ID E6ZTU7_SPORE Unreviewed; 379 AA.
AC E6ZTU7;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Probable LEU2-beta-isopropyl-malate dehydrogenase {ECO:0000313|EMBL:CBQ70654.1};
GN ORFNames=sr10322 {ECO:0000313|EMBL:CBQ70654.1};
OS Sporisorium reilianum (strain SRZ2) (Maize head smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Sporisorium.
OX NCBI_TaxID=999809 {ECO:0000313|EMBL:CBQ70654.1, ECO:0000313|Proteomes:UP000008867};
RN [1] {ECO:0000313|EMBL:CBQ70654.1, ECO:0000313|Proteomes:UP000008867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRZ2 {ECO:0000313|Proteomes:UP000008867};
RX PubMed=21148393; DOI=10.1126/science.1195330;
RA Schirawski J., Mannhaupt G., Muench K., Brefort T., Schipper K.,
RA Doehlemann G., Di Stasio M., Roessel N., Mendoza-Mendoza A., Pester D.,
RA Mueller O., Winterberg B., Meyer E., Ghareeb H., Wollenberg T.,
RA Muensterkoetter M., Wong P., Walter M., Stukenbrock E., Gueldener U.,
RA Kahmann R.;
RT "Pathogenicity determinants in smut fungi revealed by genome comparison.";
RL Science 330:1546-1548(2010).
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. {ECO:0000256|ARBA:ARBA00007769,
CC ECO:0000256|RuleBase:RU004443}.
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DR EMBL; FQ311441; CBQ70654.1; -; Genomic_DNA.
DR AlphaFoldDB; E6ZTU7; -.
DR EnsemblFungi; CBQ70654; CBQ70654; sr10322.
DR VEuPathDB; FungiDB:sr10322; -.
DR eggNOG; KOG0786; Eukaryota.
DR HOGENOM; CLU_031953_0_3_1; -.
DR OrthoDB; 2606404at2759; -.
DR Proteomes; UP000008867; Chromosome 2.
DR GO; GO:0003862; F:3-isopropylmalate dehydrogenase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR InterPro; IPR004429; Isopropylmalate_DH.
DR NCBIfam; TIGR00169; leuB; 1.
DR PANTHER; PTHR42979; 3-ISOPROPYLMALATE DEHYDROGENASE; 1.
DR PANTHER; PTHR42979:SF1; 3-ISOPROPYLMALATE DEHYDROGENASE; 1.
DR Pfam; PF00180; Iso_dh; 1.
DR SMART; SM01329; Iso_dh; 1.
DR SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Leucine biosynthesis {ECO:0000256|ARBA:ARBA00022430};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU004443}.
FT DOMAIN 7..371
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 379 AA; 40297 MW; 9CD6F2FD20ED57AD CRC64;
MSKQQYNVVV LPGDGIGPEV VEQATRVLEL ISSKSDSFSI NLKSYDFGGC AIDSTGKPLP
DDTLEACKNA DAILMGSVGG PKWGVGKVRP EQGLLALRKE LDLYANIRPC LFPSESLLSH
SPLKPEVAKG VSFIVVRELV KGLYFGDRQE ADLDDPASDG AAFDTMVYNK HDVERITKLA
SYLALQSNPP APLHSIDKAN VLATSRLWRR VVQSTVDTQF ADKGITVDHQ LVDSASMVMV
SNPRKLNGIV LTENMFGDIL SDESSVIPGA LGLLPSASLS GLPDGKGKCN GLYEPIHGSA
PDIAGKGIAN PIGTILSAAM LLRYSLNQPE LASKVEDAVR KVLDAKDVGG LELRTADLGG
KHGSKDVGDQ VIAVLESLL
//
