ACEA_ARATH
ID ACEA_ARATH Reviewed; 576 AA.
AC P28297; Q41948; Q9LSZ2;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Isocitrate lyase {ECO:0000303|PubMed:10805817};
DE Short=ICL {ECO:0000303|PubMed:10805817};
DE EC=4.1.3.1 {ECO:0000269|PubMed:10805817, ECO:0000269|PubMed:15272001};
DE AltName: Full=Isocitrase {ECO:0000305};
DE AltName: Full=Isocitratsysase {ECO:0000305};
GN Name=ICL {ECO:0000303|PubMed:10805817}; OrderedLocusNames=At3g21720;
GN ORFNames=MSD21.3 {ECO:0000312|EMBL:BAB02834.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE OF 1-450.
RC STRAIN=cv. Columbia;
RA Bernhard W.R., Matile P.;
RT "Isocitrate lyase gene from Arabidopsis thaliana.";
RL Submitted (FEB-1992) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 50-152.
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RX PubMed=8281187; DOI=10.1046/j.1365-313x.1993.04061051.x;
RA Hoefte H., Desprez T., Amselem J., Chiapello H., Rouze P., Caboche M.,
RA Moisan A., Jourjon M.-F., Charpenteau J.-L., Berthomieu P., Guerrier D.,
RA Giraudat J., Quigley F., Thomas F., Yu D.-Y., Mache R., Raynal M.,
RA Cooke R., Grellet F., Delseny M., Parmentier Y., de Marcillac G., Gigot C.,
RA Fleck J., Philipps G., Axelos M., Bardet C., Tremousaygue D., Lescure B.;
RT "An inventory of 1152 expressed sequence tags obtained by partial
RT sequencing of cDNAs from Arabidopsis thaliana.";
RL Plant J. 4:1051-1061(1993).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=10805817; DOI=10.1073/pnas.97.10.5669;
RA Eastmond P.J., Germain V., Lange P.R., Bryce J.H., Smith S.M., Graham I.A.;
RT "Postgerminative growth and lipid catabolism in oilseeds lacking the
RT glyoxylate cycle.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:5669-5674(2000).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=15272001; DOI=10.1074/jbc.m407380200;
RA Cornah J.E., Germain V., Ward J.L., Beale M.H., Smith S.M.;
RT "Lipid utilization, gluconeogenesis, and seedling growth in Arabidopsis
RT mutants lacking the glyoxylate cycle enzyme malate synthase.";
RL J. Biol. Chem. 279:42916-42923(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [9]
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=19246395; DOI=10.1073/pnas.0811329106;
RA Lingard M.J., Monroe-Augustus M., Bartel B.;
RT "Peroxisome-associated matrix protein degradation in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:4561-4566(2009).
CC -!- FUNCTION: Involved in storage lipid mobilization during the growth of
CC higher plant seedling. {ECO:0000269|PubMed:10805817,
CC ECO:0000269|PubMed:15272001}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-threo-isocitrate = glyoxylate + succinate;
CC Xref=Rhea:RHEA:13245, ChEBI:CHEBI:15562, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:36655; EC=4.1.3.1; Evidence={ECO:0000269|PubMed:10805817,
CC ECO:0000269|PubMed:15272001};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P9WKK7};
CC -!- PATHWAY: Carbohydrate metabolism; glyoxylate cycle; (S)-malate from
CC isocitrate: step 1/2. {ECO:0000305}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P28240}.
CC -!- SUBCELLULAR LOCATION: Glyoxysome {ECO:0000269|PubMed:19246395}.
CC -!- DEVELOPMENTAL STAGE: Expressed from 1 to 3 days after seed imbibition
CC (PubMed:10805817). Expressed from 1 to 5 days after seed imbibition (at
CC protein level). {ECO:0000269|PubMed:10805817,
CC ECO:0000269|PubMed:19246395}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant seedlings fail to establish into plantlets with
CC true leaves under low light or short day conditions.
CC {ECO:0000269|PubMed:10805817, ECO:0000269|PubMed:15272001}.
CC -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC Isocitrate lyase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB025634; BAB02834.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76544.1; -; Genomic_DNA.
DR EMBL; AY140000; AAM98142.1; -; mRNA.
DR EMBL; BT010397; AAQ56840.1; -; mRNA.
DR EMBL; M83534; AAA32823.2; -; Genomic_DNA.
DR EMBL; Z18772; CAA79248.1; -; mRNA.
DR RefSeq; NP_188809.2; NM_113067.4.
DR AlphaFoldDB; P28297; -.
DR SMR; P28297; -.
DR BioGRID; 7058; 5.
DR IntAct; P28297; 2.
DR STRING; 3702.AT3G21720.1; -.
DR PaxDb; P28297; -.
DR PRIDE; P28297; -.
DR ProteomicsDB; 244641; -.
DR EnsemblPlants; AT3G21720.1; AT3G21720.1; AT3G21720.
DR GeneID; 821726; -.
DR Gramene; AT3G21720.1; AT3G21720.1; AT3G21720.
DR KEGG; ath:AT3G21720; -.
DR Araport; AT3G21720; -.
DR TAIR; locus:2093049; AT3G21720.
DR eggNOG; KOG1260; Eukaryota.
DR HOGENOM; CLU_019214_2_2_1; -.
DR InParanoid; P28297; -.
DR OMA; LEKDWAE; -.
DR OrthoDB; 905115at2759; -.
DR PhylomeDB; P28297; -.
DR BioCyc; ARA:AT3G21720-MON; -.
DR BioCyc; MetaCyc:MON-1601; -.
DR UniPathway; UPA00703; UER00719.
DR PRO; PR:P28297; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P28297; baseline and differential.
DR Genevisible; P28297; AT.
DR GO; GO:0009514; C:glyoxysome; IDA:UniProtKB.
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; TAS:UniProtKB.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR CDD; cd00377; ICL_PEPM; 1.
DR Gene3D; 3.20.20.60; -; 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 PANTHER; PTHR21631; PTHR21631; 1.
DR Pfam; PF00463; ICL; 1.
DR PIRSF; PIRSF001362; Isocit_lyase; 1.
DR SUPFAM; SSF51621; SSF51621; 1.
DR TIGRFAMs; TIGR01346; isocit_lyase; 1.
DR PROSITE; PS00161; ISOCITRATE_LYASE; 1.
PE 1: Evidence at protein level;
KW Glyoxylate bypass; Glyoxysome; Lyase; Magnesium; Metal-binding; Peroxisome;
KW Reference proteome; Tricarboxylic acid cycle.
FT CHAIN 1..576
FT /note="Isocitrate lyase"
FT /id="PRO_0000068801"
FT MOTIF 574..576
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000305"
FT ACT_SITE 213
FT /note="Proton acceptor"
FT /evidence="ECO:0000305"
FT BINDING 104..106
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 175
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 214..215
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 250
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 437..441
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 472
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT CONFLICT 1..10
FT /note="MAASFSVPSM -> MIDKPNQ (in Ref. 4; AAA32823)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 576 AA; 64245 MW; 528F15CE04DD4A87 CRC64;
MAASFSVPSM IMEEEGRFEA EVAEVQTWWS SERFKLTRRP YTARDVVALR GHLKQGYASN
EMAKKLWRTL KSHQANGTAS RTFGALDPVQ VTMMAKHLDT IYVSGWQCSS THTSTNEPGP
DLADYPYDTV PNKVEHLFFA QQYHDRKQRE ARMSMSREER TKTPFVDYLK PIIADGDTGF
GGTTATVKLC KLFVERGAAG VHIEDQSSVT KKCGHMAGKV LVAVSEHINR LVAARLQFDV
MGTETVLVAR TDAVAATLIQ SNIDARDHQF ILGATNPSLR GKSLSSLLAE GMTVGKNGPA
LQSIEDQWLG SAGLMTFSEA VVQAIKRMNL NENEKNQRLS EWLTHARYEN CLSNEQGRVL
AAKLGVTDLF WDWDLPRTRE GFYRFQGSVA AAVVRGWAFA QIADIIWMET ASPDLNECTQ
FAEGIKSKTP EVMLAYNLSP SFNWDASGMT DQQMVEFIPR IARLGYCWQF ITLAGFHADA
LVVDTFAKDY ARRGMLAYVE RIQREERTHG VDTLAHQKWS GANYYDRYLK TVQGGISSTA
AMGKGVTEEQ FKESWTRPGA DGMGEGTSLV VAKSRM
