ID   ALF1_LETCA              Reviewed;         363 AA.
AC   P53445;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Fructose-bisphosphate aldolase, muscle type;
DE            EC=4.1.2.13;
OS   Lethenteron camtschaticum (Japanese lamprey) (Lampetra japonica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata;
OC   Hyperoartia; Petromyzontiformes; Petromyzontidae; Lethenteron.
OX   NCBI_TaxID=980415;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=7629020; DOI=10.1093/oxfordjournals.jbchem.a124742;
RA   Zhang R., Yatsuki H., Kusakabe T., Iwabe N., Miyata T., Imai T.,
RA   Yoshida M., Hori K.;
RT   "Structures of cDNAs encoding the muscle-type and non-muscle-type isozymes
RT   of lamprey fructose bisphosphate aldolases and the evolution of aldolase
RT   genes.";
RL   J. Biochem. 117:545-553(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. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed mainly in the skeletal muscle, heart
CC       muscle, brain, and some other tissues, but probably not in liver.
CC       {ECO:0000269|PubMed:7629020}.
CC   -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
CC       family. {ECO:0000305}.
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DR   EMBL; D38620; BAA07608.1; -; mRNA.
DR   AlphaFoldDB; P53445; -.
DR   SMR; P53445; -.
DR   SABIO-RK; P53445; -.
DR   UniPathway; UPA00109; UER00183.
DR   GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
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; Schiff base.
FT   CHAIN           1..363
FT                   /note="Fructose-bisphosphate aldolase, muscle type"
FT                   /id="PRO_0000216954"
FT   ACT_SITE        230
FT                   /note="Schiff-base intermediate with dihydroxyacetone-P"
FT                   /evidence="ECO:0000250"
FT   BINDING         56
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         147
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            363
FT                   /note="Necessary for preference for fructose 1,6-
FT                   bisphosphate over fructose 1-phosphate"
SQ   SEQUENCE   363 AA;  39239 MW;  15BC9A40A7FB9EFC CRC64;
     MSPHFPALTP DQKKELADIA QRIVASGKGI LAADESVGTM GKRLTQIGLE NTDEHRRFYR
     QLLFTTDPSI KEHIGGIIFF HETMYQKTDG GVPFVKLVKD NGILVGIKVD KGVVPLAGTN
     GEGTTQGLDG LAERCAQYKK DGADFAKWRC VLKISPNTPS RLSIVENANV LARYATICQQ
     NGLVPIVEPE ILPDGDHDLK TCQYITEKVL AATYKALSDH HVYLEGTLLK PNMVTVGTAA
     PASTRPEQVA MATLTALRRT VPPAVPGITF LSGGQSEEDA SIHLNAINKL HLIKPWALTF
     SYGRALQASV LKAWGGKKEN LKAAQDELMR RAKINGQASK GEYKPTGTGA AAGESLFVAN
     HAY