ID ALF2_SYNY3 Reviewed; 359 AA. AC Q55664; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 139. DE RecName: Full=Fructose-bisphosphate aldolase class 2; DE Short=FBP aldolase; DE Short=FBPA; DE EC=4.1.2.13; DE AltName: Full=Fructose-1,6-bisphosphate aldolase; DE AltName: Full=Fructose-bisphosphate aldolase class II; GN Name=fbaA; Synonyms=fda; OrderedLocusNames=sll0018; OS Synechocystis sp. (strain PCC 6803 / Kazusa). OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae; OC Synechocystis. OX NCBI_TaxID=1111708; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27184 / PCC 6803 / N-1; RX PubMed=8590279; DOI=10.1093/dnares/2.4.153; RA Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N., RA Sugiura M., Tabata S.; RT "Sequence analysis of the genome of the unicellular cyanobacterium RT Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region RT from map positions 64% to 92% of the genome."; RL DNA Res. 2:153-166(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 6803 / Kazusa; RX PubMed=8905231; DOI=10.1093/dnares/3.3.109; RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S., RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.; RT "Sequence analysis of the genome of the unicellular cyanobacterium RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire RT genome and assignment of potential protein-coding regions."; RL DNA Res. 3:109-136(1996). RN [3] RP PROTEIN SEQUENCE OF 2-21. RX PubMed=9298645; DOI=10.1002/elps.1150180806; RA Sazuka T., Ohara O.; RT "Towards a proteome project of cyanobacterium Synechocystis sp. strain RT PCC6803: linking 130 protein spots with their respective genes."; RL Electrophoresis 18:1252-1258(1997). 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}. 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; BA000022; BAA10184.1; -; Genomic_DNA. DR PIR; S76332; S76332. DR AlphaFoldDB; Q55664; -. DR SMR; Q55664; -. DR IntAct; Q55664; 1. DR STRING; 1148.gene:10499681; -. DR BindingDB; Q55664; -. DR ChEMBL; CHEMBL4523320; -. DR PaxDb; 1148-1001557; -. DR EnsemblBacteria; BAA10184; BAA10184; BAA10184. DR KEGG; syn:sll0018; -. DR eggNOG; COG0191; Bacteria. DR InParanoid; Q55664; -. DR PhylomeDB; Q55664; -. DR BioCyc; MetaCyc:FBAASYN-MONOMER; -. DR BRENDA; 4.1.2.13; 6192. DR SABIO-RK; Q55664; -. DR UniPathway; UPA00109; UER00183. DR Proteomes; UP000001425; 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; cd00947; TBP_aldolase_IIB; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000771; FBA_II. DR InterPro; IPR006412; Fruct_bisP_Calv. DR NCBIfam; TIGR00167; cbbA; 1. DR NCBIfam; TIGR01521; FruBisAldo_II_B; 1. DR PANTHER; PTHR30304; D-TAGATOSE-1,6-BISPHOSPHATE ALDOLASE; 1. DR PANTHER; PTHR30304:SF0; D-TAGATOSE-1,6-BISPHOSPHATE ALDOLASE SUBUNIT GATY-RELATED; 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 Direct protein sequencing; Glycolysis; Lyase; Metal-binding; KW Reference proteome; Zinc. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:9298645" FT CHAIN 2..359 FT /note="Fructose-bisphosphate aldolase class 2" FT /id="PRO_0000178751" FT ACT_SITE 83 FT /note="Proton donor" FT /evidence="ECO:0000250" FT BINDING 50 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000250" FT BINDING 84 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 105 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 142 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 198 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 199 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT /evidence="ECO:0000250" FT BINDING 232 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 233..235 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT /evidence="ECO:0000250" FT BINDING 275..278 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT /evidence="ECO:0000250" SQ SEQUENCE 359 AA; 38972 MW; 2D005351B70931C3 CRC64; MALVPMRLLL DHAAENGYGI PAFNVNNMEQ IISIMQAADE TDSPVILQAS RGARSYAGEN FLRHLVLGAV ETYPHIPIAM HQDHGNSPAT CYSAIRNGFT SVMMDGSLEA DAKTPASFEY NVNVTAEVVK VAHSVGASVE GELGCLGSLE TGQGEAEDGH GFEGKLDHSQ LLTDPEEAVE FVNKTQVDAL AVAIGTSHGA YKFTRKPTGE VLAISRIEEI HRLLPNTHLV MHGSSSVPQE WIDMINEFGG AIPETYGVPV EEIQKGIKSG VRKVNIDTDN RLAITAAFRE AAAKDPKNFD PRHFLKPSIK YMKQVCADRY QQFWTAGNAS KIKQLTLDDY AAKYAKGELT ATSRTSVAV //