ID A0A0F4Z0V6_TALEM Unreviewed; 308 AA.
AC A0A0F4Z0V6;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Methylisocitrate lyase {ECO:0000313|EMBL:KKA23513.1};
DE EC=4.1.3.30 {ECO:0000313|EMBL:KKA23513.1};
GN ORFNames=T310_2482 {ECO:0000313|EMBL:KKA23513.1};
OS Rasamsonia emersonii CBS 393.64.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Rasamsonia.
OX NCBI_TaxID=1408163 {ECO:0000313|EMBL:KKA23513.1, ECO:0000313|Proteomes:UP000053958};
RN [1] {ECO:0000313|EMBL:KKA23513.1, ECO:0000313|Proteomes:UP000053958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 393.64 {ECO:0000313|EMBL:KKA23513.1,
RC ECO:0000313|Proteomes:UP000053958};
RA Heijne W.H., Fedorova N.D., Nierman W.C., Vollebregt A.W., Zhao Z., Wu L.,
RA Kumar M., Stam H., van den Berg M.A., Pel H.J.;
RL Submitted (APR-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 -!- 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:KKA23513.1}.
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; LASV01000100; KKA23513.1; -; Genomic_DNA.
DR RefSeq; XP_013330125.1; XM_013474671.1.
DR AlphaFoldDB; A0A0F4Z0V6; -.
DR STRING; 1408163.A0A0F4Z0V6; -.
DR GeneID; 25314833; -.
DR OrthoDB; 554215at2759; -.
DR Proteomes; UP000053958; Unassembled WGS sequence.
DR GO; GO:0046421; F:methylisocitrate lyase activity; IEA:UniProtKB-EC.
DR CDD; cd00377; ICL_PEPM; 1.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR InterPro; IPR039556; ICL/PEPM.
DR InterPro; IPR018523; Isocitrate_lyase_ph_CS.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR PANTHER; PTHR42905; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR PANTHER; PTHR42905:SF15; PHOSPHONOMUTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G03820)-RELATED; 1.
DR Pfam; PF13714; PEP_mutase; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR PROSITE; PS00161; ISOCITRATE_LYASE; 1.
PE 4: Predicted;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:KKA23513.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053958}.
SQ SEQUENCE 308 AA; 32597 MW; B12442BAB5D944FB CRC64;
MANSTTKPVS AATLLRQKLE SGSFILAPGV YDGFSARIAL SVGFDALYMT GAGTTASMHG
QADLGIATLN DMRANAEMIA NLSPSVPLIA DADTGYGGPI MVARTTEQYA RSGVAAFHIE
DQVQTKRCGH LGGKILVDTP TFVSRIRAAV QARQRIGSDI VVIARTDALQ KYGYDESLAR
LRAARDAGAD VGFLEGVRSK EEARRIIKDL APWPMLLNMV EHGATPTISA AEAQEMGFKI
MIVPFAALAP AYTAIKQGLE RLKQTGLPGT GSELTPQALF RVCGLDESVR IDEAAGGSNF
EGGVDLPK
//
