ACEA_NEUCR
ID ACEA_NEUCR Reviewed; 548 AA.
AC P28299; Q7RVC2; Q9HEI3;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Isocitrate lyase {ECO:0000303|PubMed:1531185};
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-3 {ECO:0000303|PubMed:1531185}; ORFNames=2E4.10, NCU04230;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=74A;
RX PubMed=1531185; DOI=10.1007/bf00318653;
RA Gainey L.D.S., Connerton I.F., Lewis E.H., Turner G., Ballance D.J.;
RT "Characterization of the glyoxysomal isocitrate lyase genes of Aspergillus
RT nidulans (acuD) and Neurospora crassa (acu-3).";
RL Curr. Genet. 21:43-47(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=4390938; DOI=10.1016/0006-291x(69)90858-4;
RA Kobr M.J., Vanderhaeghe F., Combepine G.;
RT "Particulate enzymes of the glyoxylate cycle in Neurospora crassa.";
RL Biochem. Biophys. Res. Commun. 37:640-645(1969).
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:0000269|PubMed:4390938}.
CC -!- INDUCTION: By acetate. {ECO:0000269|PubMed:1531185}.
CC -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC Isocitrate lyase family. {ECO:0000305}.
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DR EMBL; X62697; CAA44573.1; -; Genomic_DNA.
DR EMBL; AL451022; CAC18302.1; -; Genomic_DNA.
DR EMBL; CM002240; EAA31618.1; -; Genomic_DNA.
DR PIR; S26858; S26858.
DR RefSeq; XP_960854.1; XM_955761.3.
DR AlphaFoldDB; P28299; -.
DR SMR; P28299; -.
DR STRING; 5141.EFNCRP00000003928; -.
DR EnsemblFungi; EAA31618; EAA31618; NCU04230.
DR GeneID; 3877001; -.
DR KEGG; ncr:NCU04230; -.
DR VEuPathDB; FungiDB:NCU04230; -.
DR HOGENOM; CLU_019214_2_2_1; -.
DR InParanoid; P28299; -.
DR OMA; LEKDWAE; -.
DR UniPathway; UPA00703; UER00719.
DR Proteomes; UP000001805; Chromosome 2, Linkage Group V.
DR GO; GO:0009514; C:glyoxysome; IEA:UniProtKB-SubCell.
DR GO; GO:0004451; F:isocitrate lyase activity; IBA:GO_Central.
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 Gene3D; 3.20.20.60; -; 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 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 2: Evidence at transcript level;
KW Glyoxylate bypass; Glyoxysome; Lyase; Magnesium; Metal-binding; Peroxisome;
KW Reference proteome; Tricarboxylic acid cycle.
FT CHAIN 1..548
FT /note="Isocitrate lyase"
FT /id="PRO_0000068794"
FT ACT_SITE 215
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 106..108
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 177
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 216..217
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 252
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 434..438
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 468
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT CONFLICT 132
FT /note="V -> C (in Ref. 1; CAA44573)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="D -> H (in Ref. 1; CAA44573)"
FT /evidence="ECO:0000305"
FT CONFLICT 422..424
FT /note="VHA -> PR (in Ref. 1; CAA44573)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 548 AA; 61214 MW; 4C3414CE0794D44C CRC64;
MAANNMVNPA VDPALEDELF AKEVEEVKKW WSDSRWRQTK RPFTAEQIVS KRGNLKIEYA
SNAQAKKLWK ILEDRFAKRD ASYTYGCLEP TMVTQMAKYL DTVYVSGWQS SSTASSSDEP
GPDLADYPYT TVPNKVGHLF MAQLFHDRKQ RQERLSVPKD QREKLANIDY LRPIVADADT
GHGGLTAVMK LTKLFIEKGA AGIHIEDQAP GTKKCGHMAG KVLVPIQEHI NRLVAIRAQA
DIMGSDLLCI ARTDAEAATL ITTTIDPRDH AFILGCTNPD LEPLADLMMK AEAEGKTGAQ
LQAIEDDWLA KADLKRFDEA VLDVIAKGKF SNAKDLAAKY QAAVKGKQIS NREARAIARQ
LLGQEIFFDW ESPRTREGYY RLKGGCDCSI NRAISYAPYC DAIWMESKLP DYAQAEEFAK
GVHAVWPEQK LAYNLSPSFN WKTAMGRDDQ ETYIRRLAKL GYCWQFITLA GLHTTALISD
QFAKAYSKIG MRAYGELVQE PEIDNGVDVV KHQKWSGATY VDELQKMVTG GVSSTAAMGK
GVTEDQFH
