ID M7THU7_EUTLA Unreviewed; 549 AA.
AC M7THU7;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Isocitrate lyase {ECO:0000256|ARBA:ARBA00017446, ECO:0000256|PIRNR:PIRNR001362};
GN ORFNames=UCREL1_6705 {ECO:0000313|EMBL:EMR66300.1};
OS Eutypa lata (strain UCR-EL1) (Grapevine dieback disease fungus) (Eutypa
OS armeniacae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Diatrypaceae; Eutypa.
OX NCBI_TaxID=1287681 {ECO:0000313|EMBL:EMR66300.1, ECO:0000313|Proteomes:UP000012174};
RN [1] {ECO:0000313|Proteomes:UP000012174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR-EL1 {ECO:0000313|Proteomes:UP000012174};
RX PubMed=23723393; DOI=10.1128/genomeA.00228-13;
RA Blanco-Ulate B., Rolshausen P.E., Cantu D.;
RT "Draft genome sequence of the grapevine dieback fungus Eutypa lata UCR-
RT EL1.";
RL Genome Announc. 1:E0022813-E0022813(2013).
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 -!- CATALYTIC ACTIVITY:
CC Reaction=D-threo-isocitrate = glyoxylate + succinate;
CC Xref=Rhea:RHEA:13245, ChEBI:CHEBI:15562, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:36655; EC=4.1.3.1;
CC Evidence={ECO:0000256|ARBA:ARBA00023531};
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 -!- PATHWAY: Carbohydrate metabolism; glyoxylate cycle; (S)-malate from
CC isocitrate: step 1/2. {ECO:0000256|ARBA:ARBA00004793}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC Isocitrate lyase family. {ECO:0000256|ARBA:ARBA00005704,
CC ECO:0000256|PIRNR:PIRNR001362}.
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DR EMBL; KB706676; EMR66300.1; -; Genomic_DNA.
DR RefSeq; XP_007794598.1; XM_007796407.1.
DR AlphaFoldDB; M7THU7; -.
DR STRING; 1287681.M7THU7; -.
DR KEGG; ela:UCREL1_6705; -.
DR eggNOG; KOG1260; Eukaryota.
DR HOGENOM; CLU_019214_2_2_1; -.
DR OMA; YVSGWQV; -.
DR OrthoDB; 983054at2759; -.
DR Proteomes; UP000012174; 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:0006097; P:glyoxylate cycle; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.850; -; 1.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
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:SF3; BIFUNCTIONAL GLYOXYLATE CYCLE PROTEIN; 1.
DR PANTHER; PTHR21631; ISOCITRATE LYASE/MALATE SYNTHASE; 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 Glyoxylate bypass {ECO:0000256|ARBA:ARBA00022435};
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:UP000012174};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT ACT_SITE 216
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-1"
FT BINDING 106..108
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 178
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-3"
FT BINDING 217..218
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 253
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 435..439
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
FT BINDING 469
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001362-2"
SQ SEQUENCE 549 AA; 60601 MW; F00A5F53EDD94265 CRC64;
MASNNMINAA IDPDVEEELF AKEIEAVKKW WSDPRWRYTK RPFTAEQIVS KRGHLPIEYA
SNTQSKKLWK ILEGRFKNRD ASYTYGCLEP TMVTQMAKYL DTVYVSGWQS SSTASSSDEP
GPDLADYPYT TVPNKVKHLF MAQLFHDRKQ RQERLSAPSK AERAKLANID YLRPIIADAD
TGHGGLTAVM KLTKLFVESG AAGIHIEDQA PGTKKCGHMA GKVLVPISEH INRLVAIRAQ
ADIMGSDLLA VARTDAEAAT LITTTIDPRD HAFILGCTNP SLTPLSDLMI AGERAGKNGD
DLQAIEDAWL RDAGLQRFDD AVVDAINADP ALSDKKGAVS AYLAQAKGKS LTDARAAARA
ATGGKDVFFD WDAARTREGY YRLKGGCDCA INRAIAYAPY CDAIWMESKL PDFKQAEEFA
KGVHSVWPEQ KLAYNLSPSF NWKSAMPRDE QETYIRRLAT LGYCWQFITL AGLHTTALAS
DAFARAYARQ GMRAYGELVQ EPEMTTGVDV VRHQKWSGAT YVDELQKMIT GGVSSTAAMG
KGVTEDQFH
//
