ID A0A179HHV8_PURLI Unreviewed; 560 AA.
AC A0A179HHV8;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Isocitrate lyase {ECO:0000256|PIRNR:PIRNR001362};
GN ORFNames=PLICBS_003540 {ECO:0000313|EMBL:GJN69492.1}, VFPBJ_10982
GN {ECO:0000313|EMBL:OAQ67387.1}, VFPFJ_06211
GN {ECO:0000313|EMBL:OAQ89797.1};
OS Purpureocillium lilacinum (Paecilomyces lilacinus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Purpureocillium.
OX NCBI_TaxID=33203 {ECO:0000313|EMBL:OAQ89797.1, ECO:0000313|Proteomes:UP000078340};
RN [1] {ECO:0000313|EMBL:OAQ89797.1, ECO:0000313|Proteomes:UP000078340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PLBJ-1 {ECO:0000313|EMBL:OAQ67387.1}, and PLFJ-1
RC {ECO:0000313|EMBL:OAQ89797.1};
RA Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yin W., Xie B.;
RT "Biosynthesis of antibiotic leucinostatins and their inhibition on
RT Phytophthora in bio-control Purpureocillium lilacinum.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GJN69492.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 284.36 {ECO:0000313|EMBL:GJN69492.1};
RA Alimu Y., Kusuya Y., Yamamoto T., Shigemune N., Takahashi H., Yaguchi T.;
RT "Tolerabce induction of polyhexamethylene biguanide on Purpureocillium
RT lilacinum strains.";
RL Submitted (DEC-2021) 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 -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC Isocitrate lyase family. {ECO:0000256|ARBA:ARBA00005704,
CC ECO:0000256|PIRNR:PIRNR001362}.
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:OAQ89797.1}.
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DR EMBL; BQKW01000002; GJN69492.1; -; Genomic_DNA.
DR EMBL; LSBH01000012; OAQ67387.1; -; Genomic_DNA.
DR EMBL; LSBI01000005; OAQ89797.1; -; Genomic_DNA.
DR RefSeq; XP_018178516.1; XM_018323286.1.
DR STRING; 33203.A0A179HHV8; -.
DR GeneID; 28888335; -.
DR KEGG; plj:VFPFJ_06211; -.
DR OMA; WFVYNLS; -.
DR OrthoDB; 983054at2759; -.
DR Proteomes; UP000078240; Unassembled WGS sequence.
DR Proteomes; UP000078340; Unassembled WGS sequence.
DR Proteomes; UP001056679; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000078340}.
FT ACT_SITE 227
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-1"
FT BINDING 118..120
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 189
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
FT BINDING 228..229
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 264
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 445..449
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 480
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
SQ SEQUENCE 560 AA; 61548 MW; BD78089F33E1BF32 CRC64;
MTNPFSHAVP AADAFQLLPE SQKTGDAEDA LYEAQLKEVE AWWSSPRFQG IKRPYSAADV
VSKRGTQKIS YPSSVMATKL FELLKARLSK GEPVHTMGAI DPVQMTQQAP HQEVLYISGW
ACSSLLTTTN EVSPDFGDYP YNTVPNQVQR LAKAQSMHDR KQWDTRRKLT AQERASTPYI
DYLRPIIADG DTGHGGLSAV LKLAKLFAEN GAAAVHFEDQ LHGGKKCGHL AGKVLVPTGE
HINRLNAARF QWDVMGTENL VIARTDSESG KLISSAIDVR DHEFILGVAD PSIEPLAETI
QAMEAKGASG AEIDVFEAQW VKSTKLVTFD EAAVAHMRSE GVSKERIDEY LNATAADRDM
GITRRRALAS HYAKSPVYFN WDVPRTREGF YHFKAGMPAA TKRAIAFAPY ADLLWVETGD
PNVDVATKLG RAVRDVHPGK GLVYNLSPSF NWMAHGFTPE TLKSFIWDIA REGFVLQLVS
LAGLHSNATI SNELAKNFKT DGMKAYVELV QRREKELGCD VLTHQKWSGA SYIDGILGAI
QSGSSSSKSM GEGNTEGQFN
//
