ACEA_COPCI
ID ACEA_COPCI Reviewed; 537 AA.
AC O13439;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Isocitrate lyase {ECO:0000303|PubMed:9031626};
DE Short=ICL {ECO:0000305};
DE Short=Isocitrase {ECO:0000305};
DE Short=Isocitratase {ECO:0000305};
DE EC=4.1.3.1 {ECO:0000250|UniProtKB:P28240};
DE AltName: Full=Methylisocitrate lyase {ECO:0000250|UniProtKB:P28240};
DE Short=MICA {ECO:0000305};
DE EC=4.1.3.30 {ECO:0000250|UniProtKB:P28240};
DE AltName: Full=Threo-D(S)-isocitrate glyoxylate-lyase {ECO:0000305};
GN Name=ACU-7 {ECO:0000303|PubMed:9031626};
OS Coprinopsis cinerea (Inky cap fungus) (Hormographiella aspergillata).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Psathyrellaceae; Coprinopsis.
OX NCBI_TaxID=5346;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=JV6;
RX PubMed=9031626; DOI=10.1016/s0378-1119(96)00593-8;
RA Chaure P.T., Casselton L.A., Connerton I.F.;
RT "Molecular analysis of the isocitrate lyase gene (acu-7) of the mushroom
RT Coprinus cinereus.";
RL Gene 184:185-187(1997).
CC -!- FUNCTION: Catalyzes the formation of succinate and glyoxylate from
CC isocitrate, a key step of the glyoxylate cycle, which operates as an
CC anaplerotic route for replenishing the tricarboxylic acid cycle.
CC Required for growth on ethanol or acetate, but dispensable when
CC fermentable carbon sources are available. Acts also on 2-
CC methylisocitrate. {ECO:0000250|UniProtKB:P28240}.
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:0000250|UniProtKB:P28240};
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:0000250|UniProtKB:P28240};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P9WKK7};
CC -!- PATHWAY: Carbohydrate metabolism; glyoxylate cycle; (S)-malate from
CC isocitrate: step 1/2.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P28240}.
CC -!- SUBCELLULAR LOCATION: Glyoxysome {ECO:0000250|UniProtKB:P28299}.
CC -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC Isocitrate lyase family. {ECO:0000305}.
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DR EMBL; X98860; CAA67367.1; -; Genomic_DNA.
DR PIR; JC6182; JC6182.
DR AlphaFoldDB; O13439; -.
DR SMR; O13439; -.
DR VEuPathDB; FungiDB:CC1G_07122; -.
DR VEuPathDB; FungiDB:CC2G_012762; -.
DR UniPathway; UPA00703; UER00719.
DR GO; GO:0009514; C:glyoxysome; IEA:UniProtKB-SubCell.
DR GO; GO:0004451; F:isocitrate lyase activity; IEA:UniProtKB-EC.
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-UniPathway.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR CDD; cd00377; ICL_PEPM; 1.
DR Gene3D; 3.20.20.60; -; 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 PANTHER; PTHR21631; PTHR21631; 1.
DR Pfam; PF00463; ICL; 1.
DR PIRSF; PIRSF001362; Isocit_lyase; 1.
DR SUPFAM; SSF51621; SSF51621; 1.
DR TIGRFAMs; TIGR01346; isocit_lyase; 1.
DR PROSITE; PS00161; ISOCITRATE_LYASE; 1.
PE 3: Inferred from homology;
KW Glyoxylate bypass; Glyoxysome; Lyase; Magnesium; Metal-binding; Peroxisome;
KW Tricarboxylic acid cycle.
FT CHAIN 1..537
FT /note="Isocitrate lyase"
FT /id="PRO_0000068787"
FT MOTIF 535..537
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 203
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 94..96
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 165
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 204..205
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 240
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 420..424
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 454
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
SQ SEQUENCE 537 AA; 59358 MW; EEAB953191CDFA82 CRC64;
MSSERAQFAS EVAEVERWWK SPRFARVNRP YTAADVVSKR GTIKINYPSD VQGKKLWKLL
SEHAKNGTPS HTYGALDPVQ VTKMAKYLET VYVSGWQSSS TASSSNEPGP DLADYPSNTV
PNKVEHLFMA QLFHDRKQRE ARSRMSDAEL ANTPVIDYLR PIVADADTGH GGLTAVMKLT
KMFVEKGAAG IHIEDQAPGT KKCGHMAGKV LVPIQEHINR LVAIRLQYDI MGVENLVVAR
TDSEAATLIT SNIDDRDHPF IQGSTNPSLP PLNNVMVEAE AQGKTGDQLQ AIEDGWIKAA
NLQLFPQALA QALANEGASR STVEKLVARV SRLSWSQAVA VAQKEFGLKQ VPYWNWDAPR
TREGYYRYQG GTECAIHRAN AFAPYADLLW METKKPILAQ AKEFAAGVHA VHPGQWLAYN
LSPSFNWKLL PQRQDMQAYV WELGKLGFVW QFITLAGLHS NAYISDLFAQ NFAKTGMKAY
VELVQSRERE IGCDVLTHQK WSGADYADSL IKTVTGGVSS TAAMGAGVTE SQFTSKL
