ID   ACEB_HYPAI              Reviewed;         561 AA.
AC   G9NNY7;
DT   24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT   22-FEB-2012, sequence version 1.
DT   25-MAY-2022, entry version 43.
DE   RecName: Full=2-methylisocitrate lyase, mitochondrial {ECO:0000250|UniProtKB:C8V9Y5};
DE            EC=4.1.3.30 {ECO:0000250|UniProtKB:C8V9Y5};
DE   Flags: Precursor;
GN   Name=mcl {ECO:0000303|PubMed:24100269}; ORFNames=TRIATDRAFT_154163;
OS   Hypocrea atroviridis (strain ATCC 20476 / IMI 206040) (Trichoderma
OS   atroviride).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=452589;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 20476 / IMI 206040;
RX   PubMed=21501500; DOI=10.1186/gb-2011-12-4-r40;
RA   Kubicek C.P., Herrera-Estrella A., Seidl-Seiboth V., Martinez D.A.,
RA   Druzhinina I.S., Thon M., Zeilinger S., Casas-Flores S., Horwitz B.A.,
RA   Mukherjee P.K., Mukherjee M., Kredics L., Alcaraz L.D., Aerts A., Antal Z.,
RA   Atanasova L., Cervantes-Badillo M.G., Challacombe J., Chertkov O.,
RA   McCluskey K., Coulpier F., Deshpande N., von Doehren H., Ebbole D.J.,
RA   Esquivel-Naranjo E.U., Fekete E., Flipphi M., Glaser F.,
RA   Gomez-Rodriguez E.Y., Gruber S., Han C., Henrissat B., Hermosa R.,
RA   Hernandez-Onate M., Karaffa L., Kosti I., Le Crom S., Lindquist E.,
RA   Lucas S., Luebeck M., Luebeck P.S., Margeot A., Metz B., Misra M.,
RA   Nevalainen H., Omann M., Packer N., Perrone G., Uresti-Rivera E.E.,
RA   Salamov A., Schmoll M., Seiboth B., Shapiro H., Sukno S.,
RA   Tamayo-Ramos J.A., Tisch D., Wiest A., Wilkinson H.H., Zhang M.,
RA   Coutinho P.M., Kenerley C.M., Monte E., Baker S.E., Grigoriev I.V.;
RT   "Comparative genome sequence analysis underscores mycoparasitism as the
RT   ancestral life style of Trichoderma.";
RL   Genome Biol. 12:R40.1-R40.15(2011).
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=24100269; DOI=10.1099/mic.0.070466-0;
RA   Dubey M.K., Broberg A., Jensen D.F., Karlsson M.;
RT   "Role of the methylcitrate cycle in growth, antagonism and induction of
RT   systemic defence responses in the fungal biocontrol agent Trichoderma
RT   atroviride.";
RL   Microbiology 159:2492-2500(2013).
CC   -!- FUNCTION: Component of the methylcitrate cycle that catalyzes the
CC       formation of pyruvate and succinate from 2-methylisocitrate during the
CC       metabolism of endogenous propionyl-CoA (By similarity). Plays an
CC       important role for growth and development, but also in antagonism, root
CC       colonization and induction of defense responses in plants
CC       (PubMed:24100269). {ECO:0000250|UniProtKB:C8V9Y5,
CC       ECO:0000269|PubMed:24100269}.
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:C8V9Y5};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:C8V9Y5};
CC   -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC       {ECO:0000250|UniProtKB:C8V9Y5}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Abolishes growth and conidial germination when
CC       propionate is the sole carbon source. Reduces growth rate and numbers
CC       of germinating conidia on butyrate, ethanol, citrate and Tween 20.
CC       Leads also to delayed conidial pigmentation when grown on non-
CC       fermentable carbon compounds as the sole carbon source. Results in
CC       decreased tolerance to osmotic stress, shows reduced in vitro
CC       antagonism against Botryotinia fuckeliana, and delays root
CC       colonization. {ECO:0000269|PubMed:24100269}.
CC   -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC       Isocitrate lyase family. {ECO:0000305}.
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DR   EMBL; ABDG02000020; EHK47774.1; -; Genomic_DNA.
DR   RefSeq; XP_013945948.1; XM_014090473.1.
DR   AlphaFoldDB; G9NNY7; -.
DR   SMR; G9NNY7; -.
DR   STRING; 63577.G9NNY7; -.
DR   EnsemblFungi; EHK47774; EHK47774; TRIATDRAFT_154163.
DR   GeneID; 25776251; -.
DR   eggNOG; KOG1260; Eukaryota.
DR   HOGENOM; CLU_019214_2_2_1; -.
DR   OMA; ARFQWDM; -.
DR   OrthoDB; 905115at2759; -.
DR   UniPathway; UPA00946; -.
DR   Proteomes; UP000005426; Unassembled WGS sequence.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
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; 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   3: Inferred from homology;
KW   Lyase; Mitochondrion; Reference proteome; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000305"
FT   CHAIN           ?..561
FT                   /note="2-methylisocitrate lyase, mitochondrial"
FT                   /id="PRO_0000433359"
FT   REGION          154..177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        155..177
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        228
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10119"
SQ   SEQUENCE   561 AA;  61684 MW;  03C2E347254DB58E CRC64;
     MAASAPSNSL PPADSYQLLP EAQKAGAAED ALYEAQVKEI EEWWASPRFA GIRRPYSAAD
     VASKRGSQHF RYPSSVMATK LFNLIREREA KGEPIHTMGA IDPVQMTQQA PHQEVLYISG
     WACSSVLTST NEVSPDFGDY PYNTVPNQVQ RLAKAQSMHD RKQWDTRRKM SPDERSKTPY
     TDYLRPIIAD GDTGHGGLSA VLKLAKLFAE NGAAAVHFED QLHGGKKCGH LAGKVLVPTG
     EHINRLNAAR FQWDVMGSEN LVIARTDSES GRLISSAIDV RDHEFILGIA DPAVEPLAET
     LQSMEARGAT GAEIDVFEAK WVKSSTLVTF DEAAVAHMKK EGVSQAKIDE YLSATALDRD
     MGISRRRALA SQFTETPVYF NWDVPRTREG YYHFRAGMEA ATKRALAFAP YADLLWVETG
     DPNVEVAAKL GRAVRSVNPG KSLVYNLSPS FNWMAHGFSE EGLKSFIWDI AKEGFTLQLI
     SLAGLHSTAT ITNELAKKFK TDGMKAYVEV VQRREKELGC DVLTHQKWSG ASYIDGILGA
     IQSGNSSSRS MGEGNTEGQF D