ID ALDOA_PANTR Reviewed; 364 AA. AC A5A6I5; DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot. DT 12-JUN-2007, sequence version 1. DT 24-JAN-2024, entry version 79. DE RecName: Full=Fructose-bisphosphate aldolase A; DE EC=4.1.2.13 {ECO:0000250|UniProtKB:P04075}; DE AltName: Full=Muscle-type aldolase; GN Name=ALDOA; OS Pan troglodytes (Chimpanzee). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Pan. OX NCBI_TaxID=9598; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Cerebellum; RX PubMed=17574350; DOI=10.1016/j.gene.2007.04.013; RA Sakate R., Suto Y., Imanishi T., Tanoue T., Hida M., Hayasaka I., RA Kusuda J., Gojobori T., Hashimoto K., Hirai M.; RT "Mapping of chimpanzee full-length cDNAs onto the human genome unveils RT large potential divergence of the transcriptome."; RL Gene 399:1-10(2007). CC -!- FUNCTION: Catalyzes the reversible conversion of beta-D-fructose 1,6- CC bisphosphate (FBP) into two triose phosphate and plays a key role in CC glycolysis and gluconeogenesis (By similarity). In addition, may also CC function as scaffolding protein (By similarity). {ECO:0000250, CC ECO:0000250|UniProtKB:P04075}. 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:P04075}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14730; CC Evidence={ECO:0000250|UniProtKB:P04075}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 4/4. CC -!- SUBUNIT: Homotetramer. Interacts with SNX9 and WAS. Interacts with CC FBP2; the interaction blocks FBP2 inhibition by physiological CC concentrations of AMP and reduces inhibition by Ca(2+) (By similarity). CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, I band CC {ECO:0000250|UniProtKB:P00883}. Cytoplasm, myofibril, sarcomere, M line CC {ECO:0000250|UniProtKB:P00883}. Note=In skeletal muscle, accumulates CC around the M line and within the I band, colocalizing with FBP2 on both CC sides of the Z line in the absence of Ca(2+). CC {ECO:0000250|UniProtKB:P00883}. CC -!- MISCELLANEOUS: In vertebrates, three forms of this ubiquitous CC glycolytic enzyme are found, aldolase A in muscle, aldolase B in liver CC and 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; AB222113; BAF62358.1; -; mRNA. DR RefSeq; NP_001138305.1; NM_001144833.1. DR AlphaFoldDB; A5A6I5; -. DR SMR; A5A6I5; -. DR STRING; 9598.ENSPTRP00000064780; -. DR PaxDb; 9598-ENSPTRP00000055755; -. DR GeneID; 454362; -. DR KEGG; ptr:454362; -. DR CTD; 226; -. DR eggNOG; KOG1557; Eukaryota. DR InParanoid; A5A6I5; -. DR OrthoDB; 3664741at2759; -. DR UniPathway; UPA00109; UER00183. DR Proteomes; UP000002277; Unplaced. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0031674; C:I band; IEA:UniProtKB-SubCell. DR GO; GO:0031430; C:M band; IEA:UniProtKB-SubCell. DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; ISS:UniProtKB. DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IBA:GO_Central. DR GO; GO:0006096; P:glycolytic process; ISS:UniProtKB. DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB. 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:SF1; FRUCTOSE-BISPHOSPHATE ALDOLASE A; 1. DR Pfam; PF00274; Glycolytic; 1. DR SUPFAM; SSF51569; Aldolase; 1. DR PROSITE; PS00158; ALDOLASE_CLASS_I; 1. PE 2: Evidence at transcript level; KW Acetylation; Cytoplasm; Glycolysis; Hydroxylation; Isopeptide bond; Lyase; KW Phosphoprotein; Reference proteome; Schiff base; Ubl conjugation. FT CHAIN 1..364 FT /note="Fructose-bisphosphate aldolase A" FT /id="PRO_0000295307" 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 BINDING 56 FT /ligand="substrate" FT BINDING 147 FT /ligand="substrate" FT SITE 364 FT /note="Necessary for preference for fructose 1,6- FT bisphosphate over fructose 1-phosphate" FT MOD_RES 5 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P05065" FT MOD_RES 9 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P04075" FT MOD_RES 36 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P04075" FT MOD_RES 39 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P04075" FT MOD_RES 42 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P04075" FT MOD_RES 46 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P04075" FT MOD_RES 99 FT /note="N6-(2-hydroxyisobutyryl)lysine" FT /evidence="ECO:0000250|UniProtKB:P04075" FT MOD_RES 108 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P04075" FT MOD_RES 111 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P09972" FT MOD_RES 111 FT /note="N6-malonyllysine; alternate" FT /evidence="ECO:0000250" FT MOD_RES 132 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P05065" FT MOD_RES 147 FT /note="N6-(2-hydroxyisobutyryl)lysine" FT /evidence="ECO:0000250|UniProtKB:P04075" FT MOD_RES 272 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P04075" FT MOD_RES 312 FT /note="N6-malonyllysine" FT /evidence="ECO:0000250" FT MOD_RES 330 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P04075" FT CROSSLNK 42 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0000250|UniProtKB:P04075" FT CROSSLNK 42 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P04075" SQ SEQUENCE 364 AA; 39434 MW; B3D6546B86D4E604 CRC64; MPYQYPALTP EQKKELSDIA HRIVAPGKGI LAADESTGSI AKRLQSIGTE NTEENRRFYR QLLLTADDRV NPCIVGVILF HETLYQKADD GRPFPQVIKS KGGVVGIKVD KGVVPLAGTN GETTTQGLDG LSERCAQYKK DGADFAKWRC VLKIGEHTPS ALAIMENANV LARYASICQQ NGIVPIAEPE ILPDGDHDLK RCQYVTEKVL AAVYKALSDH HIYLEGTLLK PNMVTPGHAC TQKFSHEEIA MATVTALRRT VPPAVTGITF LSGGQSEEEA SINLNAINKC PLLKPWALTF SYGRALQASA LKAWGGKKEN LKAAQEEYVK RALANSLACQ GKYTPSGQAG AAASESLFVS NHAY //