ID A0A168DW45_CORDF Unreviewed; 383 AA.
AC A0A168DW45;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 13-SEP-2023, entry version 21.
DE SubName: Full=3-isopropylmalate dehydrogenase {ECO:0000313|EMBL:OAA73078.1};
GN ORFNames=LEL_08862 {ECO:0000313|EMBL:OAA73078.1};
OS Akanthomyces lecanii RCEF 1005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Akanthomyces;
OC Cordyceps confragosa.
OX NCBI_TaxID=1081108 {ECO:0000313|EMBL:OAA73078.1, ECO:0000313|Proteomes:UP000076881};
RN [1] {ECO:0000313|EMBL:OAA73078.1, ECO:0000313|Proteomes:UP000076881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA73078.1,
RC ECO:0000313|Proteomes:UP000076881};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. {ECO:0000256|ARBA:ARBA00007769,
CC ECO:0000256|RuleBase:RU004443}.
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:OAA73078.1}.
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DR EMBL; AZHF01000007; OAA73078.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A168DW45; -.
DR STRING; 1081108.A0A168DW45; -.
DR OrthoDB; 2606404at2759; -.
DR Proteomes; UP000076881; 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:SF4; 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 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:UP000076881}.
FT DOMAIN 7..371
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 383 AA; 40330 MW; 0DB1A2DB3150BCBA CRC64;
MATGAFKILV LPGDHVGPEV VREALRVLDV VQECRPGLTF NITTGLAGGC SLDAHGVAIT
EEVLEQAAQS DAVLFGSVGG PKWATTVPNP ESGLLLLRKK LDAFANLRPC NIIVPALVGA
SPIKADLVKG TNFIVVRENC GGAYFGTKVE EADVASDLWV YTPKEVERCG RVAAAVARIM
TRPEDATGNH NKPAVVWSAD KANVLASGRL WRRATTSLFE REYPDIELRH QLADSMAMLM
VRNPRGFNGV IHTDNTFGDI LSDISGAIVG TLGTLPSASL SGIPGEGKCN GIYEPVHGSA
PDIASKGIVN PVAQILSLAM LLRYSCLLVD EAAAIEAAVA KVLDDKSQGG LEIRTGDMGG
KASTAELGSA VCGVLRERLN KRA
//
