ACEA_GIBZE
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 03-AUG-2022, entry version 103.
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}.
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; 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; 5518.FGSG_09896P0; -.
DR EnsemblFungi; ESU16540; ESU16540; FGSG_09896.
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 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; 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 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
