ID ALF_NOSS1 Reviewed; 359 AA. AC Q8YNK2; DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 27-MAR-2024, entry version 102. DE RecName: Full=Fructose-bisphosphate aldolase {ECO:0000250|UniProtKB:Q55664}; DE Short=FBP aldolase {ECO:0000250|UniProtKB:Q55664}; DE Short=FBPA {ECO:0000250|UniProtKB:Q55664}; DE EC=4.1.2.13; DE AltName: Full=Fructose-1,6-bisphosphate aldolase {ECO:0000250|UniProtKB:Q55664}; GN Name=fda {ECO:0000312|EMBL:BAB76262.1}; OrderedLocusNames=all4563; OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576). OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc. OX NCBI_TaxID=103690; RN [1] {ECO:0000312|EMBL:BAB76262.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576; RX PubMed=11759840; DOI=10.1093/dnares/8.5.205; RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A., RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M., RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M., RA Takazawa M., Yamada M., Yasuda M., Tabata S.; RT "Complete genomic sequence of the filamentous nitrogen-fixing RT cyanobacterium Anabaena sp. strain PCC 7120."; RL DNA Res. 8:205-213(2001). RN [2] {ECO:0000305} RP PROTEIN SEQUENCE OF 282-289, AND MASS SPECTROMETRY. RA Singh H., Rajaram H., Apte S.K.; RL Submitted (DEC-2008) to UniProtKB. 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|UniProtKB:Q55664}. 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 Evidence={ECO:0000250|UniProtKB:Q55664}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000250|UniProtKB:Q55664}; CC Note=Binds 2 Zn(2+) ions per subunit. One is catalytic and the other CC provides a structural contribution. {ECO:0000250|UniProtKB:Q55664}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 4/4. CC {ECO:0000250|UniProtKB:Q55664}. CC -!- MASS SPECTROMETRY: Mass=38764; Mass_error=1; Method=MALDI; CC Evidence={ECO:0000269|Ref.2}; CC -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase CC family. {ECO:0000255}. 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; BA000019; BAB76262.1; -; Genomic_DNA. DR PIR; AC2376; AC2376. DR RefSeq; WP_010998695.1; NZ_RSCN01000007.1. DR AlphaFoldDB; Q8YNK2; -. DR SMR; Q8YNK2; -. DR STRING; 103690.gene:10496613; -. DR KEGG; ana:all4563; -. DR eggNOG; COG0191; Bacteria. DR OrthoDB; 9803995at2; -. DR UniPathway; UPA00109; UER00183. DR Proteomes; UP000002483; 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:0000250|UniProtKB:Q55664" FT CHAIN 2..359 FT /note="Fructose-bisphosphate aldolase" FT /evidence="ECO:0000250|UniProtKB:Q55664" FT /id="PRO_0000366199" FT ACT_SITE 83 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:Q55664" FT BINDING 50 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000250|UniProtKB:Q55664" 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|UniProtKB:Q55664" FT BINDING 105 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:Q55664" FT BINDING 142 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:Q55664" 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|UniProtKB:Q55664" FT BINDING 199 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT /evidence="ECO:0000250|UniProtKB:Q55664" 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|UniProtKB:Q55664" FT BINDING 233..235 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT /evidence="ECO:0000250|UniProtKB:Q55664" FT BINDING 275..278 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT /evidence="ECO:0000250|UniProtKB:Q55664" SQ SEQUENCE 359 AA; 38617 MW; E91D84D7591007B1 CRC64; MALVPLRLLL DHAAENGYGI PAFNVNNLEQ IQAILKAAAE TDSPVILQAS RGARNYAGEN FLRHLILAAV ETYPEIPIVM HQDHGNAPST CYSAIKNNFT SVMMDGSLEA DAKTPASFEY NVNVTREVVN VAHALGVSVE GELGCLGSLE TGAGEAEDGH GFEGTLDHSQ LLTDPDEAVN FVEATQVDAL AVAIGTSHGA YKFTRKPTGE ILAISRIEEI HRRLPNTHLV MHGSSSVPED LIALINEYGG AIPETYGVPV EEIQKGIKSG VRKVNIDTDN RLAITAAVRE ALAKNPKEFD PRHFLKPSIT YMQKVCAERY VQFGTAGNAS KIKQVSLETF AAKYAKGELN AISKAAAKV //