ALDOA_PONAB
ID ALDOA_PONAB Reviewed; 364 AA.
AC Q5NVR5;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 88.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CR925940; CAI29598.1; -; mRNA.
DR RefSeq; NP_001127068.1; NM_001133596.2.
DR AlphaFoldDB; Q5NVR5; -.
DR SMR; Q5NVR5; -.
DR STRING; 9601.ENSPPYP00000024596; -.
DR GeneID; 100174098; -.
DR KEGG; pon:100174098; -.
DR CTD; 226; -.
DR eggNOG; KOG1557; Eukaryota.
DR InParanoid; Q5NVR5; -.
DR UniPathway; UPA00109; UER00183.
DR Proteomes; UP000001595; Unplaced.
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:0006096; P:glycolytic process; ISS:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
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 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_0000230295"
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; 39448 MW; 4DAED62BFE37CD33 CRC64;
MPYQYPALTP EQKKELSDIA HRIVAPGKGI LAADESTGSI AKRLQSIGTE NTEENRRFYR
QLLLTADDRV NPCIGGVILF HETLYQKADD GRPFPQVIKS KGGVVGIKVD KGVVPLAGTN
GETTTQGLDG LSERCAQYKK DGADFAKWRC VLKIGEHTPS ALAIMENANV LARYASICQQ
NGIVPIVEPE ILPDGDHDLK RCQYVTEKVL AAVYKALSDH HIYLEGTLLK PNMVTPGHAC
TQKFSHEEIV MATVTALRRT VPPAVTGITF LSGGQSEEEA SINLNAINKC PLLKPWALTF
SYGRALQASA LKAWGGKKEN LKAAQEEYVK RALANSLACQ GKYTPSGQAG AAASESLFVS
NHAY
