ID   A0A178AF82_9PLEO        Unreviewed;       313 AA.
AC   A0A178AF82;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Methylisocitrate lyase-like protein {ECO:0000313|EMBL:OAK95589.1};
GN   ORFNames=IQ06DRAFT_231943 {ECO:0000313|EMBL:OAK95589.1};
OS   Stagonospora sp. SRC1lsM3a.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX   NCBI_TaxID=765868 {ECO:0000313|EMBL:OAK95589.1, ECO:0000313|Proteomes:UP000077206};
RN   [1] {ECO:0000313|EMBL:OAK95589.1, ECO:0000313|Proteomes:UP000077206}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAK95589.1,
RC   ECO:0000313|Proteomes:UP000077206};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001050};
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DR   EMBL; KV441722; OAK95589.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A178AF82; -.
DR   STRING; 765868.A0A178AF82; -.
DR   InParanoid; A0A178AF82; -.
DR   OrthoDB; 554215at2759; -.
DR   Proteomes; UP000077206; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   CDD; cd00377; ICL_PEPM; 1.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   InterPro; IPR039556; ICL/PEPM.
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; PTHR42905; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   PANTHER; PTHR42905:SF2; PHOSPHOENOLPYRUVATE CARBOXYLASE FAMILY PROTEIN; 1.
DR   Pfam; PF13714; PEP_mutase; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   PROSITE; PS00161; ISOCITRATE_LYASE; 1.
PE   4: Predicted;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:OAK95589.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077206}.
SQ   SEQUENCE   313 AA;  33290 MW;  F8237D98A750BA50 CRC64;
     MGSIATSNGE KKMTAVQKLR SMLADPDRFI ACPGVYDGFT AQIALREGVD CLYMTGAGTT
     MSRLGQADMG VATLHDMVTN ANMIASLSPS TPLIADADTG YGGAIMVGRT VTSYIRAGVA
     GLHLEDQVVN KRCGHLKGKQ LVDVSEYASR MRAAVRAREE SGGDIVIIAR TDALQGYGYD
     EAVKRLKAAI AAGADVAFLE GVNTKDEAER VCKELAPTPC LFNNVPGGVS PDWSADEAKA
     LGYKLAIFPA LSFEVVYPVV RRAMQQLLTT GRVDSQEKDG RRYGPKELFQ VCGLDEMVEF
     DNAVGGGAYT NGA
//