ID ALDOB_CHICK Reviewed; 364 AA. AC P07341; DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 24-JAN-2024, entry version 155. DE RecName: Full=Fructose-bisphosphate aldolase B; DE EC=4.1.2.13; DE AltName: Full=Liver-type aldolase; GN Name=ALDOB; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; OC Phasianinae; Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2985560; DOI=10.1016/s0021-9258(18)89114-1; RA Burgess D.G., Penhoet E.E.; RT "Characterization of the chicken aldolase B gene."; RL J. Biol. Chem. 260:4604-4614(1985). 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 -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 4/4. CC -!- SUBUNIT: Homotetramer. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing CC center, centrosome, centriolar satellite {ECO:0000250}. CC -!- MISCELLANEOUS: In vertebrates, 3 forms of this ubiquitous glycolytic CC enzyme are found, aldolase A in muscle, aldolase B in liver and CC aldolase C in brain. CC -!- SIMILARITY: Belongs to the class I 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; M10946; AAA48587.1; -; Genomic_DNA. DR PIR; A22568; ADCHB. DR RefSeq; NP_001007978.1; NM_001007977.2. DR AlphaFoldDB; P07341; -. DR SMR; P07341; -. DR BioGRID; 686645; 1. DR IntAct; P07341; 1. DR STRING; 9031.ENSGALP00000036836; -. DR PaxDb; 9031-ENSGALP00000036836; -. DR Ensembl; ENSGALT00000086136; ENSGALP00000062100; ENSGALG00000015544. DR Ensembl; ENSGALT00010013368.1; ENSGALP00010007922.1; ENSGALG00010005583.1. DR Ensembl; ENSGALT00015069468; ENSGALP00015042603; ENSGALG00015028640. DR GeneID; 427308; -. DR KEGG; gga:427308; -. DR CTD; 229; -. DR VEuPathDB; HostDB:geneid_427308; -. DR eggNOG; KOG1557; Eukaryota. DR GeneTree; ENSGT00950000182987; -. DR HOGENOM; CLU_031243_0_0_1; -. DR InParanoid; P07341; -. DR OMA; ANCQAAQ; -. DR OrthoDB; 3664741at2759; -. DR PhylomeDB; P07341; -. DR TreeFam; TF314203; -. DR Reactome; R-GGA-352875; Gluconeogenesis. DR Reactome; R-GGA-352882; Glycolysis. DR Reactome; R-GGA-70171; Glycolysis. DR Reactome; R-GGA-70263; Gluconeogenesis. DR Reactome; R-GGA-70350; Fructose catabolism. DR UniPathway; UPA00109; UER00183. DR PRO; PR:P07341; -. DR Proteomes; UP000000539; Chromosome Z. DR Bgee; ENSGALG00000015544; Expressed in liver and 11 other cell types or tissues. DR GO; GO:0034451; C:centriolar satellite; ISA:AgBase. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0070062; C:extracellular exosome; ISA:AgBase. DR GO; GO:0005815; C:microtubule organizing center; ISA:AgBase. DR GO; GO:0051117; F:ATPase binding; ISA:AgBase. DR GO; GO:0008092; F:cytoskeletal protein binding; ISA:AgBase. DR GO; GO:0070061; F:fructose binding; ISA:AgBase. DR GO; GO:0061609; F:fructose-1-phosphate aldolase activity; ISA:AgBase. DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; ISA:AgBase. DR GO; GO:0042802; F:identical protein binding; ISA:AgBase. DR GO; GO:0060090; F:molecular adaptor activity; IEA:Ensembl. DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; ISA:AgBase. DR GO; GO:0061624; P:fructose catabolic process to hydroxyacetone phosphate and glyceraldehyde-3-phosphate; IEA:Ensembl. DR GO; GO:0006000; P:fructose metabolic process; ISA:AgBase. DR GO; GO:0006094; P:gluconeogenesis; TAS:Reactome. DR GO; GO:0006096; P:glycolytic process; ISA:AgBase. DR GO; GO:0001889; P:liver development; IEP:AgBase. DR GO; GO:0006116; P:NADH oxidation; ISA:AgBase. DR GO; GO:1905856; P:negative regulation of pentose-phosphate shunt; IEA:Ensembl. DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; ISA:AgBase. DR GO; GO:0070072; P:vacuolar proton-transporting V-type ATPase complex assembly; ISA:AgBase. DR CDD; cd00948; FBP_aldolase_I_a; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR InterPro; IPR029768; Aldolase_I_AS. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000741; FBA_I. DR NCBIfam; NF033379; FrucBisAld_I; 1. DR PANTHER; PTHR11627; FRUCTOSE-BISPHOSPHATE ALDOLASE; 1. DR PANTHER; PTHR11627:SF2; FRUCTOSE-BISPHOSPHATE ALDOLASE B; 1. DR Pfam; PF00274; Glycolytic; 1. DR SUPFAM; SSF51569; Aldolase; 1. DR PROSITE; PS00158; ALDOLASE_CLASS_I; 1. PE 3: Inferred from homology; KW Cytoplasm; Cytoskeleton; Glycolysis; Lyase; Reference proteome; KW Schiff base. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250" FT CHAIN 2..364 FT /note="Fructose-bisphosphate aldolase B" FT /id="PRO_0000216945" FT ACT_SITE 188 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT ACT_SITE 230 FT /note="Schiff-base intermediate with dihydroxyacetone-P" FT /evidence="ECO:0000250" FT BINDING 56 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 147 FT /ligand="substrate" FT /evidence="ECO:0000250" FT SITE 364 FT /note="Necessary for preference for fructose 1,6- FT bisphosphate over fructose 1-phosphate" FT /evidence="ECO:0000250" SQ SEQUENCE 364 AA; 39296 MW; 40E0C300FB574CEB CRC64; MTHQFPALSP EQKKALSDIA QRIVASGKGI LAADESVGTM GNRLQRINVE NTEENRRAFR EILFSSDASI SKSIGGVILF HETLYQKDSS GKPFPAIIKE KGMVVGIKLD AGTAPLAGTN GETTIQGLDK LAERCAQYKK DGADFGKWRA VLKISSTTPS QLAIQENANT LARYASICQQ NGLVPIVEPE VLPDGDHDLQ RCQYVTEKVL AAVYKALNDH HVYLEGTLLK PNMVTAGHSC PKKYTPQDVA VATVTTLLRT VPAAVPGICF LSGGQSEEEA SLNLNAMNQS PLPKPWKLTF SYGRALQASA LAAWLGKSEN KKAAQEAFCK RAQINSLACR GQYVTSGKTD TAATQSLFTA SYTY //