ID ALF_CORGL Reviewed; 344 AA. AC P19537; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 145. 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=Cgl2770, cg3068; OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / OS JCM 1318 / LMG 3730 / NCIMB 10025). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; OC Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=196627; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-11. RC STRAIN=ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613; RX PubMed=2615658; DOI=10.1111/j.1365-2958.1989.tb00148.x; RA von der Osten C.H., Barbas C.F. III, Wong C.-H., Sinskey A.J.; RT "Molecular cloning, nucleotide sequence and fine-structural analysis of the RT Corynebacterium glutamicum fda gene: structural comparison of C. glutamicum RT fructose-1,6-biphosphate aldolase to class I and class II aldolases."; RL Mol. Microbiol. 3:1625-1637(1989). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / RC NCIMB 10025; RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1; RA Ikeda M., Nakagawa S.; RT "The Corynebacterium glutamicum genome: features and impacts on RT biotechnological processes."; RL Appl. Microbiol. Biotechnol. 62:99-109(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / RC NCIMB 10025; RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8; RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.; RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its RT impact on the production of L-aspartate-derived amino acids and vitamins."; RL J. Biotechnol. 104:5-25(2003). 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; X17313; CAA35190.1; -; Genomic_DNA. DR EMBL; BA000036; BAC00164.1; -; Genomic_DNA. DR EMBL; BX927156; CAF20791.1; -; Genomic_DNA. DR PIR; S09283; S09283. DR RefSeq; NP_601964.1; NC_003450.3. DR RefSeq; WP_011015363.1; NC_006958.1. DR AlphaFoldDB; P19537; -. DR SMR; P19537; -. DR STRING; 196627.cg3068; -. DR KEGG; cgb:cg3068; -. DR KEGG; cgl:Cgl2770; -. DR PATRIC; fig|196627.13.peg.2701; -. DR eggNOG; COG0191; Bacteria. DR HOGENOM; CLU_036923_1_0_11; -. DR OrthoDB; 9803995at2; -. DR BioCyc; CORYNE:G18NG-12387-MONOMER; -. DR UniPathway; UPA00109; UER00183. DR Proteomes; UP000000582; Chromosome. DR Proteomes; UP000001009; 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 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. DR World-2DPAGE; 0001:P19537; -. 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:2615658" FT CHAIN 2..344 FT /note="Fructose-bisphosphate aldolase" FT /id="PRO_0000178712" FT ACT_SITE 95 FT /note="Proton donor" FT /evidence="ECO:0000250" FT BINDING 53 FT /ligand="D-glyceraldehyde 3-phosphate" FT /ligand_id="ChEBI:CHEBI:59776" FT /evidence="ECO:0000250" FT BINDING 96 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 131 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 161 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 212 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 213 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT /evidence="ECO:0000250" FT BINDING 252 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 253..255 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT /evidence="ECO:0000250" FT BINDING 274..277 FT /ligand="dihydroxyacetone phosphate" FT /ligand_id="ChEBI:CHEBI:57642" FT /evidence="ECO:0000250" FT CONFLICT 280 FT /note="Q -> H (in Ref. 1; CAA35190)" FT /evidence="ECO:0000305" SQ SEQUENCE 344 AA; 37214 MW; 745B189A2AC72BBF CRC64; MPIATPEVYN EMLDRAKEGG FAFPAINCTS SETINAALKG FAEAESDGII QFSTGGAEFG SGLAVKNKVK GAVALAAFAH EAAKSYGINV ALHTDHCQKE VLDEYVRPLL AISQERVDRG ELPLFQSHMW DGSAVPIDEN LEIAQELLAK AKAANIILEV EIGVVGGEED GVEAKAGANL YTSPEDFEKT IDAIGTGEKG RYLLAATFGN VHGVYKPGNV KLRPEVLLEG QQVARKKLGL ADDALPFDFV FHGGSGSEKE KIEEALTYGV IKMNVDTDTQ YAFTRPIVSH MFENYNGVLK IDGEVGNKKA YDPRSYMKKA EQSMSERIIE SCQDLKSVGK TTSK //