ID ALF_CAMJJ Reviewed; 354 AA. AC A1VYV7; P53818; DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 1. DT 27-MAR-2024, entry version 85. 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=fbaA, fda, fdaC; OrderedLocusNames=CJJ81176_0625; OS Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176). OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=354242; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8525063; DOI=10.1016/0923-2508(96)80292-0; RA Burucoa C., Fremaux C., Pei Z., Tummuru M., Blaser M.J., Cenatiempo Y., RA Fauchere J.L.; RT "Nucleotide sequence and characterization of peb4A encoding an antigenic RT protein in Campylobacter jejuni."; RL Res. Microbiol. 146:467-476(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=81-176; RA Fouts D.E., Nelson K.E., Sebastian Y.; RL Submitted (DEC-2006) 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 -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase CC family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X84703; CAA59176.1; -; Genomic_DNA. DR EMBL; CP000538; EAQ73283.1; -; Genomic_DNA. DR PIR; S52413; S52413. DR RefSeq; WP_002856965.1; NC_008787.1. DR AlphaFoldDB; A1VYV7; -. DR SMR; A1VYV7; -. DR KEGG; cjj:CJJ81176_0625; -. DR eggNOG; COG0191; Bacteria. DR HOGENOM; CLU_036923_0_0_7; -. DR UniPathway; UPA00109; UER00183. DR Proteomes; UP000000646; 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; Aldolase class I; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000771; FBA_II. DR InterPro; IPR006411; Fruct_bisP_bact. DR NCBIfam; TIGR00167; cbbA; 1. DR NCBIfam; TIGR01520; FruBisAldo_II_A; 1. DR PANTHER; PTHR30559:SF0; FRUCTOSE-BISPHOSPHATE ALDOLASE; 1. DR PANTHER; PTHR30559; FRUCTOSE-BISPHOSPHATE ALDOLASE CLASS 2; 1. DR Pfam; PF01116; F_bP_aldolase; 1. DR PIRSF; PIRSF001359; F_bP_aldolase_II; 1. DR SUPFAM; SSF51569; Aldolase; 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; Zinc. FT CHAIN 1..354 FT /note="Fructose-bisphosphate aldolase" FT /id="PRO_0000281895" FT ACT_SITE 104 FT /note="Proton donor" FT /evidence="ECO:0000250" FT BINDING 61 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000250" FT BINDING 105 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 139 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 169 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 221 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 222 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT /evidence="ECO:0000250" FT BINDING 260 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 261..263 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT /evidence="ECO:0000250" FT BINDING 282..285 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT /evidence="ECO:0000250" FT CONFLICT 20 FT /note="V -> I (in Ref. 1; CAA59176)" FT /evidence="ECO:0000305" SQ SEQUENCE 354 AA; 38716 MW; 3F42FDE4782192C3 CRC64; MGVLDIVKAG VISGDELNKV YDYAKAEGFA IPAVNVVGTD SINAVLEAAK KVNSPVIIQF SNGGAKFYAG KNCPNGEVLG AISGAKHVHL LAKAYGVPVI LHTDHAARKL LPWIDGLIEA NAQYKKTHGQ ALFSSHMLDL SEESLEENLS TCEVYLQKLD ALGVALEIEL GCTGGEEDGV DNTGIDNSKL YTQPEDVALA YERLGKISDK FSIAASFGNV HGVYKPGNVS LQPEILKNSQ KFVKDKFALN SDKPINFVFH GGSGSELKDI KNAVSYGVIK MNIDTDTQWA FWDGVREYEL KNRAYLQGQI GNPEGDDKPN KKYYDPRVWL RSGEESMIKR LEIAFEDLNC INKN //