ID ALF_CAMJE Reviewed; 354 AA. AC Q0PAS0; P53818; DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot. DT 19-SEP-2006, sequence version 1. DT 27-MAR-2024, entry version 96. 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, fdaC; OrderedLocusNames=Cj0597; OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / OS NCTC 11168). OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=192222; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700819 / NCTC 11168; RX PubMed=10688204; DOI=10.1038/35001088; RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S., RA Barrell B.G.; RT "The genome sequence of the food-borne pathogen Campylobacter jejuni RT reveals hypervariable sequences."; RL Nature 403:665-668(2000). 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; AL111168; CAL34743.1; -; Genomic_DNA. DR PIR; S52413; S52413. DR RefSeq; WP_002852272.1; NZ_SZUC01000002.1. DR RefSeq; YP_002344027.1; NC_002163.1. DR PDB; 3QM3; X-ray; 1.85 A; A/B/C/D/E/F/G/H=1-354. DR PDBsum; 3QM3; -. DR AlphaFoldDB; Q0PAS0; -. DR SMR; Q0PAS0; -. DR IntAct; Q0PAS0; 9. DR STRING; 192222.Cj0597; -. DR PaxDb; 192222-Cj0597; -. DR EnsemblBacteria; CAL34743; CAL34743; Cj0597. DR GeneID; 904922; -. DR KEGG; cje:Cj0597; -. DR PATRIC; fig|192222.6.peg.589; -. DR eggNOG; COG0191; Bacteria. DR HOGENOM; CLU_036923_0_0_7; -. DR OrthoDB; 9803995at2; -. DR UniPathway; UPA00109; UER00183. DR Proteomes; UP000000799; 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 1: Evidence at protein level; KW 3D-structure; Glycolysis; Lyase; Metal-binding; Reference proteome; Zinc. FT CHAIN 1..354 FT /note="Fructose-bisphosphate aldolase" FT /id="PRO_0000178711" 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 HELIX 3..5 FT /evidence="ECO:0007829|PDB:3QM3" FT STRAND 9..11 FT /evidence="ECO:0007829|PDB:3QM3" FT HELIX 14..16 FT /evidence="ECO:0007829|PDB:3QM3" FT HELIX 17..27 FT /evidence="ECO:0007829|PDB:3QM3" FT STRAND 31..35 FT /evidence="ECO:0007829|PDB:3QM3" FT HELIX 39..52 FT /evidence="ECO:0007829|PDB:3QM3" FT STRAND 56..60 FT /evidence="ECO:0007829|PDB:3QM3" FT HELIX 62..69 FT /evidence="ECO:0007829|PDB:3QM3" FT HELIX 76..95 FT /evidence="ECO:0007829|PDB:3QM3" FT STRAND 98..103 FT /evidence="ECO:0007829|PDB:3QM3" FT HELIX 108..110 FT /evidence="ECO:0007829|PDB:3QM3" FT HELIX 111..128 FT /evidence="ECO:0007829|PDB:3QM3" FT STRAND 134..137 FT /evidence="ECO:0007829|PDB:3QM3" FT HELIX 145..161 FT /evidence="ECO:0007829|PDB:3QM3" FT STRAND 165..169 FT /evidence="ECO:0007829|PDB:3QM3" FT TURN 188..190 FT /evidence="ECO:0007829|PDB:3QM3" FT HELIX 194..204 FT /evidence="ECO:0007829|PDB:3QM3" FT TURN 205..207 FT /evidence="ECO:0007829|PDB:3QM3" FT STRAND 211..214 FT /evidence="ECO:0007829|PDB:3QM3" FT HELIX 234..246 FT /evidence="ECO:0007829|PDB:3QM3" FT STRAND 257..259 FT /evidence="ECO:0007829|PDB:3QM3" FT HELIX 267..275 FT /evidence="ECO:0007829|PDB:3QM3" FT STRAND 278..283 FT /evidence="ECO:0007829|PDB:3QM3" FT HELIX 285..302 FT /evidence="ECO:0007829|PDB:3QM3" FT HELIX 303..305 FT /evidence="ECO:0007829|PDB:3QM3" FT STRAND 306..312 FT /evidence="ECO:0007829|PDB:3QM3" FT STRAND 315..319 FT /evidence="ECO:0007829|PDB:3QM3" FT HELIX 321..324 FT /evidence="ECO:0007829|PDB:3QM3" FT HELIX 326..347 FT /evidence="ECO:0007829|PDB:3QM3" SQ SEQUENCE 354 AA; 38730 MW; E4ACB44EA1860135 CRC64; MGVLDIVKAG VISGDELNKI 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 //