ALFC_CHLRE
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 03-AUG-2022, entry version 111.
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 STRING; 3055.EDO97897; -.
DR PaxDb; Q42690; -.
DR PRIDE; Q42690; -.
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 InParanoid; Q42690; -.
DR OMA; EVASMVW; -.
DR OrthoDB; 799973at2759; -.
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; IPR013785; Aldolase_TIM.
DR InterPro; IPR000741; FBA_I.
DR PANTHER; PTHR11627; PTHR11627; 1.
DR Pfam; PF00274; Glycolytic; 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; AAC60574/
FT 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; AAC60574/
FT 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
