ID   ALDCA_DANRE             Reviewed;         364 AA.
AC   Q4KMC8;
DT   24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Fructose-bisphosphate aldolase C-A {ECO:0000312|ZFIN:ZDB-GENE-050706-128};
DE            EC=4.1.2.13;
DE   AltName: Full=Aldolase C-like {ECO:0000312|ZFIN:ZDB-GENE-050706-128};
DE   AltName: Full=Brain-type aldolase-A {ECO:0000250|UniProtKB:P09117};
GN   Name=aldoca {ECO:0000312|ZFIN:ZDB-GENE-050706-128};
GN   Synonyms=aldocl {ECO:0000312|ZFIN:ZDB-GENE-050706-128},
GN   zebrin II {ECO:0000303|PubMed:19371731}; ORFNames=zgc:112357;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1] {ECO:0000312|EMBL:AAH98624.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain {ECO:0000312|EMBL:AAH98624.1};
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000305}
RP   INDUCTION.
RX   PubMed=17013923; DOI=10.1002/neu.20328;
RA   Harden M.V., Newton L.A., Lloyd R.C., Whitlock K.E.;
RT   "Olfactory imprinting is correlated with changes in gene expression in the
RT   olfactory epithelia of the zebrafish.";
RL   J. Neurobiol. 66:1452-1466(2006).
RN   [3] {ECO:0000305}
RP   TISSUE SPECIFICITY.
RX   PubMed=19371731; DOI=10.1016/j.ydbio.2009.04.013;
RA   Bae Y.-K., Kani S., Shimizu T., Tanabe K., Nojima H., Kimura Y.,
RA   Higashijima S., Hibi M.;
RT   "Anatomy of zebrafish cerebellum and screen for mutations affecting its
RT   development.";
RL   Dev. Biol. 330:406-426(2009).
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:0000305};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 4/4.
CC       {ECO:0000305}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P09117}.
CC   -!- TISSUE SPECIFICITY: Expressed specifically in Purkinje cells in the
CC       brain. {ECO:0000269|PubMed:19371731}.
CC   -!- INDUCTION: By phenylethyl alcohol (PEA) in the olfactory sensory
CC       epithelium. {ECO:0000269|PubMed:17013923}.
CC   -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
CC       family. {ECO:0000255}.
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DR   EMBL; BC098624; AAH98624.1; -; mRNA.
DR   RefSeq; NP_001025123.1; NM_001029952.1.
DR   AlphaFoldDB; Q4KMC8; -.
DR   SMR; Q4KMC8; -.
DR   STRING; 7955.ENSDARP00000074827; -.
DR   PaxDb; Q4KMC8; -.
DR   GeneID; 792692; -.
DR   KEGG; dre:792692; -.
DR   CTD; 792692; -.
DR   ZFIN; ZDB-GENE-050706-128; aldoca.
DR   eggNOG; KOG1557; Eukaryota.
DR   InParanoid; Q4KMC8; -.
DR   OrthoDB; 799973at2759; -.
DR   PhylomeDB; Q4KMC8; -.
DR   UniPathway; UPA00109; UER00183.
DR   PRO; PR:Q4KMC8; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IBA:GO_Central.
DR   GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IBA:GO_Central.
DR   GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
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   Glycolysis; Lyase; Reference proteome; Schiff base.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P09117"
FT   CHAIN           2..364
FT                   /note="Fructose-bisphosphate aldolase C-A"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000389523"
FT   ACT_SITE        188
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P00883"
FT   ACT_SITE        230
FT                   /note="Schiff-base intermediate with dihydroxyacetone-P"
FT                   /evidence="ECO:0000250|UniProtKB:P09117"
FT   BINDING         56
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P09117"
FT   BINDING         147
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P09117"
FT   SITE            364
FT                   /note="Necessary for preference for fructose 1,6-
FT                   bisphosphate over fructose 1-phosphate"
FT                   /evidence="ECO:0000250|UniProtKB:P09117"
SQ   SEQUENCE   364 AA;  39870 MW;  7AB3C287EAF1862E CRC64;
     MTHQFPPLTT EQKKELHEIA LRIVSPGKGI LAADESIGSM GKRLNQIGVE NNEENRRLFR
     QVLFTADDRI DNCIGGVIFF HETLYQNSDD GVPFVKMIKD KGITIGIKVD KGVVPLPGTN
     GETATQGLDG LSERCAQYKK DGADFAKWRC VMKISETTPS NLCITENAKV LARYASICQQ
     HGIVPIVEPE ILPDGDHNLK RCQFVTERVL AAVYKAMFDH HVYLEGTLLK PNMVTPGHGC
     PTKYSAEEVA MATVTALRRT VPPAVTGVTF LSGGQSEEEA SINLSAINNC RLVKPWALTF
     SFGRALQASA LKTWRGQREN EAAATEEFIK RAEINSLASQ GKYTVCGDSS GATGLSHYLS
     SYAY