ID   ALFC_SPIOL              Reviewed;         394 AA.
AC   P16096;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 3.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Fructose-bisphosphate aldolase, chloroplastic;
DE            EC=4.1.2.13;
DE   Flags: Precursor;
OS   Spinacia oleracea (Spinach).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX   NCBI_TaxID=3562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8425060; DOI=10.1007/bf00019948;
RA   Pelzer-Reith B., Penger A., Schnarrenberger C.;
RT   "Plant aldolase: cDNA and deduced amino-acid sequences of the chloroplast
RT   and cytosol enzyme from spinach.";
RL   Plant Mol. Biol. 21:331-340(1993).
RN   [2]
RP   PROTEIN SEQUENCE OF 47-64.
RX   PubMed=6420397; DOI=10.1016/s0021-9258(17)43558-7;
RA   Lebherz H.G., Leadbetter M.M., Bradshaw R.A.;
RT   "Isolation and characterization of the cytosolic and chloroplast forms of
RT   spinach leaf fructose diphosphate aldolase.";
RL   J. Biol. Chem. 259:1011-1017(1984).
RN   [3]
RP   IDENTIFICATION OF PROBABLE FRAMESHIFT.
RA   Bairoch A.;
RL   Unpublished observations (NOV-1995).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   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
CC       family. {ECO:0000305}.
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DR   EMBL; X66814; CAA47293.1; -; mRNA.
DR   PIR; S31090; ADSPAP.
DR   AlphaFoldDB; P16096; -.
DR   SMR; P16096; -.
DR   PRIDE; P16096; -.
DR   BioCyc; MetaCyc:MON-12899; -.
DR   BRENDA; 4.1.2.13; 5812.
DR   SABIO-RK; P16096; -.
DR   UniPathway; UPA00109; UER00183.
DR   GO; GO:0009507; C:chloroplast; IDA:AgBase.
DR   GO; GO:0032991; C:protein-containing complex; IDA:AgBase.
DR   GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IDA:AgBase.
DR   GO; GO:0043621; F:protein self-association; IDA:AgBase.
DR   GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; TAS:AgBase.
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   1: Evidence at protein level;
KW   Chloroplast; Direct protein sequencing; Glycolysis; Lyase; Plastid;
KW   Schiff base; Transit peptide.
FT   TRANSIT         1..46
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000269|PubMed:6420397"
FT   CHAIN           47..394
FT                   /note="Fructose-bisphosphate aldolase, chloroplastic"
FT                   /id="PRO_0000001113"
FT   ACT_SITE        223
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        265
FT                   /note="Schiff-base intermediate with dihydroxyacetone-P"
FT                   /evidence="ECO:0000250"
FT   BINDING         93
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         183
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            394
FT                   /note="Necessary for preference for fructose 1,6-
FT                   bisphosphate over fructose 1-phosphate"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        260..263
FT                   /note="EGSS -> RDP (in Ref. 1; CAA47293)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   394 AA;  42468 MW;  9D8A813E1636B274 CRC64;
     MASASLLKTS PVLDNPEFLK GQTLRIPSVA GVRFTPSGSS SLTVRASSYA DELVKTAKTV
     ASPGRGILAM DESNATCGKR LASIGLENTE ANRQAYRTLL ISAPGLGQYV SGAILFEETL
     YQSTTDGKKM VDVLIEQGIV PGIKVDKGWL PLPGSNDESW CQGLDGLACR SAAYYQQGAR
     FAKWRTVVSI PNGPSALAVK EAAWGLARYA AITQDNGLDP ILEPEIMLDG EHGIDRTFRV
     AQQVWAEVFF NLAENNVLLE GSSLKPSMVG PGALSARKGP PEQVADYPLK LLHRRRGPVV
     PGIMVLSGGQ SEVEATLNLN AMNQSPNPWH VSFSYARALQ NTCLKTWVEG QENVKAQDFA
     CAKSNSLAQL GKYTGEGESE ERKKDMFVKA TLTY