ID A0A0D7A245_9AGAR Unreviewed; 638 AA.
AC A0A0D7A245;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=methylisocitrate lyase {ECO:0000256|ARBA:ARBA00012260};
DE EC=4.1.3.30 {ECO:0000256|ARBA:ARBA00012260};
GN ORFNames=FISHEDRAFT_77203 {ECO:0000313|EMBL:KIY44795.1};
OS Fistulina hepatica ATCC 64428.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Fistulinaceae; Fistulina.
OX NCBI_TaxID=1128425 {ECO:0000313|EMBL:KIY44795.1, ECO:0000313|Proteomes:UP000054144};
RN [1] {ECO:0000313|EMBL:KIY44795.1, ECO:0000313|Proteomes:UP000054144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 64428 {ECO:0000313|EMBL:KIY44795.1,
RC ECO:0000313|Proteomes:UP000054144};
RX PubMed=25683379; DOI=10.1016/j.fgb.2015.02.002;
RA Floudas D., Held B.W., Riley R., Nagy L.G., Koehler G., Ransdell A.S.,
RA Younus H., Chow J., Chiniquy J., Lipzen A., Tritt A., Sun H., Haridas S.,
RA LaButti K., Ohm R.A., Kues U., Blanchette R.A., Grigoriev I.V., Minto R.E.,
RA Hibbett D.S.;
RT "Evolution of novel wood decay mechanisms in Agaricales revealed by the
RT genome sequences of Fistulina hepatica and Cylindrobasidium torrendii.";
RL Fungal Genet. Biol. 76:78-92(2015).
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 -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC Isocitrate lyase family. {ECO:0000256|ARBA:ARBA00005704}.
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; KN882065; KIY44795.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D7A245; -.
DR OrthoDB; 983054at2759; -.
DR Proteomes; UP000054144; Unassembled WGS sequence.
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 Gene3D; 1.10.10.850; -; 1.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR InterPro; IPR006254; Isocitrate_lyase.
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:SF3; BIFUNCTIONAL GLYOXYLATE CYCLE PROTEIN; 1.
DR PANTHER; PTHR21631; ISOCITRATE LYASE/MALATE SYNTHASE; 1.
DR Pfam; PF00463; ICL; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Pyruvate {ECO:0000313|EMBL:KIY44795.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054144}.
SQ SEQUENCE 638 AA; 71782 MW; A56B9A17A4A38C14 CRC64;
MAIPVHIAGY TLSHTETLQA FRKKFPNSRV LQTDDYPTQL GIIPHFGLTY VDQSRIRARF
AYATFGQPVE ENKRFIFVTR YAKDTKSKPW DIKVPWDEDD EDRAVKHCLI ESFGDLPLKW
GNSVTDIQFA IARTDSEAAT LITSNIDGRD HPFILGNINP SLAPLSAIMI AAEQAGKGGD
ALQAIEDAWV ADAKLQLFSE ALSAALQREG ASPAKLADFN VAVKYVSWPE AVGIARTRFG
LKTVPHWDWD APRTREGFYR YRGGTQCAIV RANAFAPYAD LLWMETKKPI AAQAEEFAAG
VHAVHPGHWL AYNLSPSFNW DAAGLGERDM QEYVWRLGRL GFVWQFITLA GLHSNAYISD
LFAQEFAKTG MRAYRNASWA RTSLHIKRRQ CSKAAHQLLF CNFQLYFIPY NLLTGVQAMA
DVNFVQSEQP EVPALPAWVR QRLEVTVDPP PDIRAPRHEA SFYGLINSIL GTIFPATQSF
MIKPQGLLRR PYVDPSLSLD SYDGPVRPHQ DGHALVGDEL FADFIIVKGS GVVQHDIIVS
IVEVKKKKTR MSAAIKQLSD YIKMASPKQR YRHMCGFLVA GNRTQRFTYN FTNPFRPYVS
HVIEFDTLDL EQQLAGLAAD TWMLENDTPN IQRSIAPV
//