ID   ALDOC_PANTR             Reviewed;         364 AA.
AC   Q5R1X4;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-NOV-2023, entry version 101.
DE   RecName: Full=Fructose-bisphosphate aldolase C;
DE            EC=4.1.2.13;
DE   AltName: Full=Brain-type aldolase;
GN   Name=ALDOC; Synonyms=ALDC;
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;
RA   Hirai M., Sakate R., Hida M., Sugano S., Hayasaka I., Suto Y., Osada N.,
RA   Hashimoto K.;
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
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. Interacts with ATP6V1E1. {ECO:0000250}.
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; AB188273; BAD74024.1; -; mRNA.
DR   RefSeq; NP_001009147.1; NM_001009147.2.
DR   AlphaFoldDB; Q5R1X4; -.
DR   SMR; Q5R1X4; -.
DR   STRING; 9598.ENSPTRP00000015230; -.
DR   PaxDb; 9598-ENSPTRP00000015230; -.
DR   GeneID; 493951; -.
DR   KEGG; ptr:493951; -.
DR   CTD; 230; -.
DR   eggNOG; KOG1557; Eukaryota.
DR   InParanoid; Q5R1X4; -.
DR   OrthoDB; 3664741at2759; -.
DR   UniPathway; UPA00109; UER00183.
DR   Proteomes; UP000002277; Unplaced.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004332; F:fructose-bisphosphate aldolase activity; ISS:UniProtKB.
DR   GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; ISS:UniProtKB.
DR   GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
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:SF3; FRUCTOSE-BISPHOSPHATE ALDOLASE C; 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; Glycolysis; Lyase; Phosphoprotein; Reference proteome;
KW   Schiff base.
FT   CHAIN           1..364
FT                   /note="Fructose-bisphosphate aldolase C"
FT                   /id="PRO_0000216950"
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         36
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P09972"
FT   MOD_RES         39
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P09972"
FT   MOD_RES         45
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P09972"
FT   MOD_RES         111
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P09972"
FT   MOD_RES         132
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P05065"
SQ   SEQUENCE   364 AA;  39527 MW;  5064305BB473D8AE CRC64;
     MPHSYPALSA EQKKELSDIA LRIVAPGKGI LAADESVGSM AKRLSQIGVE NTEENRRLYR
     QVLFSADDRV KKCIGGVIFF HETLYQKDDN GVPFIRTILD KGIVVGIKVD KGVVPLAGTD
     GETTTQGLDG LSERCAQYKK DGADFAKWRC VLKISERTPS ALAILENANV LARYASICQQ
     NGIVPIVEPE ILPDGDHDLK RCQYVTEKVL AAVYKALSDH HVYLEGTLLK PNMVTPGHAC
     PIKYTPEEIA MATVTALRRT VPPAVPGVTF LSGGQSEEEA SFNLNAINRC PLPRPWALTF
     SYGRALQASA LNAWRGQRDN AEAATEEFIK RAEVNGLAAQ GKYEGSGEDG GAAAQSLYIA
     NHAY
//