ID   ALDOB_SPAAU             Reviewed;         364 AA.
AC   P53447;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Fructose-bisphosphate aldolase B;
DE            EC=4.1.2.13;
DE   AltName: Full=Liver-type aldolase;
GN   Name=aldob;
OS   Sparus aurata (Gilthead sea bream).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Spariformes; Sparidae; Sparus.
OX   NCBI_TaxID=8175;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=7632737; DOI=10.1016/0167-4781(95)00096-y;
RA   Llewellyn L., Ramsurn V.P., Sweeney G.E., Wigham T., Santos C.R.,
RA   Power D.M.;
RT   "Cloning and characterisation of a fish aldolase B gene.";
RL   Biochim. Biophys. Acta 1263:75-78(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   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome, centriolar satellite {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
CC       family. {ECO:0000305}.
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DR   EMBL; X82278; CAA57729.1; -; mRNA.
DR   PIR; S57270; S48810.
DR   AlphaFoldDB; P53447; -.
DR   SMR; P53447; -.
DR   UniPathway; UPA00109; UER00183.
DR   Proteomes; UP000472265; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
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   Cytoplasm; Cytoskeleton; Glycolysis; Lyase; Reference proteome;
KW   Schiff base.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..364
FT                   /note="Fructose-bisphosphate aldolase B"
FT                   /id="PRO_0000216946"
FT   ACT_SITE        188
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
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"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   364 AA;  39645 MW;  EA7A5E75AF7D72FA CRC64;
     MTHQFPSLSP EQKKELSDIA QRIVAPGKGI LAADESTGTM GKRFQNINVE NIEENRRCFR
     DILFSTDASI ANCVGGIIFF HETLYQKSSN GKLFPQVVKE KGIVVGIKVD KGTAPLMGTD
     KETTTQGLDG LSERCAQYKK DGCDFAKWRC VLKISDGCPF ALAIAENANV LARYASICQM
     NGLVPIVEPE ILPDGDHDLQ RCQYATEKVL AAVYKALSDH HVYLEGTLLK PNMVTPGHSC
     PKKFTPQEVA MATVTALRRT VPASVPGICF LSGGQSEEEA SIHLNAINQV PLHRPWKLTF
     SYGRALQASA LAAWQGKDAN KAATQQVFVT RAKINGLASK GEYKPSGSAD QASQQSLYTA
     SYVY