ACEA_EMENI
ID ACEA_EMENI Reviewed; 538 AA.
AC P28298; C8VFW4; Q5B1E6;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 3.
DT 03-AUG-2022, entry version 151.
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=acuD {ECO:0000303|PubMed:1531185}; ORFNames=AN5634;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=R153;
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=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), AND SUBUNIT.
RX PubMed=10801489; DOI=10.1016/s0969-2126(00)00117-9;
RA Britton K.L., Langridge S.J., Baker P.J., Weeradechapon K.,
RA Sedelnikova S.E., De Lucas J.R., Rice D.W., Turner G.;
RT "The crystal structure and active site location of isocitrate lyase from
RT the fungus Aspergillus nidulans.";
RL Structure 8:349-362(2000).
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:0000269|PubMed:10801489}.
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; X62696; CAA44572.1; -; Genomic_DNA.
DR EMBL; AACD01000098; EAA62727.1; -; Genomic_DNA.
DR EMBL; BN001305; CBF81510.1; -; Genomic_DNA.
DR PIR; S26857; S26857.
DR RefSeq; XP_663238.1; XM_658146.1.
DR PDB; 1DQU; X-ray; 2.80 A; A=1-538.
DR PDBsum; 1DQU; -.
DR AlphaFoldDB; P28298; -.
DR SMR; P28298; -.
DR STRING; 162425.CADANIAP00003436; -.
DR EnsemblFungi; CBF81510; CBF81510; ANIA_05634.
DR EnsemblFungi; EAA62727; EAA62727; AN5634.2.
DR GeneID; 2871925; -.
DR KEGG; ani:AN5634.2; -.
DR VEuPathDB; FungiDB:AN5634; -.
DR eggNOG; KOG1260; Eukaryota.
DR HOGENOM; CLU_019214_2_2_1; -.
DR InParanoid; P28298; -.
DR OMA; LEKDWAE; -.
DR OrthoDB; 905115at2759; -.
DR UniPathway; UPA00703; UER00719.
DR EvolutionaryTrace; P28298; -.
DR Proteomes; UP000000560; Chromosome V.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0009514; C:glyoxysome; IEA:UniProtKB-SubCell.
DR GO; GO:0005782; C:peroxisomal matrix; IDA:AspGD.
DR GO; GO:0005777; C:peroxisome; IDA:AspGD.
DR GO; GO:0004451; F:isocitrate lyase activity; ISO: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:0045733; P:acetate catabolic process; IMP:AspGD.
DR GO; GO:0015976; P:carbon utilization; IMP:AspGD.
DR GO; GO:0009062; P:fatty acid catabolic process; IMP:AspGD.
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 1: Evidence at protein level;
KW 3D-structure; Glyoxylate bypass; Glyoxysome; Lyase; Magnesium;
KW Metal-binding; Peroxisome; Reference proteome; Tricarboxylic acid cycle.
FT CHAIN 1..538
FT /note="Isocitrate lyase"
FT /id="PRO_0000068790"
FT ACT_SITE 206
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:10801489"
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 17
FT /note="Missing (in Ref. 1; CAA44572)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="Missing (in Ref. 1; CAA44572)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="A -> T (in Ref. 1; CAA44572)"
FT /evidence="ECO:0000305"
FT HELIX 3..16
FT /evidence="ECO:0007829|PDB:1DQU"
FT HELIX 18..22
FT /evidence="ECO:0007829|PDB:1DQU"
FT HELIX 25..29
FT /evidence="ECO:0007829|PDB:1DQU"
FT HELIX 36..42
FT /evidence="ECO:0007829|PDB:1DQU"
FT HELIX 52..69
FT /evidence="ECO:0007829|PDB:1DQU"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:1DQU"
FT HELIX 81..90
FT /evidence="ECO:0007829|PDB:1DQU"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:1DQU"
FT HELIX 98..104
FT /evidence="ECO:0007829|PDB:1DQU"
FT HELIX 122..146
FT /evidence="ECO:0007829|PDB:1DQU"
FT HELIX 150..153
FT /evidence="ECO:0007829|PDB:1DQU"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:1DQU"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:1DQU"
FT HELIX 176..188
FT /evidence="ECO:0007829|PDB:1DQU"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:1DQU"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:1DQU"
FT HELIX 217..233
FT /evidence="ECO:0007829|PDB:1DQU"
FT STRAND 239..243
FT /evidence="ECO:0007829|PDB:1DQU"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:1DQU"
FT STRAND 249..253
FT /evidence="ECO:0007829|PDB:1DQU"
FT HELIX 258..263
FT /evidence="ECO:0007829|PDB:1DQU"
FT STRAND 264..267
FT /evidence="ECO:0007829|PDB:1DQU"
FT HELIX 275..284
FT /evidence="ECO:0007829|PDB:1DQU"
FT HELIX 290..302
FT /evidence="ECO:0007829|PDB:1DQU"
FT HELIX 309..317
FT /evidence="ECO:0007829|PDB:1DQU"
FT HELIX 324..335
FT /evidence="ECO:0007829|PDB:1DQU"
FT HELIX 340..351
FT /evidence="ECO:0007829|PDB:1DQU"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:1DQU"
FT HELIX 375..385
FT /evidence="ECO:0007829|PDB:1DQU"
FT STRAND 390..393
FT /evidence="ECO:0007829|PDB:1DQU"
FT HELIX 401..412
FT /evidence="ECO:0007829|PDB:1DQU"
FT STRAND 419..423
FT /evidence="ECO:0007829|PDB:1DQU"
FT STRAND 426..428
FT /evidence="ECO:0007829|PDB:1DQU"
FT HELIX 430..432
FT /evidence="ECO:0007829|PDB:1DQU"
FT HELIX 436..440
FT /evidence="ECO:0007829|PDB:1DQU"
FT HELIX 442..448
FT /evidence="ECO:0007829|PDB:1DQU"
FT STRAND 451..456
FT /evidence="ECO:0007829|PDB:1DQU"
FT HELIX 459..478
FT /evidence="ECO:0007829|PDB:1DQU"
FT HELIX 480..486
FT /evidence="ECO:0007829|PDB:1DQU"
FT HELIX 488..494
FT /evidence="ECO:0007829|PDB:1DQU"
FT HELIX 497..499
FT /evidence="ECO:0007829|PDB:1DQU"
FT HELIX 501..505
FT /evidence="ECO:0007829|PDB:1DQU"
FT HELIX 507..518
FT /evidence="ECO:0007829|PDB:1DQU"
SQ SEQUENCE 538 AA; 60321 MW; 21B5B56E5345681E CRC64;
MSYIEEEDQR YWDEVAAVKN WWKDSRWRYT KRPFTAEQIV AKRGNLKIEY PSNVQAKKLW
GILERNFKNK EASFTYGCLD PTMVTQMAKY LDTVYVSGWQ SSSTASSTDE PSPDLADYPM
NTVPNKVNHL WMAQLFHDRK QREERMTTPK DQRHKVANVD YLRPIIADAD TGHGGLTAVM
KLTKLFVERG AAGIHIEDQA PGTKKCGHMA GKVLVPISEH INRLVAIRAQ ADIMGTDLLA
IARTDSEAAT LITSTIDHRD HPFIIGSTNP DIQPLNDLMV MAEQAGKNGA ELQAIEDEWL
AKAGLKLFND AVVDAINNSP LPNKKAAIEK YLTQSKGKSN LEARAIAKEI AGTDIYFDWE
APRTREGYYR YQGGTQCAIN RAVAYAPFAD LIWMESKLPD YKQAKEFADG VHAVWPEQKL
AYNLSPSFNW KKAMPRDEQE TYIKRLGALG YAWQFITLAG LHTTALISDT FAKAYAKQGM
RAYGELVQEP EMANGVDVVT HQKWSGANYV DNMLKMITGG VSSTAAMGKG VTEDQFKS
