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Database: UniProt
Entry: A8J244_CHLRE
LinkDB: A8J244_CHLRE
Original site: A8J244_CHLRE 
ID   A8J244_CHLRE            Unreviewed;       417 AA.
AC   A8J244;
DT   04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT   04-DEC-2007, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   RecName: Full=isocitrate lyase {ECO:0000256|ARBA:ARBA00012909};
DE            EC=4.1.3.1 {ECO:0000256|ARBA:ARBA00012909};
GN   ORFNames=CHLRE_06g282800v5 {ECO:0000313|EMBL:PNW82533.1};
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:PNW82533.1, ECO:0000313|Proteomes:UP000006906};
RN   [1] {ECO:0000313|EMBL:PNW82533.1, ECO:0000313|Proteomes:UP000006906}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC-503 {ECO:0000313|Proteomes:UP000006906};
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).
CC   -!- FUNCTION: Involved in storage lipid mobilization during the growth of
CC       higher plant seedling. {ECO:0000256|ARBA:ARBA00003575}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR001362-3};
CC       Note=Can also use Mn(2+) ion. {ECO:0000256|PIRSR:PIRSR001362-3};
CC   -!- PATHWAY: Carbohydrate metabolism; glyoxylate cycle; (S)-malate from
CC       isocitrate: step 1/2. {ECO:0000256|ARBA:ARBA00004793}.
CC   -!- SUBCELLULAR LOCATION: Glyoxysome {ECO:0000256|ARBA:ARBA00004130}.
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DR   EMBL; CM008967; PNW82533.1; -; Genomic_DNA.
DR   RefSeq; XP_001695331.1; XM_001695279.1.
DR   AlphaFoldDB; A8J244; -.
DR   SMR; A8J244; -.
DR   STRING; 3055.A8J244; -.
DR   PaxDb; 3055-EDP01589; -.
DR   ProMEX; A8J244; -.
DR   EnsemblPlants; PNW82533; PNW82533; CHLRE_06g282800v5.
DR   GeneID; 5720950; -.
DR   Gramene; PNW82533; PNW82533; CHLRE_06g282800v5.
DR   KEGG; cre:CHLRE_06g282800v5; -.
DR   eggNOG; KOG1260; Eukaryota.
DR   HOGENOM; CLU_019214_2_0_1; -.
DR   InParanoid; A8J244; -.
DR   OMA; IYMNGSG; -.
DR   OrthoDB; 983054at2759; -.
DR   UniPathway; UPA00703; UER00719.
DR   Proteomes; UP000006906; Chromosome 6.
DR   ExpressionAtlas; A8J244; baseline and differential.
DR   GO; GO:0009514; C:glyoxysome; IBA:GO_Central.
DR   GO; GO:0004451; F:isocitrate lyase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   CDD; cd00377; ICL_PEPM; 1.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   InterPro; IPR039556; ICL/PEPM.
DR   InterPro; IPR006254; Isocitrate_lyase.
DR   InterPro; IPR018523; Isocitrate_lyase_ph_CS.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   NCBIfam; TIGR01346; isocit_lyase; 1.
DR   PANTHER; PTHR21631:SF3; BIFUNCTIONAL GLYOXYLATE CYCLE PROTEIN; 1.
DR   PANTHER; PTHR21631; ISOCITRATE LYASE/MALATE SYNTHASE; 1.
DR   Pfam; PF00463; ICL; 2.
DR   PIRSF; PIRSF001362; Isocit_lyase; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   PROSITE; PS00161; ISOCITRATE_LYASE; 1.
PE   4: Predicted;
KW   Glyoxylate bypass {ECO:0000256|ARBA:ARBA00022435};
KW   Glyoxysome {ECO:0000256|ARBA:ARBA00022453};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR001362-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001362-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006906};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT   ACT_SITE        178
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-1"
FT   BINDING         79..81
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         140
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
FT   BINDING         179..180
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         215
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         300..304
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT   BINDING         334
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
SQ   SEQUENCE   417 AA;  45749 MW;  E10317B47051EECB CRC64;
     MASNGAAPDR WSNVKRVYTR QDVEKLRGSI KIEYTLARLG AERFWNLLHT EDYVPALGAM
     TGGQAVEMVA AGLKAIYLSG WQVAADANSA SQTYPDQSLY PVDSVPRVVS RINNAFQRMD
     QMQHSEGRGD TYWFAPIVAD AEAGFGGNLN AYELMKALIE AGASCVHFED QLASAKKCGH
     LGGKVLVPTK EFVQKLTAAR LAADVMDVPT LIIARTDALG AYLLTSDADE YDKPFMTGER
     TAEGFYCVRG GIDAAIARGL AYAPYADLVW FETSEPSMEE AKKFAAAIHA QYPGKLLAYN
     CSPSFNWKKK LSDDEIAKFQ KTLGSLGYKF QFITLAGFHS LNYGMFSLAR DYASRGMSAY
     AQLQEAEFAS EKQGYRATTH QKFVGTGYFD LVSTVITQGT SSTNALKGST EEEQFHH
//
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