ID   ACEA_GIBZE              Reviewed;         546 AA.
AC   Q4HYR2; A0A0E0RVC2; V6RX12;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2005, sequence version 1.
DT   24-JAN-2024, entry version 108.
DE   RecName: Full=Isocitrate lyase {ECO:0000250|UniProtKB:P28240};
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:0000250|UniProtKB:P28240};
GN   ORFNames=FGRRES_09896, FGSG_09896;
OS   Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS   / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=229533;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX   PubMed=17823352; DOI=10.1126/science.1143708;
RA   Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA   Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA   Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA   Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA   Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA   Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA   Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA   Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT   "The Fusarium graminearum genome reveals a link between localized
RT   polymorphism and pathogen specialization.";
RL   Science 317:1400-1402(2007).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX   PubMed=20237561; DOI=10.1038/nature08850;
RA   Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA   Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA   Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA   Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA   Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA   Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA   Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA   Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA   Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA   Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA   Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA   Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT   "Comparative genomics reveals mobile pathogenicity chromosomes in
RT   Fusarium.";
RL   Nature 464:367-373(2010).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX   PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA   King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA   Hammond-Kosack K.E.;
RT   "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT   graminearum.";
RL   BMC Genomics 16:544-544(2015).
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. {ECO:0000250|UniProtKB:P28240}.
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   -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC       Isocitrate lyase family. {ECO:0000305}.
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DR   EMBL; DS231669; ESU16540.1; -; Genomic_DNA.
DR   EMBL; HG970332; CEF75197.1; -; Genomic_DNA.
DR   RefSeq; XP_011318802.1; XM_011320500.1.
DR   PDB; 5E9H; X-ray; 2.30 A; A/B=1-546.
DR   PDBsum; 5E9H; -.
DR   AlphaFoldDB; Q4HYR2; -.
DR   SMR; Q4HYR2; -.
DR   STRING; 229533.Q4HYR2; -.
DR   GeneID; 23556822; -.
DR   KEGG; fgr:FGSG_09896; -.
DR   VEuPathDB; FungiDB:FGRAMPH1_01G06785; -.
DR   eggNOG; KOG1260; Eukaryota.
DR   HOGENOM; CLU_019214_2_2_1; -.
DR   InParanoid; Q4HYR2; -.
DR   OrthoDB; 983054at2759; -.
DR   BRENDA; 4.1.3.1; 2428.
DR   UniPathway; UPA00703; UER00719.
DR   Proteomes; UP000070720; Chromosome 1.
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; 1.10.10.850; -; 1.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 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   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; 1.
DR   PIRSF; PIRSF001362; Isocit_lyase; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   PROSITE; PS00161; ISOCITRATE_LYASE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Glyoxylate bypass; Glyoxysome; Lyase; Magnesium;
KW   Metal-binding; Peroxisome; Reference proteome; Tricarboxylic acid cycle.
FT   CHAIN           1..546
FT                   /note="Isocitrate lyase"
FT                   /id="PRO_0000286157"
FT   ACT_SITE        215
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT   BINDING         106..108
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT   BINDING         177
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT   BINDING         216..217
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT   BINDING         252
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT   BINDING         432..436
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT   BINDING         466
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT   TURN            13..16
FT                   /evidence="ECO:0007829|PDB:5E9H"
FT   HELIX           17..31
FT                   /evidence="ECO:0007829|PDB:5E9H"
FT   HELIX           34..36
FT                   /evidence="ECO:0007829|PDB:5E9H"
FT   HELIX           45..49
FT                   /evidence="ECO:0007829|PDB:5E9H"
FT   HELIX           60..77
FT                   /evidence="ECO:0007829|PDB:5E9H"
FT   STRAND          82..86
FT                   /evidence="ECO:0007829|PDB:5E9H"
FT   HELIX           90..96
FT                   /evidence="ECO:0007829|PDB:5E9H"
FT   TURN            97..99
FT                   /evidence="ECO:0007829|PDB:5E9H"
FT   STRAND          103..105
FT                   /evidence="ECO:0007829|PDB:5E9H"
FT   HELIX           107..113
FT                   /evidence="ECO:0007829|PDB:5E9H"
FT   STRAND          122..125
FT                   /evidence="ECO:0007829|PDB:5E9H"
FT   HELIX           131..155
FT                   /evidence="ECO:0007829|PDB:5E9H"
FT   HELIX           159..161
FT                   /evidence="ECO:0007829|PDB:5E9H"
FT   STRAND          174..177
FT                   /evidence="ECO:0007829|PDB:5E9H"
FT   STRAND          182..184
FT                   /evidence="ECO:0007829|PDB:5E9H"
FT   HELIX           185..198
FT                   /evidence="ECO:0007829|PDB:5E9H"
FT   STRAND          201..208
FT                   /evidence="ECO:0007829|PDB:5E9H"
FT   TURN            210..212
FT                   /evidence="ECO:0007829|PDB:5E9H"
FT   HELIX           226..243
FT                   /evidence="ECO:0007829|PDB:5E9H"
FT   STRAND          248..253
FT                   /evidence="ECO:0007829|PDB:5E9H"
FT   TURN            255..257
FT                   /evidence="ECO:0007829|PDB:5E9H"
FT   STRAND          260..262
FT                   /evidence="ECO:0007829|PDB:5E9H"
FT   HELIX           267..270
FT                   /evidence="ECO:0007829|PDB:5E9H"
FT   HELIX           284..293
FT                   /evidence="ECO:0007829|PDB:5E9H"
FT   HELIX           298..311
FT                   /evidence="ECO:0007829|PDB:5E9H"
FT   HELIX           317..327
FT                   /evidence="ECO:0007829|PDB:5E9H"
FT   HELIX           333..344
FT                   /evidence="ECO:0007829|PDB:5E9H"
FT   HELIX           349..360
FT                   /evidence="ECO:0007829|PDB:5E9H"
FT   STRAND          367..369
FT                   /evidence="ECO:0007829|PDB:5E9H"
FT   STRAND          378..380
FT                   /evidence="ECO:0007829|PDB:5E9H"
FT   HELIX           384..394
FT                   /evidence="ECO:0007829|PDB:5E9H"
FT   HELIX           395..397
FT                   /evidence="ECO:0007829|PDB:5E9H"
FT   STRAND          399..403
FT                   /evidence="ECO:0007829|PDB:5E9H"
FT   HELIX           410..421
FT                   /evidence="ECO:0007829|PDB:5E9H"
FT   STRAND          429..432
FT                   /evidence="ECO:0007829|PDB:5E9H"
FT   HELIX           439..442
FT                   /evidence="ECO:0007829|PDB:5E9H"
FT   HELIX           445..448
FT                   /evidence="ECO:0007829|PDB:5E9H"
FT   HELIX           451..457
FT                   /evidence="ECO:0007829|PDB:5E9H"
FT   STRAND          460..465
FT                   /evidence="ECO:0007829|PDB:5E9H"
FT   HELIX           468..487
FT                   /evidence="ECO:0007829|PDB:5E9H"
FT   HELIX           489..495
FT                   /evidence="ECO:0007829|PDB:5E9H"
FT   HELIX           497..502
FT                   /evidence="ECO:0007829|PDB:5E9H"
FT   HELIX           506..508
FT                   /evidence="ECO:0007829|PDB:5E9H"
FT   HELIX           510..513
FT                   /evidence="ECO:0007829|PDB:5E9H"
FT   HELIX           516..525
FT                   /evidence="ECO:0007829|PDB:5E9H"
FT   HELIX           541..544
FT                   /evidence="ECO:0007829|PDB:5E9H"
SQ   SEQUENCE   546 AA;  60826 MW;  C90BD9BFBAB4BE9D CRC64;
     MASQNMTNPS INPDIEDELF QKEVEAVKTW WSDSRWRQTK RPFTAEQIVS KRGYLPIDYA
     SNTQAKKLWK ILEHRFENRD ASYTYGCLEP TMVTQMAKYL DTVYVSGWQS SSTASASDEP
     GPDLADYPYT TVPNKVGHLF MAQLFHDRKQ RQERLSVPKE QRANLLNIDY LRPIVADADT
     GHGGLTAVMK LTKLFIEKGA AGIHIEDQAP GTKKCGHMAG KVLVPIQEHI NRLVAIRAQA
     DIMGSDLLAI ARTDAEAATL LSTNIDPRDH AFILGSTNST LKPLNDLMIA AEATGKSGAE
     LQRIEDEWLA KANLSSFDDA VAAAIDAGSF SDKAGIKQEY TSRAKGKSNF EARAVARQLL
     GRDIFFDWDA PRTREGYFRL KGGCDCAVNR AIAYAPYCDA IWMESKLPDF AQAEQFAQGV
     HAVWPEKKLA YNLSPSFNWK TAMPRDEQET YIRRLAKLGY CWQFITLAGL HTTALISDQF
     AKAYSTVGMR AYGELVQEPE MDQKVDVVKH QKWSGATYVD ELQKMVTGGI SSTAAMGAGV
     TEDQFK
//