ID A0A0G2H1S7_9EURO Unreviewed; 971 AA.
AC A0A0G2H1S7;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=methylisocitrate lyase {ECO:0000256|ARBA:ARBA00012260};
DE EC=4.1.3.30 {ECO:0000256|ARBA:ARBA00012260};
GN ORFNames=UCRPC4_g03075 {ECO:0000313|EMBL:KKY22750.1};
OS Phaeomoniella chlamydospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Phaeomoniellales; Phaeomoniellaceae; Phaeomoniella.
OX NCBI_TaxID=158046 {ECO:0000313|EMBL:KKY22750.1, ECO:0000313|Proteomes:UP000053317};
RN [1] {ECO:0000313|EMBL:KKY22750.1, ECO:0000313|Proteomes:UP000053317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY22750.1};
RA Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT "Distinctive expansion of gene families associated with plant cell wall
RT degradation and secondary metabolism in the genomes of grapevine trunk
RT pathogens.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKY22750.1, ECO:0000313|Proteomes:UP000053317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY22750.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
RL Submitted (MAY-2015) 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:KKY22750.1}.
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DR EMBL; LCWF01000073; KKY22750.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2H1S7; -.
DR OrthoDB; 983054at2759; -.
DR Proteomes; UP000053317; 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; 3.30.300.30; -; 1.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR045851; AMP-bd_C_sf.
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 InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
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; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR PROSITE; PS00161; ISOCITRATE_LYASE; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:KKY22750.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053317}.
FT COILED 749..776
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 971 AA; 107650 MW; 1692E3264308306E CRC64;
MSHSLMSSTL QPVEPPVSIA HPTDSFQLLP TAIKAGQAED ELYQKQTEDT KEWWAGPRFE
GIKRPYTAED VVSKRGSLQI SYPSSIMARK LFDLLNERAA AGLPVHTMGA IDPVQMTQQA
PNQEVLYISG WACSSTLTTT NEVSPDFGDY PYNTVPNQVD RLFKAQKLHD RKAWDARRKL
TSEERKNTPY VDYMRPIIAD GDTGHGGLSA VLKLAKLFAE NGAAAVHFED QLHGGKKCGH
LAGKVLVPVG EHINRLVAAR FQWDMMGTEN LVIARTDSES GKLLSSAIDV RDHEFILGIA
DDVEPLAEQI QAMELDGASG PEIDQFESAW VKKYQLVTFD EAAEAHLKSQ GIDPSDYLSR
TSKDRNMSLS RRKALAAKYS KTPVIWSCDS PRTREGFYHY RAGIPAATKR AIEFGPYADL
LWLETGTASV EMAAKFAGDI RAELPGKKLV YNLSPSFNWA AQGYDDAALK AFIWDLAKHG
FVLQLISLAG LHSTATITQE LSRGFKDDGM LAYVNLVQKR EKELGVDVLT HQNWSGASYM
DGIIGAIQSG SSGSRSMGEG NTEKRKILSV SPRTRSARVH VFVELIQAED GLEDTEASDT
SGQAFHQAAN STRQLPVPTN VFEPDLNMGI RPARAARQSF YQNHQRREEA YFEVDPRADV
MPTQALHQEF YQQRPSPEPE MICLCREPKA GRRTIRCSIG EFCLTKEFHL DCIGLERRPH
RSESWTCPEC SEYASDAGGA GGNDAPEAAN STLSTINHLT EVMKELEAEN IRGKDKWNVA
RDRLLTRNID RDALRRTDDG LWYFMDRLGD TYRWKSENVS TAEVAEVLGG YSGVTEAIVY
GVLVPNHDGR AGCAALVIDP AAKATFDFDA LYKYTRSKLP SYAAPVFLRL ISHSLIAHNN
KQNKGPLREE GVDISQFGSK VAGVEGDRVQ YYGFRHADQG MTRATSTLAR RIGKGWSMGE
HDYSTADIAC V
//
