ID A0A1L7WUS6_9HELO Unreviewed; 546 AA.
AC A0A1L7WUS6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=methylisocitrate lyase {ECO:0000256|ARBA:ARBA00012260};
DE EC=4.1.3.30 {ECO:0000256|ARBA:ARBA00012260};
GN ORFNames=PAC_06431 {ECO:0000313|EMBL:CZR56542.1};
OS Phialocephala subalpina.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Mollisiaceae; Phialocephala;
OC Phialocephala fortinii species complex.
OX NCBI_TaxID=576137 {ECO:0000313|EMBL:CZR56542.1, ECO:0000313|Proteomes:UP000184330};
RN [1] {ECO:0000313|EMBL:CZR56542.1, ECO:0000313|Proteomes:UP000184330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 11012 {ECO:0000313|EMBL:CZR56542.1,
RC ECO:0000313|Proteomes:UP000184330};
RA Ploux O.;
RL Submitted (MAR-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};
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 -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC Isocitrate lyase family. {ECO:0000256|ARBA:ARBA00005704}.
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DR EMBL; FJOG01000008; CZR56542.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L7WUS6; -.
DR STRING; 576137.A0A1L7WUS6; -.
DR OrthoDB; 1981645at2759; -.
DR Proteomes; UP000184330; 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 Gene3D; 1.10.10.850; -; 1.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 2.
DR InterPro; IPR006254; Isocitrate_lyase.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR PANTHER; PTHR21631:SF3; BIFUNCTIONAL GLYOXYLATE CYCLE PROTEIN; 1.
DR PANTHER; PTHR21631; ISOCITRATE LYASE/MALATE SYNTHASE; 1.
DR Pfam; PF00463; ICL; 2.
DR PIRSF; PIRSF001362; Isocit_lyase; 3.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 2.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:CZR56542.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR001362-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001362-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000184330}.
FT BINDING 170
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
SQ SEQUENCE 546 AA; 61201 MW; 0D147A58135313E0 CRC64;
MPALETDIAT EQAAFDAEVA SIEQAWKSPR QAHLKRPYSA RTIAGLRNSI PQTYVSSTMA
DKLWGQLNEH RKHGTCELTY GATDPIQVSQ MVKHQQTIYV SGSLCGTSEV STPGRDAADY
PWDTVPKVVD KIFRSQMWHD QRQRQQRFST PESKRGELEN WDYLAPIVAD ADMGFGGLTS
TIKMTKAFVE AGVAMIHMDD LATGMKRFSM GMGRTTVPTS EYVSRLTAVR MQFDIMGPKL
GSGAEPVLFI FAFWRYQVRE ADIYSATTML MCRCDTATCE FITSVIDPRD HPYILGATKD
VPSLTSAISA ATTTPDYQWI RNTWKESAGL VTFDEAVKSN TSEEQYKVYT SKLAEKEVTP
MSQRRQIAKE VLGKDVFWDW ELPRSLEGQY MWAPTIQTVI ERASAVAPLG DVTWARIDAP
TLSSLTEFHS AMNALFPNRL FGFGYVAGYD FSKAGFSEEE IKHLHKILAK MGVVWQVQPV
WVTGALSDVT EKFGKMWQEK GMGMWVREYQ RTGWLKGVDG AHKLEWSGGY LADGFAEAVS
GRDMAL
//
