ACEA_BRANA
ID ACEA_BRANA Reviewed; 576 AA.
AC P25248; O04910;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Isocitrate lyase {ECO:0000250|UniProtKB:P28297};
DE Short=ICL {ECO:0000250|UniProtKB:P28297};
DE EC=4.1.3.1 {ECO:0000250|UniProtKB:P28297};
DE AltName: Full=Isocitrase {ECO:0000250|UniProtKB:P28297};
DE AltName: Full=Isocitratsysase {ECO:0000250|UniProtKB:P28297};
OS Brassica napus (Rape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3708;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX PubMed=2535504; DOI=10.2307/3869009;
RA Comai L., Dietrich R.A., Maslyar D.J., Baden C.S., Harada J.J.;
RT "Coordinate expression of transcriptionally regulated isocitrate lyase and
RT malate synthase genes in Brassica napus L.";
RL Plant Cell 1:293-300(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8479425; DOI=10.1007/bf00279545;
RA Zhang J.Z., Gomez-Pedrozo M., Baden C.S., Harada J.J.;
RT "Two classes of isocitrate lyase genes are expressed during late embryogeny
RT and postgermination in Brassica napus L.";
RL Mol. Gen. Genet. 238:177-184(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Global; TISSUE=Cotyledon;
RA Olesen C., Thomsen K.K., Svendsen I., Brandt A.;
RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in storage lipid mobilization during the growth of
CC higher plant seedling. {ECO:0000250|UniProtKB:P28297}.
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;
CC Evidence={ECO:0000250|UniProtKB:P28297};
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:0000250|UniProtKB:P28297}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P28297}.
CC -!- SUBCELLULAR LOCATION: Glyoxysome {ECO:0000250|UniProtKB:P28297}.
CC -!- DEVELOPMENTAL STAGE: Expressed maximally during postgerminative growth.
CC {ECO:0000269|PubMed:2535504}.
CC -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC Isocitrate lyase family. {ECO:0000305}.
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DR EMBL; L08482; AAA32992.1; -; Genomic_DNA.
DR EMBL; Y13356; CAA73792.1; -; mRNA.
DR PIR; JQ1105; WZRPI.
DR RefSeq; NP_001302775.1; NM_001315846.1.
DR AlphaFoldDB; P25248; -.
DR SMR; P25248; -.
DR GeneID; 106389063; -.
DR KEGG; bna:106389063; -.
DR UniPathway; UPA00703; UER00719.
DR GO; GO:0009514; C:glyoxysome; IEA:UniProtKB-SubCell.
DR GO; GO:0004451; F:isocitrate lyase activity; IEA:UniProtKB-EC.
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; -; 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 2: Evidence at transcript level;
KW Glyoxylate bypass; Glyoxysome; Lyase; Magnesium; Metal-binding; Peroxisome;
KW Tricarboxylic acid cycle.
FT CHAIN 1..576
FT /note="Isocitrate lyase"
FT /id="PRO_0000068802"
FT MOTIF 574..576
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 213
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
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 75
FT /note="A -> V (in Ref. 3; CAA73792)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="D -> G (in Ref. 3; CAA73792)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="A -> P (in Ref. 3; CAA73792)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="S -> N (in Ref. 3; CAA73792)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="N -> T (in Ref. 3; CAA73792)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="N -> I (in Ref. 3; CAA73792)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 576 AA; 64326 MW; 81A87701A4ACC350 CRC64;
MAASFSVPSM IMEEEGRFEA EVAEVQTWWS SERFKLTRRP YTARDVVALR GHLKQGYASN
EMAKKLWRTL KSHQANGTAS RTFGALDPVQ VTMMAKHLDT IYVSGWQCSS THTSTNEPGP
DLADYPYDTV PNKVEHLFFA QQYHDRKQRE ARMSMSREER AKTPFVDYLK PIIADGDTGF
GGTTATVKLC KLFVERGAAG VHIEDQSSVT KKCGHMAGKV LVAVSEHINR LVAARLQFDV
MGTETVLVAR TDAVAATLIQ SNIDSRDHQF ILGVTNPSLR GKSLSSLLAE GMAVGNNGPA
LQAIEDQWLS SARLMTFSDA VVEALKRMNL SENEKSRRVN EWLNHARYEN CLSNEQGREL
AAKLGVTDLF WDWDLPRTRE GFYRFQGSVT AAVVRGWAFA QIADLIWMET ASPDLNECTQ
FAEGVKSKTP EVMLAYNLSP SFNWDASGMT DQQMMEFIPR IARLGYCWQF ITLAGFHADA
LVVDTFAKDY ARRGMLAYVE RIQREERSNG VDTLAHQKWS GANYYDRYLK TVQGGISSTA
AMGKGVTEEQ FKETWTRPGA AGMGEGTSLV VAKSRM
