase_IIA; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000771; FBA_II.
DR InterPro; IPR006411; Fruct_bisP_bact.
DR PANTHER; PTHR30559; PTHR30559; 1.
DR Pfam; PF01116; F_bP_aldolase; 1.
DR PIRSF; PIRSF001359; F_bP_aldolase_II; 1.
DR TIGRFAMs; TIGR00167; cbbA; 1.
DR TIGRFAMs; TIGR01520; FruBisAldo_II_A; 1.
DR PROSITE; PS00602; ALDOLASE_CLASS_II_1; 1.
DR PROSITE; PS00806; ALDOLASE_CLASS_II_2; 1.
PE 3: Inferred from homology;
KW Glycolysis; Lyase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..358
FT /note="Fructose-bisphosphate aldolase"
FT /id="PRO_0000178715"
FT ACT_SITE 109
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 62
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250"
FT BINDING 264
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 265..267
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250"
FT BINDING 286..289
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250"
FT CONFLICT 20
FT /note="K -> E (in Ref. 1; AAB92572)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 358 AA; 39155 MW; 0EAADF89554D8049 CRC64;
MSKIFDFVKP GVIFGDDVQK VFQVAKENKF ALPAVNCVGT DSINAVMEAA AKVRAPIIVQ
FSNGGAAFIA GKGLKLEGQQ GAILGAIAGA HHVHQMAEYY GVPVILHTDH CAKKLLPWLD
GLLDAGEKHF AATGKPLFSS HMIDLSEESL EENIEICSQY LARMSKIGMT LELELGCTGG
EEDGVDNSHL DNSALYTQPE DVDYAFTKLS AISPRFTIAA SFGNVHGVYK PGNVQLTPVI
LKNSQEYVSK KHNLPHNSLN FVFHGGSGST AAEIKEAVSY GVVKMNIDTD TQWATWEGVL
KYYKKNEGYL QGQLGNPEGD DKPNKKYYDP RVWLRAAQTG MIERLEQAFK ELNCIDVL
