LEUC_ASHGO
ID LEUC_ASHGO Reviewed; 776 AA.
AC Q74ZM9;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=3-isopropylmalate dehydratase;
DE EC=4.2.1.33;
DE AltName: Full=Alpha-IPM isomerase;
DE Short=IPMI;
DE AltName: Full=Isopropylmalate isomerase;
GN Name=LEU1; OrderedLocusNames=AGR169W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 169 AND 482.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
CC -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate and 3-
CC isopropylmalate, via the formation of 2-isopropylmaleate.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate;
CC Xref=Rhea:RHEA:32287, ChEBI:CHEBI:1178, ChEBI:CHEBI:35121;
CC EC=4.2.1.33;
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 2/4.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000305}.
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DR EMBL; AE016820; AAS54659.2; -; Genomic_DNA.
DR RefSeq; NP_986835.2; NM_211897.2.
DR AlphaFoldDB; Q74ZM9; -.
DR SMR; Q74ZM9; -.
DR STRING; 33169.AAS54659; -.
DR EnsemblFungi; AAS54659; AAS54659; AGOS_AGR169W.
DR GeneID; 4623137; -.
DR KEGG; ago:AGOS_AGR169W; -.
DR eggNOG; KOG0454; Eukaryota.
DR HOGENOM; CLU_006714_1_0_1; -.
DR InParanoid; Q74ZM9; -.
DR OMA; DHIVNEQ; -.
DR UniPathway; UPA00048; UER00071.
DR Proteomes; UP000000591; Chromosome VII.
DR GO; GO:0009316; C:3-isopropylmalate dehydratase complex; IEA:InterPro.
DR GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01583; IPMI; 1.
DR CDD; cd01577; IPMI_Swivel; 1.
DR Gene3D; 3.20.19.10; -; 1.
DR Gene3D; 3.30.499.10; -; 2.
DR HAMAP; MF_01026; LeuC_type1; 1.
DR HAMAP; MF_01031; LeuD_type1; 1.
DR InterPro; IPR004430; 3-IsopropMal_deHydase_lsu.
DR InterPro; IPR004431; 3-IsopropMal_deHydase_ssu.
DR InterPro; IPR012235; 3-IsopropMal_deHydtase_ssu/lsu.
DR InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3.
DR InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba.
DR InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR InterPro; IPR018136; Aconitase_4Fe-4S_BS.
DR InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR InterPro; IPR033941; IPMI_cat.
DR InterPro; IPR033940; IPMI_Swivel.
DR Pfam; PF00330; Aconitase; 1.
DR Pfam; PF00694; Aconitase_C; 1.
DR PIRSF; PIRSF001418; ACN; 1.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; SSF53732; 1.
DR TIGRFAMs; TIGR00170; leuC; 1.
DR TIGRFAMs; TIGR00171; leuD; 1.
DR PROSITE; PS00450; ACONITASE_1; 1.
DR PROSITE; PS01244; ACONITASE_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW Iron; Iron-sulfur; Leucine biosynthesis; Lyase; Metal-binding;
KW Reference proteome.
FT CHAIN 1..776
FT /note="3-isopropylmalate dehydratase"
FT /id="PRO_0000233187"
FT REGION 482..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..541
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 357
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 418
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 421
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
SQ SEQUENCE 776 AA; 84553 MW; E1FF1A3F8AD3433E CRC64;
MMTNGAKTLY DKVFEAHIVH QDESGSCLLY IDRHLVHEVT SPQAFEGLKT AGRPVRRTDC
TLATVDHNIP TESRRHFRNT ESFIKEADSR LQVQTLEQNV KDFHVPYLGM SDERQGIVHI
IGPEQGFTLP GTTVVCGDSH TSTHGAFGAL AFGIGTSEVE HVLATQTVIQ SKSKNMRIHV
EGSLSPGITS KDLILHIIGV IGTAGGTGCV IEFTGQAIQE LTMEARMSMC NMAIEAGARA
GMIQPDETTF EYLKGRPLAP TGAEWEKAVT YWKTLKTDED AVFDISVTVK GADIRPTITW
GTSPQDALPI DAAVPDPANV SDPIKRSGME AALEYMGLEP NTLLKDIKID KVFIGSCTNA
RIEDLRAAAA VVDGHRIAPT VKRAMVVPGS GLVKKQAEAE GLDKIFEAAG FEWREAGCSM
CLGMNPDILG PKERCASTSN RNFEGRQGRL SRTHLMSPAM AAAAGIMGHF VDIREFEFKE
SSAPKVEVRH DTDSSTLEEA NYGHAKEEPP SAELSDVAKQ EKVNDIPVSN SSTQSPGSAP
SADAGLQPFL QLQGIAAPLD KANVDTDAII PKQFLKTIKR TGLKEGLFYD WRFAKHADGK
VTGTDFVLNR EPYRKATTLV VTGPNFGCGS SREHAPWALK DFGIMCIIAP SFGDIFYNNS
FKNGLLPIRL PQDVIKEKLY PIASAGGELV IDLPAQQIAD GEGHILVTQF DVEPSRKHCL
VNGLDDIGLT LQKERFIADY EAMRRRDFSF LEGGSKLLPR ISHSKPTSMP QAANDW
