ID U4LIX0_PYROM Unreviewed; 575 AA.
AC U4LIX0;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Isocitrate lyase {ECO:0000256|PIRNR:PIRNR001362};
GN ORFNames=PCON_11975 {ECO:0000313|EMBL:CCX31898.1};
OS Pyronema omphalodes (strain CBS 100304) (Pyronema confluens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Pyronemataceae; Pyronema.
OX NCBI_TaxID=1076935 {ECO:0000313|EMBL:CCX31898.1};
RN [1] {ECO:0000313|EMBL:CCX31898.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS100304 {ECO:0000313|EMBL:CCX31898.1};
RC TISSUE=Vegetative mycelium {ECO:0000313|EMBL:CCX31898.1};
RX PubMed=24068976; DOI=10.1371/journal.pgen.1003820;
RA Traeger S., Altegoer F., Freitag M., Gabaldon T., Kempken F., Kumar A.,
RA Marcet-Houben M., Poggeler S., Stajich J.E., Nowrousian M.;
RT "The genome and development-dependent transcriptomes of Pyronema confluens:
RT a window into fungal evolution.";
RL PLoS Genet. 9:E1003820-E1003820(2013).
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};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR001362-3};
CC Note=Can also use Mn(2+) ion. {ECO:0000256|PIRSR:PIRSR001362-3};
CC -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC Isocitrate lyase family. {ECO:0000256|ARBA:ARBA00005704,
CC ECO:0000256|PIRNR:PIRNR001362}.
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DR EMBL; HF935702; CCX31898.1; -; Genomic_DNA.
DR AlphaFoldDB; U4LIX0; -.
DR STRING; 1076935.U4LIX0; -.
DR eggNOG; KOG1260; Eukaryota.
DR OMA; WFVYNLS; -.
DR OrthoDB; 983054at2759; -.
DR Proteomes; UP000018144; Unassembled WGS sequence.
DR GO; GO:0004451; F:isocitrate lyase activity; IEA:InterPro.
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: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; 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 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; 1.
DR PIRSF; PIRSF001362; Isocit_lyase; 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 Magnesium {ECO:0000256|PIRSR:PIRSR001362-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001362-3}.
FT ACT_SITE 245
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-1"
FT BINDING 136..138
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 207
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
FT BINDING 246..247
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 282
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 462..466
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 497
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
SQ SEQUENCE 575 AA; 63918 MW; 768D4681FAE31E93 CRC64;
MLRLPRIRPL PRILSSTNIP NSTFVITTRM SSTARPLHVA PTPEQEEAAL EAEIKAIEEW
WSSPRFKGIK RPYSAREVAT KRGNLPQTYP SSEMAKKLFS LLSERSSQGL PVHTMGAIDP
VQMTQQAPNQ EVLYVSGWAA SSVLTTTNEV SPDLGDYPYN TVPNQVQRLF KAQQLHDRRL
RDERLSMTLA QKKATPYVDY LRPIIADADT GHGGLSAVMK LAKLFAENGA AAIHMEDQMH
GGKKCGHLSG KVLVPTGEHI NRLIATRMQW DIMGTENLII ARTDSETGKL ISSSVDARDH
QFILGVTEDV EPLAEQLFKL ERQGVNGAKI AEVEAEWVGK HKLVTFDEAV VEAAKKDGIA
EEKIENYLKD AATRSNTDSR AVAKELLGRE IFFSWDVPRT REGYYHYKAG MPAAIKRTKA
FAPFADMLWL ETKKPSLKQA QGFAREIRAP GSPGEGKWMV YNLSPSFNWL NEGFDKEGLK
SFVWDMAKEG FVLQLISLAG LHSNAAATWE LSKSFKENGM LAYVDLVQKK EKEIGCDVLT
HQKWSGANYL DGILQSISNS AATSAVGKDS TEHTF
//
