ID   ALDOC_DANRE             Reviewed;         363 AA.
AC   Q8JH70;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 46.
DE   RecName: Full=Fructose-bisphosphate aldolase C;
DE            EC=4.1.2.13;
DE   AltName: Full=Brain-type aldolase;
GN   Name=aldoc;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=12486526; DOI=10.1007/s00239-002-2363-8;
RA   Merritt T.J.S., Quattro J.M.;
RT   "Negative charge correlates with neural expression in vertebrate
RT   aldolase isozymes.";
RL   J. Mol. Evol. 55:674-683(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: D-fructose 1,6-bisphosphate = glycerone
CC       phosphate + D-glyceraldehyde 3-phosphate.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 4/4.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
CC       family.
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DR   EMBL; AF533647; AAN04478.1; -; mRNA.
DR   EMBL; BC053192; AAH53192.1; -; mRNA.
DR   IPI; IPI00490850; -.
DR   RefSeq; NP_919365.1; -.
DR   UniGene; Dr.19223; -.
DR   HSSP; P00883; 6ALD.
DR   SMR; Q8JH70; 3-363.
DR   PRIDE; Q8JH70; -.
DR   Ensembl; ENSDARG00000019702; Danio rerio.
DR   GeneID; 369193; -.
DR   KEGG; dre:369193; -.
DR   ZFIN; ZDB-GENE-030821-1; aldoc.
DR   HOGENOM; Q8JH70; -.
DR   HOVERGEN; Q8JH70; -.
DR   OMA; Q8JH70; ACPIKYT.
DR   BRENDA; 4.1.2.13; 96826.
DR   ArrayExpress; Q8JH70; -.
DR   Bgee; Q8JH70; -.
DR   GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:EC.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR000741; Aldolase_I.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1.
DR   PANTHER; PTHR11627; Aldolase_I; 1.
DR   Pfam; PF00274; Glycolytic; 1.
DR   ProDom; PD001128; Aldolase_I; 1.
DR   PROSITE; PS00158; ALDOLASE_CLASS_I; 1.
PE   2: Evidence at transcript level;
KW   Glycolysis; Lyase; Schiff base.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    363       Fructose-bisphosphate aldolase C.
FT                                /FTId=PRO_0000291612.
FT   ACT_SITE    230    230       Schiff-base intermediate with
FT                                dihydroxyacetone-P (By similarity).
FT   BINDING      56     56       Substrate (By similarity).
FT   BINDING     147    147       Substrate (By similarity).
FT   SITE        363    363       Necessary for preference for fructose
FT                                1,6-bisphosphate over fructose 1-
FT                                phosphate (By similarity).
SQ   SEQUENCE   363 AA;  39259 MW;  84D269B36579E6A0 CRC64;
     MTHQYPALTA EQKKELQDIA QRIVAPGKGI LAADESTGSM AKRLNPIGVE NTEENRRLYR
     QLLFSADERI DKCIGGVIFF HETLYQNTDD GTNFAQLIKD RGIVVGIKVD KGVVPLAGTN
     GETTTQGLDG LSERCAQYKK DGADFAKWRS VLKISDTTPS ELAIMENANV LARYASICQQ
     NGIVPIVEPE ILPDGEHDLK RCQYVTEKVL AACYKALSDH HVYLEGTLLK PNMVTAGHSC
     PTKYSSEEIA MATVTALRRT VPPAVSGVTF LSGGQSEEEA SVNLNSINNC PLAKPWPLTF
     SYGRALQASA LSAWRGAKSN EKAATEEFIK RAEANGLAAQ GKYVSSGTCG AAGQSLYVAN
     HAY
//