ID   ALF2_LETCA              Reviewed;         364 AA.
AC   P53446;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   13-SEP-2023, entry version 83.
DE   RecName: Full=Fructose-bisphosphate aldolase, non-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 liver and also in brain and
CC       other tissues, except for the heart muscle.
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; D38619; BAA07607.1; -; mRNA.
DR   AlphaFoldDB; P53446; -.
DR   SMR; P53446; -.
DR   SABIO-RK; P53446; -.
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   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:SF80; FRUCTOSE-BISPHOSPHATE ALDOLASE; 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   Glycolysis; Lyase; Schiff base.
FT   CHAIN           1..364
FT                   /note="Fructose-bisphosphate aldolase, non-muscle type"
FT                   /id="PRO_0000216955"
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            364
FT                   /note="Necessary for preference for fructose 1,6-
FT                   bisphosphate over fructose 1-phosphate"
SQ   SEQUENCE   364 AA;  38952 MW;  1F495DB6AAA1A7E5 CRC64;
     MAALYPALTP EQKKELAEIA QRIVSNGKGI LAADESTGTM GKRLSAIKVE NVDENRRVYR
     QLLFSSDPSV TKAIGGVIFY EETLYQKTDD GTPFVKLIKD RGIVVGIKVD KGTVPLAGTD
     GESTTQGLDG LAERCARYKK DGADFAKWRC VLKISKNTPS ALAIAENANV LARYASICQQ
     NGLVPIVEPE ILPDGDHDLK TCQYVTEKVL AATYKALSDH HVYLEGSLLK PNMVTAGQAS
     KIRCSPQEVA MATVTALRRT VPSAVPGITF LSGGQSEEDA SLNLNAINQL PLERPWALSF
     SYGRALQASV LKAWAGAPAN IPAAKKEFEK RAAINGLAAQ GKYVPAGSSG SAASESLFIA
     NHNY
//