ALFC1_PEA
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 03-AUG-2022, entry version 95.
DE RecName: Full=Fructose-bisphosphate aldolase 1, chloroplastic;
DE EC=4.1.2.13;
DE Flags: Precursor; Fragment;
OS Pisum sativum (Garden pea).
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 PRIDE; 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 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..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