ACEA_ASPFU
ID ACEA_ASPFU Reviewed; 538 AA.
AC Q6T267; Q4WQP2;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Isocitrate lyase {ECO:0000250|UniProtKB:P28240};
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=icl1 {ECO:0000250|UniProtKB:P28240}; Synonyms=icl {ECO:0000303|Ref.1};
GN ORFNames=AFUA_4G13510;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Shankar J., Madan T., Sarma P.U.;
RT "Aspergillus fumigatus isocitrate lyase (icl) gene.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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; AY442291; AAR15146.1; -; Genomic_DNA.
DR EMBL; AAHF01000005; EAL89442.1; -; Genomic_DNA.
DR RefSeq; XP_751480.1; XM_746387.1.
DR AlphaFoldDB; Q6T267; -.
DR SMR; Q6T267; -.
DR STRING; 746128.CADAFUBP00006860; -.
DR EnsemblFungi; EAL89442; EAL89442; AFUA_4G13510.
DR GeneID; 3509073; -.
DR KEGG; afm:AFUA_4G13510; -.
DR VEuPathDB; FungiDB:Afu4g13510; -.
DR eggNOG; KOG1260; Eukaryota.
DR HOGENOM; CLU_019214_2_2_1; -.
DR InParanoid; Q6T267; -.
DR OMA; LEKDWAE; -.
DR OrthoDB; 905115at2759; -.
DR UniPathway; UPA00703; UER00719.
DR Proteomes; UP000002530; Chromosome 4.
DR GO; GO:0009514; C:glyoxysome; IEA:UniProtKB-SubCell.
DR GO; GO:0004451; F:isocitrate lyase activity; IDA:AspGD.
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 3: Inferred from homology;
KW Glyoxylate bypass; Glyoxysome; Lyase; Magnesium; Metal-binding; Peroxisome;
KW Reference proteome; Tricarboxylic acid cycle.
FT CHAIN 1..538
FT /note="Isocitrate lyase"
FT /id="PRO_0000068783"
FT ACT_SITE 206
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 97..99
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 168
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 207..208
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 243
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 423..427
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT BINDING 457
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P9WKK7"
FT CONFLICT 68..69
FT /note="EK -> D (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="G -> GE (in Ref. 1; AAR15146)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 538 AA; 60244 MW; 5FC535DE4C376D6F CRC64;
MGFLEDEDQK YWDDVQAVKA WWKDSRWRYT KRPYTAEQIV AKRGNLKIHY PSNDQSKKLW
KILESNFEKK VASFTYGCLE PTMLTQMAKY LDTVYVSGWQ SSSTASSTDE PSPDLADYPM
NTVPNKVNQL FMAQLFHDRK QREERITTPK DQRSKLPNID YLRPIIADAD TGHGGLTAVM
KLTKLFIERG AAGIHIEDQA PGTKKCGHMA GKVLVPISEH INRLVAIRAQ ADIMGTDLLA
IARTDSEAAT LITSTIDHRD HAFIVGSTNP NLQPLNDLML AGEQAGKTGE ELQAIEDQWI
AQAGLKLFDD AVVDTIKAGV HVNKDALIKE YLTAAKGKSN SEARAIAKGI TGVDIYWDWD
APRTREGYYR YQGGTQCAIN RAVAYAPFAD LIWMESKLPD YAQAKEFADG VHAVWPEQKL
AYNLSPSFNW KKAMPREEQE TYIKRLGALG YAWQFITLAG LHTTALISDQ FARAYAKQGM
RAYGELVQEP EMEQGVDVVT HQKWSGANYV DNMLKMLTGG VSSTAAMGKG VTEDQFKH
