ID   ALFC_CHLRE              Reviewed;         377 AA.
AC   Q42690; A8JE10; Q36725;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   22-FEB-2012, sequence version 2.
DT   24-JAN-2024, entry version 117.
DE   RecName: Full=Fructose-bisphosphate aldolase 1, chloroplastic;
DE            EC=4.1.2.13;
DE   Flags: Precursor;
GN   Name=ALDCHL; ORFNames=CHLREDRAFT_24459;
OS   Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=3055;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   PubMed=8053679; DOI=10.1006/abbi.1994.1374;
RA   Schnarrenberger C., Pelzer-Reith B., Yatsuki H., Freund S., Jacobshagen S.,
RA   Hori K.;
RT   "Expression and sequence of the only detectable aldolase in Chlamydomonas
RT   reinhardtii.";
RL   Arch. Biochem. Biophys. 313:173-178(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7565612; DOI=10.1007/bf02191648;
RA   Pelzer-Reith B., Freund S., Schnarrenberger C., Yatsuki H., Hori K.;
RT   "The plastid aldolase gene from Chlamydomonas reinhardtii: intron/exon
RT   organization, evolution, and promoter structure.";
RL   Mol. Gen. Genet. 248:481-486(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC-503;
RX   PubMed=17932292; DOI=10.1126/science.1143609;
RA   Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J.,
RA   Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L.,
RA   Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H.,
RA   Kapitonov V.V., Ren Q., Ferris P., Lindquist E., Shapiro H., Lucas S.M.,
RA   Grimwood J., Schmutz J., Cardol P., Cerutti H., Chanfreau G., Chen C.L.,
RA   Cognat V., Croft M.T., Dent R., Dutcher S., Fernandez E., Fukuzawa H.,
RA   Gonzalez-Ballester D., Gonzalez-Halphen D., Hallmann A., Hanikenne M.,
RA   Hippler M., Inwood W., Jabbari K., Kalanon M., Kuras R., Lefebvre P.A.,
RA   Lemaire S.D., Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L.,
RA   Mittag M., Mittelmeier T., Moroney J.V., Moseley J., Napoli C.,
RA   Nedelcu A.M., Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G.J.,
RA   Purton S., Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L.,
RA   Schroda M., Stern D., Umen J., Willows R., Wilson N., Zimmer S.L.,
RA   Allmer J., Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C.,
RA   Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J.,
RA   Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P.,
RA   Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P., Jorgensen R.,
RA   Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T., Brokstein P.,
RA   Dubchak I., Goodstein D., Hornick L., Huang Y.W., Jhaveri J., Luo Y.,
RA   Martinez D., Ngau W.C., Otillar B., Poliakov A., Porter A., Szajkowski L.,
RA   Werner G., Zhou K., Grigoriev I.V., Rokhsar D.S., Grossman A.R.;
RT   "The Chlamydomonas genome reveals the evolution of key animal and plant
RT   functions.";
RL   Science 318:245-250(2007).
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; X69969; CAA49590.1; -; mRNA.
DR   EMBL; S72951; AAC60574.1; -; Genomic_DNA.
DR   EMBL; X85495; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; DS496165; EDO97897.1; -; Genomic_DNA.
DR   PIR; S48639; S48639.
DR   RefSeq; XP_001700659.1; XM_001700607.1.
DR   PDB; 7B2N; X-ray; 2.36 A; A/B/C/D/E/F/G/H=28-377.
DR   PDBsum; 7B2N; -.
DR   AlphaFoldDB; Q42690; -.
DR   SMR; Q42690; -.
DR   PaxDb; 3055-EDO97897; -.
DR   ProMEX; Q42690; -.
DR   EnsemblPlants; PNW83518; PNW83518; CHLRE_05g234550v5.
DR   EnsemblPlants; PNW83519; PNW83519; CHLRE_05g234550v5.
DR   GeneID; 5726208; -.
DR   Gramene; PNW83518; PNW83518; CHLRE_05g234550v5.
DR   Gramene; PNW83519; PNW83519; CHLRE_05g234550v5.
DR   KEGG; cre:CHLRE_05g234550v5; -.
DR   eggNOG; KOG1557; Eukaryota.
DR   HOGENOM; CLU_031243_0_0_1; -.
DR   OMA; EVASMVW; -.
DR   OrthoDB; 3595068at2759; -.
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; IPR013785; Aldolase_TIM.
DR   InterPro; IPR000741; FBA_I.
DR   NCBIfam; NF033379; FrucBisAld_I; 1.
DR   PANTHER; PTHR11627; FRUCTOSE-BISPHOSPHATE ALDOLASE; 1.
DR   PANTHER; PTHR11627:SF75; FRUCTOSE-BISPHOSPHATE ALDOLASE 3, CHLOROPLASTIC; 1.
DR   Pfam; PF00274; Glycolytic; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Chloroplast; Glycolysis; Lyase; Plastid; Schiff base;
KW   Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..377
FT                   /note="Fructose-bisphosphate aldolase 1, chloroplastic"
FT                   /id="PRO_0000001111"
FT   ACT_SITE        204
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        246
FT                   /note="Schiff-base intermediate with dihydroxyacetone-P"
FT                   /evidence="ECO:0000250"
FT   BINDING         74
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         164
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            377
FT                   /note="Necessary for preference for fructose 1,6-
FT                   bisphosphate over fructose 1-phosphate"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        16..27
FT                   /note="AGRSRRAVVVRA -> LAALAAPSLCAP (in Ref. 1;
FT                   AAC60574/CAA49590)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        133..139
FT                   /note="LSNTNGE -> CPTPTM (in Ref. 1; AAC60574/CAA49590)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        148..152
FT                   /note="LDKRC -> WTSA (in Ref. 1; AAC60574/CAA49590)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        178..183
FT                   /note="IAARDC -> MLPRL (in Ref. 1; AAC60574/CAA49590)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        240..241
FT                   /note="FE -> LQ (in Ref. 1; AAC60574/CAA49590)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        274..280
FT                   /note="RRRVPPA -> AARAPP (in Ref. 1; AAC60574/CAA49590)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        321
FT                   /note="Q -> T (in Ref. 1; AAC60574/CAA49590)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        330..334
FT                   /note="GKPEN -> ASPRT (in Ref. 1; AAC60574/CAA49590)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        338..346
FT                   /note="AQAALLKRA -> PRLAAQAR (in Ref. 1;
FT                   AAC60574/CAA49590)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        374
FT                   /note="G -> GKG (in Ref. 1; AAC60574/CAA49590)"
FT                   /evidence="ECO:0000305"
FT   HELIX           31..41
FT                   /evidence="ECO:0007829|PDB:7B2N"
FT   STRAND          47..51
FT                   /evidence="ECO:0007829|PDB:7B2N"
FT   HELIX           55..63
FT                   /evidence="ECO:0007829|PDB:7B2N"
FT   TURN            64..66
FT                   /evidence="ECO:0007829|PDB:7B2N"
FT   HELIX           71..82
FT                   /evidence="ECO:0007829|PDB:7B2N"
FT   HELIX           87..89
FT                   /evidence="ECO:0007829|PDB:7B2N"
FT   STRAND          91..96
FT                   /evidence="ECO:0007829|PDB:7B2N"
FT   HELIX           100..102
FT                   /evidence="ECO:0007829|PDB:7B2N"
FT   HELIX           111..117
FT                   /evidence="ECO:0007829|PDB:7B2N"
FT   STRAND          121..125
FT                   /evidence="ECO:0007829|PDB:7B2N"
FT   STRAND          130..132
FT                   /evidence="ECO:0007829|PDB:7B2N"
FT   STRAND          136..138
FT                   /evidence="ECO:0007829|PDB:7B2N"
FT   STRAND          140..142
FT                   /evidence="ECO:0007829|PDB:7B2N"
FT   HELIX           148..157
FT                   /evidence="ECO:0007829|PDB:7B2N"
FT   STRAND          162..169
FT                   /evidence="ECO:0007829|PDB:7B2N"
FT   HELIX           177..197
FT                   /evidence="ECO:0007829|PDB:7B2N"
FT   STRAND          200..207
FT                   /evidence="ECO:0007829|PDB:7B2N"
FT   HELIX           215..235
FT                   /evidence="ECO:0007829|PDB:7B2N"
FT   HELIX           240..242
FT                   /evidence="ECO:0007829|PDB:7B2N"
FT   HELIX           262..274
FT                   /evidence="ECO:0007829|PDB:7B2N"
FT   STRAND          283..287
FT                   /evidence="ECO:0007829|PDB:7B2N"
FT   HELIX           293..302
FT                   /evidence="ECO:0007829|PDB:7B2N"
FT   STRAND          309..317
FT                   /evidence="ECO:0007829|PDB:7B2N"
FT   HELIX           318..328
FT                   /evidence="ECO:0007829|PDB:7B2N"
FT   HELIX           332..334
FT                   /evidence="ECO:0007829|PDB:7B2N"
FT   HELIX           335..353
FT                   /evidence="ECO:0007829|PDB:7B2N"
SQ   SEQUENCE   377 AA;  40985 MW;  76B5BED0C422E77C CRC64;
     MALMMKSSAS LKAVSAGRSR RAVVVRAGKY DEELIKTAGT VASKGRGILA MDESNATCGK
     RLDSIGVENT EENRRAYREL LVTAPGLGQY ISGAILFEET LYQSTASGKK FVDVMKEQNI
     VPGIKVDKGL VPLSNTNGES WCMGLDGLDK RCAEYYKAGA RFAKWRSVVS IPHGPSIIAA
     RDCAYGLARY AAIAQNAGLV PIVEPEVLLD GEHDIDRCLE VQEAIWAETF KYMADNKVMF
     EGILLKPAMV TPGADCKNKA GPAKVAEYTL KMLRRRVPPA VPGIMFLSGG QSELESTLNL
     NAMNQSPNPW HVSFSYARAL QNTVLKTWQG KPENVQAAQA ALLKRAKANS DAQQGKYDAT
     TEGKEAAQGM YEKGYVY
//