ID A0A139H034_9PEZI Unreviewed; 366 AA.
AC A0A139H034;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=3-isopropylmalate dehydrogenase {ECO:0000256|ARBA:ARBA00013101};
DE EC=1.1.1.85 {ECO:0000256|ARBA:ARBA00013101};
GN ORFNames=AC578_6269 {ECO:0000313|EMBL:KXS95817.1};
OS Pseudocercospora eumusae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=321146 {ECO:0000313|EMBL:KXS95817.1, ECO:0000313|Proteomes:UP000070133};
RN [1] {ECO:0000313|EMBL:KXS95817.1, ECO:0000313|Proteomes:UP000070133}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114824 {ECO:0000313|EMBL:KXS95817.1,
RC ECO:0000313|Proteomes:UP000070133};
RA Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT link between parallel evolutionary changes in Pseudocercospora fijiensis
RT and Pseudocercospora eumusae and increased virulence on the banana host.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. {ECO:0000256|ARBA:ARBA00007769}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KXS95817.1}.
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DR EMBL; LFZN01000199; KXS95817.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A139H034; -.
DR STRING; 321146.A0A139H034; -.
DR OrthoDB; 2606404at2759; -.
DR Proteomes; UP000070133; Unassembled WGS sequence.
DR GO; GO:0003862; F:3-isopropylmalate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR InterPro; IPR004429; Isopropylmalate_DH.
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.
DR PROSITE; PS00470; IDH_IMDH; 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 Reference proteome {ECO:0000313|Proteomes:UP000070133}.
FT DOMAIN 20..354
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 366 AA; 39001 MW; 2C468DEC2D8B576E CRC64;
MSATHAANGP TVPPPAKGGK ILVLPGDHIG PEVVTEALKV LDIIEEATGT KFERDFDLCG
GCSLDKHKDS VTEAVLQKCE KVDAVFFGSA GGPEWGTAQP NPESGLLRIR KRMQASVDFM
LIRENCGGAY YGKKIEEQDY ACDPWEYSRA EIERVARVAG ALALQHDPPL PVFSADKANV
LANSRVWRRV VSEVFEKEFP AVKLQHQLAD SLAMLLITRP KAFNGVIVTD NTFGDILSDE
SGGLTGSLGL LPSASLAGAP GTSLGQNSVG GVVGLYEPVH GSAPDISGKG LANPVAQVLS
LAMMLRYSFN MHREADVVED AVARVLDAKK DGGLEVRTGD LGGKATTKDM SEAIQGEVKR
LLKERP
//
