ID A0A3E2HJF3_SCYLI Unreviewed; 600 AA.
AC A0A3E2HJF3;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=methylisocitrate lyase {ECO:0000256|ARBA:ARBA00012260};
DE EC=4.1.3.30 {ECO:0000256|ARBA:ARBA00012260};
DE Flags: Fragment;
GN ORFNames=B7463_g2836 {ECO:0000313|EMBL:RFU33536.1};
OS Scytalidium lignicola (Hyphomycete).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Scytalidium.
OX NCBI_TaxID=5539 {ECO:0000313|EMBL:RFU33536.1, ECO:0000313|Proteomes:UP000258309};
RN [1] {ECO:0000313|EMBL:RFU33536.1, ECO:0000313|Proteomes:UP000258309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 105466 {ECO:0000313|EMBL:RFU33536.1,
RC ECO:0000313|Proteomes:UP000258309};
RA Buettner E., Gebauer A.M., Hofrichter M., Liers C., Kellner H.;
RT "Draft genome sequence of Scytalidium lignicola DSM 105466, a ubiquitous
RT saprotrophic fungus.";
RL Submitted (MAY-2018) 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 -!- 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:RFU33536.1}.
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DR EMBL; NCSJ02000034; RFU33536.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3E2HJF3; -.
DR STRING; 5539.A0A3E2HJF3; -.
DR OMA; WFVYNLS; -.
DR Proteomes; UP000258309; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Magnesium {ECO:0000256|PIRSR:PIRSR001362-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001362-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000258309}.
FT ACT_SITE 268
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-1"
FT BINDING 159..161
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 230
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
FT BINDING 269..270
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 305
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 486..490
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 521
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RFU33536.1"
FT NON_TER 600
FT /evidence="ECO:0000313|EMBL:RFU33536.1"
SQ SEQUENCE 600 AA; 66395 MW; 32366D1112BE57C8 CRC64;
MLRRIATAAP RRVNVARIAA SHTQITPLNA LSACRMASTL KPPQHPLSTS LTSDAFQLLP
ESQKAGVAED ELYEQQLKDV EAWWASPRYE GIKRPYSAAD VVSKRGSQQQ SYPSSVMARK
LFNLIKEREA KGEPIHTMGA IDPVQMTQQA VNQEVLYISG WACSSVLTTT NEVSPDFGDY
PYNTVPNQVQ RLAKAQSMHD RKQWDARRKL TAEERAKTPY TDYLRPIIAD GDTGHGGLSA
VLKLAKLFAE NGAAAVHFED QLHGGKKCGH LAGKVLVPVG EHINRLVAAR FQWDVMGSEN
LVIARTDSES GKLLSSAIDV RDHEFILGVA DPNIEPLAET LQAMELNDAS GEEINVFEAD
WVKKTEMMTC DEAIVKQLKA HGVSQSSIDE YLKATSENRD MSIVQRQKLA KKYTDKPLYF
SIDVPRTREG FYHYRAGMTA ATKRAIEYAP YADLLWVETG DPNVKNAAQF AGEIRAKHPH
KGLVYNLSPS FNWMGHGFTD ETLKSFIWDI AKHGFVIQLI SLAGLHSTAA VTYELSQAFK
TDGMKAYVDL IQKREKELGV DVLTHQKWSG AAYIDGILGA IQSGSSHSKS MGDGNTEGQF
//
