ACEA_LEPMC
ID ACEA_LEPMC Reviewed; 537 AA.
AC Q86ZF1;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Isocitrate lyase {ECO:0000303|PubMed:12455691};
DE Short=ICL {ECO:0000305};
DE Short=Isocitrase {ECO:0000305};
DE Short=Isocitratase {ECO:0000305};
DE EC=4.1.3.1 {ECO:0000250|UniProtKB:P28240};
DE AltName: Full=Methylisocitrate lyase {ECO:0000250|UniProtKB:P28240};
DE Short=MICA {ECO:0000305};
DE EC=4.1.3.30 {ECO:0000250|UniProtKB:P28240};
DE AltName: Full=Threo-D(S)-isocitrate glyoxylate-lyase {ECO:0000305};
GN Name=ICL1 {ECO:0000303|PubMed:12455691};
OS Leptosphaeria maculans (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Leptosphaeria; Leptosphaeria maculans species complex.
OX NCBI_TaxID=5022;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, DISRUPTION PHENOTYPE, AND
RP FUNCTION.
RX PubMed=12455691; DOI=10.1128/ec.1.5.719-724.2002;
RA Idnurm A., Howlett B.J.;
RT "Isocitrate lyase is essential for pathogenicity of the fungus
RT Leptosphaeria maculans on canola (Brassica napus).";
RL Eukaryot. Cell 1:719-724(2002).
CC -!- FUNCTION: Catalyzes the formation of succinate and glyoxylate from
CC isocitrate, a key step of the glyoxylate cycle, which operates as an
CC anaplerotic route for replenishing the tricarboxylic acid cycle.
CC Required for growth on ethanol or acetate, but dispensable when
CC fermentable carbon sources are available. Acts also on 2-
CC methylisocitrate (By similarity). Plays an important role in plant
CC pathogenicity. {ECO:0000250|UniProtKB:P28240,
CC ECO:0000269|PubMed:12455691}.
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:P28240};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = pyruvate +
CC succinate; Xref=Rhea:RHEA:16809, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:57429; EC=4.1.3.30;
CC Evidence={ECO:0000250|UniProtKB:P28240};
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.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P28240}.
CC -!- SUBCELLULAR LOCATION: Glyoxysome {ECO:0000250|UniProtKB:P28299}.
CC -!- INDUCTION: Expression is induced by starvation and acetate.
CC {ECO:0000269|PubMed:12455691}.
CC -!- DISRUPTION PHENOTYPE: Leads to limited hyphal growth in plants and
CC extremely low germination rate of pycnidiospores.
CC {ECO:0000269|PubMed:12455691}.
CC -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC Isocitrate lyase family. {ECO:0000305}.
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DR EMBL; AY118108; AAM89498.1; -; Genomic_DNA.
DR AlphaFoldDB; Q86ZF1; -.
DR SMR; Q86ZF1; -.
DR UniPathway; UPA00703; UER00719.
DR PHI-base; PHI:261; -.
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:0046421; F:methylisocitrate lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-UniPathway.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.60; -; 1.
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..537
FT /note="Isocitrate lyase"
FT /id="PRO_0000068792"
FT ACT_SITE 206
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 97..99
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 168
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 207..208
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 243
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 423..427
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 457
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
SQ SEQUENCE 537 AA; 60126 MW; 681DDBDD138CAC92 CRC64;
MSHMDAEDAQ FQKEVAEVKQ WWNDSRWRYT KRTFTAEEIV SKRGNLKITY PSNSQSKKLW
NIVEHRFKNK DVSYTYGCLD PVMVTQMAKY LDTVYVSGWQ ASSTASSTDE PGPDLADYPY
TTVPNKVGHL FMAQLFHDRK QREERLTTPK ADRAKVANVD YLRPIIADAD TGHGGLTAIM
KLTKLFIEKG AAGIHIEDQA PGTKKCGHMA GKVLVPISEH INRLVAIRAQ ADIMGTDLLA
VARTDSEAAT LITSTIDPRD HYYIQGCTNP ALQPLSELMY AAEQSGKSGS ELQAIEDAWV
KEANLKLFHE AVVDTINAGV HVNKQELINQ FLEQSKGKSN AEARTIAQGL TGVDVYFNWD
AARTREGYYR YKGGCQCAIN RAIAYAPFCD MIWMESKLPD YAQAKEFADG VHAVWPEQKL
AYNLSPSFNW KAAMPRDEQE TYIQRLAQLG YCWQFITLAG LHQSALMADT FSKAYSKQGM
RAYGEIIQEP EAENKVDVLT HQKWSGANYV DNMLKMVSGG VSSTAAMGKG VTEDQFK
