UniProt: A0A0D2CD98

Database: UniProt
Entry: A0A0D2CD98_9EURO

LinkDB:  A0A0D2CD98_9EURO 
Original site:  A0A0D2CD98_9EURO

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Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (6)   
   InterPro (3)   
   Pfam (1)   
   PROSITE (1)   
   SMART (1)   
All databases (14)   

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ID   A0A0D2CD98_9EURO        Unreviewed;       371 AA.
AC   A0A0D2CD98;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=3-isopropylmalate dehydrogenase {ECO:0000256|ARBA:ARBA00013101, ECO:0000256|RuleBase:RU004445};
DE            EC=1.1.1.85 {ECO:0000256|ARBA:ARBA00013101, ECO:0000256|RuleBase:RU004445};
GN   ORFNames=PV07_07971 {ECO:0000313|EMBL:KIW28295.1};
OS   Cladophialophora immunda.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Cladophialophora.
OX   NCBI_TaxID=569365 {ECO:0000313|EMBL:KIW28295.1, ECO:0000313|Proteomes:UP000054466};
RN   [1] {ECO:0000313|EMBL:KIW28295.1, ECO:0000313|Proteomes:UP000054466}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 83496 {ECO:0000313|EMBL:KIW28295.1,
RC   ECO:0000313|Proteomes:UP000054466};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Cladophialophora immunda CBS83496.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-
CC       methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-
CC       oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.
CC       {ECO:0000256|RuleBase:RU004445}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentanoate
CC         + CO2 + NADH; Xref=Rhea:RHEA:32271, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:17865, ChEBI:CHEBI:35121, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.1.1.85;
CC         Evidence={ECO:0000256|RuleBase:RU004445};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU004445};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|RuleBase:RU004445};
CC       Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit.
CC       {ECO:0000256|RuleBase:RU004445};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC       from 3-methyl-2-oxobutanoate: step 3/4.
CC       {ECO:0000256|RuleBase:RU004445}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738,
CC       ECO:0000256|RuleBase:RU004445}.
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; KN847043; KIW28295.1; -; Genomic_DNA.
DR   RefSeq; XP_016248511.1; XM_016395092.1.
DR   AlphaFoldDB; A0A0D2CD98; -.
DR   STRING; 569365.A0A0D2CD98; -.
DR   GeneID; 27347165; -.
DR   VEuPathDB; FungiDB:PV07_07971; -.
DR   HOGENOM; CLU_031953_0_3_1; -.
DR   OrthoDB; 2606404at2759; -.
DR   UniPathway; UPA00048; UER00072.
DR   Proteomes; UP000054466; 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-UniPathway.
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   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.
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   ECO:0000256|RuleBase:RU004445};
KW   Leucine biosynthesis {ECO:0000256|ARBA:ARBA00022430,
KW   ECO:0000256|RuleBase:RU004445}; Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU004445};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU004445};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU004443};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054466}.
FT   DOMAIN          5..360
FT                   /note="Isopropylmalate dehydrogenase-like"
FT                   /evidence="ECO:0000259|SMART:SM01329"
SQ   SEQUENCE   371 AA;  40117 MW;  CC67D2D9142BB43D CRC64;
     MPTYNIVVFA GDYAGPEVTK EAVKVLKVVE KCSKDVKFNF QDHLLGGCSI DAHGTPLTDE
     ALSAAKSAHA VLLGAIGGPR YGVGKVRPEQ GLLKLRKEMG TFGNLRPCFF ASPSLASRSP
     LKEEVCQGTD FMIVRELTGG IYFGERIEGK PEDGENEWAE DREPYSRKEI ERITRLAAYL
     ALAKNPPSKV WSLDKANVLA TSRLWRRVFT ETMQKEFPQL QFEHQLIDSA AMIMVKNPRA
     LNGVIVTSNL FGDIISDEAS VIPGSLGLLP SASLSGVPDG KGHCNGIYEP IHGSAPDIAG
     KGVINPVAAI LSVAMLLLYS LNLPRESLLV EQAVKIVIEK GIVTKDIGGE SSTVEVGDAV
     ARELESLFKD L
//

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