ID A0A0S7DIR5_9EURO Unreviewed; 724 AA.
AC A0A0S7DIR5;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=methylisocitrate lyase {ECO:0000256|ARBA:ARBA00012260};
DE EC=4.1.3.30 {ECO:0000256|ARBA:ARBA00012260};
GN ORFNames=CNMCM8060_002498 {ECO:0000313|EMBL:KAF4179775.1};
OS Aspergillus lentulus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=293939 {ECO:0000313|EMBL:KAF4179775.1, ECO:0000313|Proteomes:UP000713487};
RN [1] {ECO:0000313|EMBL:KAF4179775.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CNM-CM8060 {ECO:0000313|EMBL:KAF4179775.1};
RA dos Santos R.A.C., Steenwyk J.L., Rivero-Menendez O., Mead M.E.,
RA Silva L.P., Bastos R.W., Alastruey-Izquierdo A., Goldman G.H., Rokas A.;
RT "Genomic and phenotypic heterogeneity of clinical isolates of the human
RT pathogens Aspergillus fumigatus, Aspergillus lentulus and Aspergillus
RT fumigatiaffinis.";
RL bioRxiv 0:0-0(2020).
RN [2] {ECO:0000313|EMBL:KAF4179775.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CNM-CM8060 {ECO:0000313|EMBL:KAF4179775.1};
RA Santos R.A.C., Steenwyk J.L., Rivero-Menendez O., Mead M.E., Silva L.P.,
RA Bastos R.W., Alastruey-Izquierdo A., Goldman G.H., Rokas A.;
RL Submitted (APR-2020) 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 -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC Isocitrate lyase family. {ECO:0000256|ARBA:ARBA00005704}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAF4179775.1}.
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DR EMBL; JAAAPS010000016; KAF4179775.1; -; Genomic_DNA.
DR STRING; 293939.A0A0S7DIR5; -.
DR VEuPathDB; FungiDB:TMP_alenIFM54703_1108; -.
DR Proteomes; UP000713487; 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 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 SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR PROSITE; PS00161; ISOCITRATE_LYASE; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239}.
SQ SEQUENCE 724 AA; 81049 MW; 6F55EE055B206E08 CRC64;
MPKYANLRDR VSFPKVLDLP DYQIYDPEHY KHVSDQVIEP RRHWCLLAEI IKINKGSPLK
LMARSLYNEE SFHIVFHTHD LGDSFVTPDL KLERTVAIMY ARKLISRWKS INVIVTDHYS
IKMFRSVPRR IPRRLPTLSS TAGSPSRLAL RSFTCGYPRM SSSPLPTVEP PVSTTLPSDS
FQLLSTTEKA GAAEDALYEQ QVKDVETWWK SPRFEGIKRP YSAADVVSKR GTLQQTYPSS
LMARKLFNLL NERAAEGKPV HTMGAIDPVQ MTQQAPNQEV LYISGWACSS LLTTTNEVSP
DFGDYPYNTV PNQVQRLFKA QQMHDRKQWD ARRKMTPEQR KSTPYVDYMR PIVADGDTGH
GGLSAVLKLA KLFAENGAAA VHFEDQLHGG KKCGHLAGKV IVPIGEHINR LVAARFQWDM
MGVENLVIAR TDSESGKLIS SAIDVRDHEF ILGVAEEVEP LAETLQAMER EGAAPAEVDA
FELEWVKKHK LVTFDEAVDA HLEAEGAPQS ARDAYKKKVQ ANPDLSISRR RALASDYTKK
PVVWSCDSPR TREGFYHYRA GFPAATKRAK EFAPYADLLW VETGDPNVEK AGKLASEVRA
AYPGKKLVYN LSPSFNWMGQ GFDEASLKSF VWDLAKHGFV LQLISLAGLH SNATITTELS
RAFKDEGMLA YVRLIQSREK ELGVEVLTHQ KWSGAPYMDG ILGAIQSGSS SSKSMGEGNT
EKGF
//