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Database: UniProt
Entry: X0D0R8_FUSOX
LinkDB: X0D0R8_FUSOX
Original site: X0D0R8_FUSOX 
ID   X0D0R8_FUSOX            Unreviewed;       301 AA.
AC   X0D0R8;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=3-isopropylmalate dehydrogenase {ECO:0000313|EMBL:EXK97143.1};
GN   ORFNames=FOQG_02445 {ECO:0000313|EMBL:EXK97143.1};
OS   Fusarium oxysporum f. sp. raphani 54005.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=1089458 {ECO:0000313|EMBL:EXK97143.1, ECO:0000313|Proteomes:UP000030663};
RN   [1] {ECO:0000313|EMBL:EXK97143.1, ECO:0000313|Proteomes:UP000030663}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=54005 {ECO:0000313|EMBL:EXK97143.1,
RC   ECO:0000313|Proteomes:UP000030663};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA   Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA   Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Fusarium oxysporum PHW815.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
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; JH658364; EXK97143.1; -; Genomic_DNA.
DR   AlphaFoldDB; X0D0R8; -.
DR   HOGENOM; CLU_031953_0_3_1; -.
DR   Proteomes; UP000030663; Unassembled WGS sequence.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030663}.
FT   DOMAIN          5..301
FT                   /note="Isopropylmalate dehydrogenase-like"
FT                   /evidence="ECO:0000259|SMART:SM01329"
SQ   SEQUENCE   301 AA;  31941 MW;  9D89154C1C2F895A CRC64;
     MAEHNIVVFA GDHCGPEVIA EAIKVIKAVE DISPTAGKFN LEHLLLGGCS IDKTGTPLTD
     EALAAAKASD AVLLGAIGGP EWGTGAVRPE QGLLKLRSEM CAYGNLRPCF FASDALVETS
     PLKASVCRGV DMMLVRELTS GLYFGERKEY DGVNAFDTTV YTKPEIERIA RLGGYLAKTR
     GDSRVISLDK ANVLATSRLW RSVVDEVYKN EFPDLKVEHQ LIDSAAMIMV KNPTQLNGVM
     IAPNLAGDIL SDEASAITGS IGLLPSASLC GVPEVGSKVL SIYEPIHGSA PDISGKGIVV
     R
//
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