ID   ALDOC_CHICK             Reviewed;         137 AA.
AC   P53449;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   08-NOV-2023, entry version 112.
DE   RecName: Full=Fructose-bisphosphate aldolase C;
DE            EC=4.1.2.13;
DE   AltName: Full=Brain-type aldolase;
DE   Flags: Fragment;
GN   Name=ALDOC;
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 [MRNA].
RC   TISSUE=Brain;
RX   PubMed=7768978; DOI=10.1002/jcb.240570308;
RA   Meighan-Mantha R.L., Tolan D.R.;
RT   "Noncoordinate changes in the steady-state mRNA expressed from aldolase A
RT   and aldolase C genes during differentiation of chicken myoblasts.";
RL   J. Cell. Biochem. 57:423-431(1995).
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   -!- 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; L25375; AAA48589.1; -; mRNA.
DR   EMBL; S78291; AAB34480.1; -; mRNA.
DR   PIR; I51292; I51292.
DR   AlphaFoldDB; P53449; -.
DR   SMR; P53449; -.
DR   STRING; 9031.ENSGALP00000043256; -.
DR   PaxDb; 9031-ENSGALP00000043256; -.
DR   VEuPathDB; HostDB:geneid_395492; -.
DR   eggNOG; KOG1557; Eukaryota.
DR   HOGENOM; CLU_031243_0_0_1; -.
DR   InParanoid; P53449; -.
DR   PhylomeDB; P53449; -.
DR   BRENDA; 4.1.2.13; 1306.
DR   Reactome; R-GGA-352875; Gluconeogenesis.
DR   Reactome; R-GGA-352882; Glycolysis.
DR   UniPathway; UPA00109; UER00183.
DR   Proteomes; UP000000539; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
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:0006094; P:gluconeogenesis; TAS:Reactome.
DR   GO; GO:0006096; P:glycolytic process; TAS:Reactome.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR000741; FBA_I.
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.
PE   2: Evidence at transcript level;
KW   Glycolysis; Lyase; Reference proteome; Schiff base.
FT   CHAIN           <1..137
FT                   /note="Fructose-bisphosphate aldolase C"
FT                   /id="PRO_0000216952"
FT   ACT_SITE        3
FT                   /note="Schiff-base intermediate with dihydroxyacetone-P"
FT   SITE            137
FT                   /note="Necessary for preference for fructose 1,6-
FT                   bisphosphate over fructose 1-phosphate"
FT   NON_TER         1
SQ   SEQUENCE   137 AA;  14438 MW;  2E70FB9213133D15 CRC64;
     LLKPNMVTPG HSCPTKYSPE EIAMATVTAL RRTVPPAVPG VTFLSGGQSE EEASINLNAI
     NTCPLVRPWA LTFSYGRALQ ASALSAWRGQ RDNANAATEE FVKRAEVNGL AALGKYEGSG
     DDSGAAGQSL YVANHAY
//