ID   A0A0L6VDB8_9BASI        Unreviewed;       565 AA.
AC   A0A0L6VDB8;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Isocitrate lyase {ECO:0000256|PIRNR:PIRNR001362};
GN   Name=aceA {ECO:0000313|EMBL:KNZ58771.1};
GN   ORFNames=VP01_1865g4 {ECO:0000313|EMBL:KNZ58771.1};
OS   Puccinia sorghi.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX   NCBI_TaxID=27349 {ECO:0000313|EMBL:KNZ58771.1, ECO:0000313|Proteomes:UP000037035};
RN   [1] {ECO:0000313|EMBL:KNZ58771.1, ECO:0000313|Proteomes:UP000037035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RO10H11247 {ECO:0000313|EMBL:KNZ58771.1,
RC   ECO:0000313|Proteomes:UP000037035};
RA   Rochi L., Burguener G., Darino M., Turjanski A., Kreff E., Dieguez M.J.,
RA   Sacco F.;
RT   "Next Generation Sequencing and Analysis of the Genome of Puccinia sorghi L
RT   Schw, the Causal Agent of Maize Common Rust.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC       Isocitrate lyase family. {ECO:0000256|ARBA:ARBA00005704,
CC       ECO:0000256|PIRNR:PIRNR001362}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KNZ58771.1}.
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DR   EMBL; LAVV01006687; KNZ58771.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L6VDB8; -.
DR   STRING; 27349.A0A0L6VDB8; -.
DR   VEuPathDB; FungiDB:VP01_1865g4; -.
DR   OrthoDB; 983054at2759; -.
DR   Proteomes; UP000037035; Unassembled WGS sequence.
DR   GO; GO:0004451; F:isocitrate lyase activity; IEA:InterPro.
DR   GO; GO:0046421; F:methylisocitrate lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   CDD; cd00377; ICL_PEPM; 1.
DR   Gene3D; 1.10.10.850; -; 1.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 2.
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; ISOCITRATE LYASE/MALATE SYNTHASE; 1.
DR   PANTHER; PTHR21631:SF13; MITOCHONDRIAL 2-METHYLISOCITRATE LYASE ICL2; 1.
DR   Pfam; PF00463; ICL; 2.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   PROSITE; PS00161; ISOCITRATE_LYASE; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR001362};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037035}.
FT   REGION          479..500
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   565 AA;  62938 MW;  1F2554F9EA5E4A8F CRC64;
     MTGTQADKLA ELTRSIQDWF DSPRFANTQR SYSAELIATK RGSLPVHQDS YANLQARKLR
     QLLAQAKETQ QPVMTMGALD PVQQSQMAHH LPIVYVSGWA ASSTFVPGTH EVGPDLADYP
     YHTVPTAVQR LVKAQQLHER KEWDRQFSKS ATAREPVEYL KPIIADGDNG HGGLSTVMKL
     AKAFGEAGVA GVHFEDQLVG GKKCGHQAGK VLVPTCEHLS RLTAARMQWD IMGLETLLIG
     RTDAESAKLI SSDHDPRDHP FILGIQSHPQ KPHTIPLAEE IIIAEERGAS ADEINEIEKR
     WTESLSDEHL KNIKCPRINI PNTCRRSSDL IGWSAQSART REGYYRFNGC LQAAVNRALK
     FSPLSDLVWI ETKEPNLRIA QSISSQILHH FPTQFTVFFF FFFWGGGGVD VICRNLVYNL
     SPSFNWSAHG FSEQALKSFV WDLSGLGFNL QLISESREAG SQQDFFFLVQ MKRDRDKGNL
     QKDWGGGDST TGAKLQGGGH AWVRETDPGG GESDRVRCVE APAVERLGVH RRDLERLRLP
     SPHLSLSSVD GCAHLLTLGV WFLFI
//