ALDOB_CHICK
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 03-AUG-2022, entry version 150.
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}.
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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; P07341; -.
DR Ensembl; ENSGALT00000037630; ENSGALP00000036836; ENSGALG00000015544.
DR Ensembl; ENSGALT00000086136; ENSGALP00000062100; ENSGALG00000015544.
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; 799973at2759; -.
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 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: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: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 Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR029768; Aldolase_I_AS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000741; FBA_I.
DR PANTHER; PTHR11627; PTHR11627; 1.
DR Pfam; PF00274; Glycolytic; 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
