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Database: UniProt
Entry: A8JCY4_CHLRE
LinkDB: A8JCY4_CHLRE
Original site: A8JCY4_CHLRE 
ID   A8JCY4_CHLRE            Unreviewed;       391 AA.
AC   A8JCY4;
DT   04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT   04-DEC-2007, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   RecName: Full=Fructose-bisphosphate aldolase {ECO:0000256|ARBA:ARBA00013068, ECO:0000256|RuleBase:RU003994};
DE            EC=4.1.2.13 {ECO:0000256|ARBA:ARBA00013068, ECO:0000256|RuleBase:RU003994};
GN   ORFNames=CHLRE_01g006950v5 {ECO:0000313|EMBL:PNW87917.1};
OS   Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=3055 {ECO:0000313|EMBL:PNW87917.1, ECO:0000313|Proteomes:UP000006906};
RN   [1] {ECO:0000313|EMBL:PNW87917.1, ECO:0000313|Proteomes:UP000006906}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC-503 {ECO:0000313|Proteomes:UP000006906}, and CC-503 cw92 mt+
RC   {ECO:0000313|EMBL:PNW87917.1};
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.,
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).
RN   [2] {ECO:0000313|EMBL:PNW87917.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CC-503 cw92 mt+ {ECO:0000313|EMBL:PNW87917.1};
RG   Chlamydomonas Annotation Team;
RG   JGI Annotation Team;
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., Grigoriev I.V., Rokhsar D.S.;
RT   "WGS assembly of Chlamydomonas reinhardtii.";
RL   Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
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         Evidence={ECO:0000256|ARBA:ARBA00000441,
CC         ECO:0000256|RuleBase:RU003994};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 4/4.
CC       {ECO:0000256|ARBA:ARBA00004714}.
CC   -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
CC       family. {ECO:0000256|ARBA:ARBA00010387, ECO:0000256|RuleBase:RU003994}.
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DR   EMBL; CM008962; PNW87917.1; -; Genomic_DNA.
DR   EMBL; CM008962; PNW87918.1; -; Genomic_DNA.
DR   RefSeq; XP_001700318.1; XM_001700266.1.
DR   SMR; A8JCY4; -.
DR   STRING; 3055.A8JCY4; -.
DR   PaxDb; 3055-EDO98285; -.
DR   ProMEX; A8JCY4; -.
DR   EnsemblPlants; PNW87917; PNW87917; CHLRE_01g006950v5.
DR   EnsemblPlants; PNW87918; PNW87918; CHLRE_01g006950v5.
DR   GeneID; 5725868; -.
DR   Gramene; PNW87917; PNW87917; CHLRE_01g006950v5.
DR   Gramene; PNW87918; PNW87918; CHLRE_01g006950v5.
DR   KEGG; cre:CHLRE_01g006950v5; -.
DR   eggNOG; KOG1557; Eukaryota.
DR   HOGENOM; CLU_031243_0_0_1; -.
DR   OrthoDB; 3595068at2759; -.
DR   UniPathway; UPA00109; UER00183.
DR   Proteomes; UP000006906; Chromosome 1.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IBA:GO_Central.
DR   GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IBA:GO_Central.
DR   GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
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:SF70; FRUCTOSE-BISPHOSPHATE ALDOLASE; 1.
DR   Pfam; PF00274; Glycolytic; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   PROSITE; PS00158; ALDOLASE_CLASS_I; 1.
PE   3: Inferred from homology;
KW   Glycolysis {ECO:0000256|RuleBase:RU003994};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU003994};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006906};
KW   Schiff base {ECO:0000256|ARBA:ARBA00023270}.
SQ   SEQUENCE   391 AA;  42063 MW;  BF770B0D7E71B61D CRC64;
     MQAKMQTRAV SGRAAARSRV STTKVVCRAL NSMESPYAEE LKKTAAYISQ KGKGILASDE
     SNATTGKRLE SVGVENTEDN RRAWRELLYT APGLGQYISG AIMFEETLYQ KARDGRQFVD
     ILLAQGIYPG IKVDTGLQIL PGDKGETTTQ GLDGLADRCK AYRKQGARFA KWRAVVKIGE
     AGCPSTTAVL ENAHGLARYA QICQENGLVP IVEPEVTLGP GDYSIEETAF WSERVYSHTM
     RLLNEYGVVL EGILLKPNMC LPGLDAPVAS PQLVAEVTTR TMMRSIPPAV PGIHFLSGGM
     SEEESTLNLQ ALNEACPNAP WALTFSYGRA LQSSTLKTWA GKESNWAAAQ DILLKLAKAN
     SEASTGSFKG PHPVPGGGRI LQALRTGGAG K
//
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