ALFC2_PEA
ID ALFC2_PEA Reviewed; 349 AA.
AC Q01517;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Fructose-bisphosphate aldolase 2, chloroplastic;
DE EC=4.1.2.13;
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] OF 2-349, AND PROTEIN SEQUENCE OF 1-32.
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; M97477; AAA33643.1; -; Genomic_DNA.
DR PIR; S29048; S29048.
DR AlphaFoldDB; Q01517; -.
DR SMR; Q01517; -.
DR SABIO-RK; Q01517; -.
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.
FT CHAIN 1..349
FT /note="Fructose-bisphosphate aldolase 2, chloroplastic"
FT /id="PRO_0000216926"
FT ACT_SITE 177
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 219
FT /note="Schiff-base intermediate with dihydroxyacetone-P"
FT /evidence="ECO:0000250"
FT BINDING 47
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 349
FT /note="Necessary for preference for fructose 1,6-
FT bisphosphate over fructose 1-phosphate"
FT /evidence="ECO:0000250"
FT VARIANT 29
FT /note="A -> W (in strain: cv. Little Marvel)"
SQ SEQUENCE 349 AA; 37827 MW; E50715D246B5D7D1 CRC64;
GSYADELVKT AKTIASPGRG ILAMDESNAT CGKRLDSIGL ENTEANRQAW RTLLVTVPTL
GEYISGAILF EETLYQSTVD GRKIVDVLVE QNIIPGIKVD KGLVPLAGSN NESWCQGLDG
LASRSAAYYQ QGARFAKWRT VVSIPNGPSA LAVKEAAWGL ARYAAISQDN GLVPIVEPEI
LLDGEHGIDR TFEVAQKVWA EVFYYLAENN VQFEGILLKP SMVTPGAESK DKASPTKVAE
YTLNLLHRRI PPAVPGIMFL SGGQSEVEAT LNLNAMNKSP NPWHVSFSYA RALQNTALKT
WGGLPENVKA AQEALLFRAK SNSLAQLGKY IGDGESEEAK KDCCQGYSY
