ID   ALFC1_PEA               Reviewed;         356 AA.
AC   Q01516;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   27-MAR-2024, entry version 101.
DE   RecName: Full=Fructose-bisphosphate aldolase 1, chloroplastic;
DE            EC=4.1.2.13;
DE   Flags: Precursor; Fragment;
OS   Pisum sativum (Garden pea) (Lathyrus oleraceus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 7-38.
RC   STRAIN=cv. Little Marvel, and cv. Sparkle; TISSUE=Leaf;
RX   PubMed=1524427; DOI=10.1016/0003-9861(92)90112-a;
RA   Razdan K., Heinrikson R.L., Zurcher-Neely H., Morris P.W., Anderson L.E.;
RT   "Chloroplast and cytoplasmic enzymes: isolation and sequencing of cDNAs
RT   coding for two distinct pea chloroplast aldolases.";
RL   Arch. Biochem. Biophys. 298:192-197(1992).
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; M97476; AAA33642.1; -; Genomic_DNA.
DR   PIR; S29047; S29047.
DR   AlphaFoldDB; Q01516; -.
DR   SMR; Q01516; -.
DR   SABIO-RK; Q01516; -.
DR   UniPathway; UPA00109; UER00183.
DR   GO; GO:0009507; C:chloroplast; 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   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:SF16; FRUCTOSE-BISPHOSPHATE ALDOLASE, CHLOROPLASTIC; 1.
DR   Pfam; PF00274; Glycolytic; 1.
DR   SUPFAM; SSF51569; Aldolase; 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..6
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000269|PubMed:1524427"
FT   CHAIN           7..356
FT                   /note="Fructose-bisphosphate aldolase 1, chloroplastic"
FT                   /id="PRO_0000001110"
FT   ACT_SITE        183
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        225
FT                   /note="Schiff-base intermediate with dihydroxyacetone-P"
FT                   /evidence="ECO:0000250"
FT   BINDING         53
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         143
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            356
FT                   /note="Necessary for preference for fructose 1,6-
FT                   bisphosphate over fructose 1-phosphate"
FT                   /evidence="ECO:0000250"
FT   VARIANT         35
FT                   /note="A -> W (in strain: cv. Little Marvel)"
FT   NON_TER         1
SQ   SEQUENCE   356 AA;  38657 MW;  784A76C196D20941 CRC64;
     GLTIRAGSYA DELVKTAKTI ASPGRGILAM DESNATCGKR LASIGLENTE VNRQAWRTLL
     VTVPTLGEYI SGAILFEETL YQSTTDGRKI VDVLIEQNII PGIKVDKGLV PLAGSNDESW
     CQGLDGLASR SAAYYQQGAR FAKWRTVVSI PNGPSALAVK EAAWGLARYA AISQDNGLVP
     IVEPEILLDG EHGIDRTFEV AQKVWAEVFY YLAENNVQFE GILLKPSMVT PGAESKDKAS
     PTKVAEYTLN LLHRRIPPAV PGIMFLSGGQ SEVEATLNLN AMNKSPNPWH VSFSYARALQ
     NTALKTWGGL PENVKAAQEA LLFRAKSNSL AQLGKYYGDG ESEEAKKELF VKGYSY
//