LEUC_USTMA
ID LEUC_USTMA Reviewed; 773 AA.
AC P49601; A0A0D1CFW1; Q4P1K3;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 129.
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; ORFNames=UMAG_06010;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8125330; DOI=10.1016/0378-1119(94)90743-9;
RA Rubin B.P., Li D., Holloman W.K.;
RT "The LEU1 gene of Ustilago maydis.";
RL Gene 140:131-135(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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; L20832; AAA34226.1; -; Genomic_DNA.
DR EMBL; CM003160; KIS65923.1; -; Genomic_DNA.
DR RefSeq; XP_011392387.1; XM_011394085.1.
DR AlphaFoldDB; P49601; -.
DR SMR; P49601; -.
DR STRING; 5270.UM06010P0; -.
DR EnsemblFungi; KIS65923; KIS65923; UMAG_06010.
DR GeneID; 23565739; -.
DR KEGG; uma:UMAG_06010; -.
DR VEuPathDB; FungiDB:UMAG_06010; -.
DR eggNOG; KOG0454; Eukaryota.
DR HOGENOM; CLU_006714_1_2_1; -.
DR InParanoid; P49601; -.
DR OMA; DHIVNEQ; -.
DR OrthoDB; 265826at2759; -.
DR BioCyc; MetaCyc:MON-17191; -.
DR UniPathway; UPA00048; UER00071.
DR Proteomes; UP000000561; Chromosome 21.
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..773
FT /note="3-isopropylmalate dehydratase"
FT /id="PRO_0000076893"
FT BINDING 355
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 415
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"
SQ SEQUENCE 773 AA; 83224 MW; A936D8D1990DDC1C CRC64;
MAPKTLYEKI FDSHLVHEEA DGTCLIYIDR HLVHEVTSPQ AFEGLRNANR KVRRTDCTLA
TVDHNIPTAS RKSYRDTKSF VEQVDSRTQC MTLEENVKAF GLTFFGLSDN RQGIVHIIGP
EQGFTLPGAT IVCGDSHTST HGAFGALAFG IGTSEVEHVL ATQTLLQKRA KNMLIQVDGE
LSQGVTSKDI ILHIIGLIGT AGGTGHVIEY AGSTIRSLSM EARMSICNMS IEAGARAGLI
APDEITYEYI KGRPLAPKQG EAWDQALAYW KTLPSDEGAQ YDTVIKIDAK DIPPTVTWGT
SPQDVVAITG TVPDPKNASN EAEAKAWTRA LEYMGLEAGT PMEKIKIDKV FIGSCTNARI
EDLRAAARVL HGRKVADGLY CMLVPGSGLV KKQAEAEGLD KIFQAAGFDW REAGCSMCLG
MNPDQLAPGE RCASTSNRNF EGRQGAGGRT HLMSPAMAAA CAVTGYLTDV RKVVGHSSAK
VGSDAAKPAF EIEVSDAKSY LVDATPAPAP TNVAAAGAGA LTDEDALRDV PASHISSSGG
GMEKFTTLTG IAAPLERSNV DTDLIIPKQF LKTIKRTGLG SALFWPLRYD AKTGEPDPAF
VLNQKPYDQS KILVVTGPNF GCGSSREHAA WSLLDFGIRA VIAESFGDIF RNNLTKNGQL
PVVLSRAQIQ RLTQDAKAGK QITVDLVDQL VITADGKEKF SFETPEFTRH CLINGLDDIA
LTLQRDAQIG AFERNRSTHT PWLDGFGYHA NSNSSSLLDS AKPLVNNVTA TDW
