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Database: UniProt
Entry: A0A098VQR8_9MICR
LinkDB: A0A098VQR8_9MICR
Original site: A0A098VQR8_9MICR 
ID   A0A098VQR8_9MICR        Unreviewed;       132 AA.
AC   A0A098VQR8;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Isopropylmalate dehydrogenase-like domain-containing protein {ECO:0000259|SMART:SM01329};
GN   ORFNames=DI09_3p670 {ECO:0000313|EMBL:KGG51305.1};
OS   Mitosporidium daphniae.
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Mitosporidium.
OX   NCBI_TaxID=1485682 {ECO:0000313|EMBL:KGG51305.1, ECO:0000313|Proteomes:UP000029725};
RN   [1] {ECO:0000313|EMBL:KGG51305.1, ECO:0000313|Proteomes:UP000029725}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UGP3 {ECO:0000313|EMBL:KGG51305.1,
RC   ECO:0000313|Proteomes:UP000029725};
RC   TISSUE=Spores {ECO:0000313|EMBL:KGG51305.1};
RA   Haag K.L., James T.Y., Larsson R., Schaer T.M., Refardt D., Pombert J.-F.,
RA   Ebert D.;
RT   "A new species of microsporidia sheds light on the evolution of extreme
RT   parasitism.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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:KGG51305.1}.
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DR   EMBL; JMKJ01000333; KGG51305.1; -; Genomic_DNA.
DR   RefSeq; XP_013237732.1; XM_013382278.1.
DR   AlphaFoldDB; A0A098VQR8; -.
DR   GeneID; 25259869; -.
DR   VEuPathDB; MicrosporidiaDB:DI09_3p670; -.
DR   HOGENOM; CLU_031953_0_4_1; -.
DR   OrthoDB; 143577at2759; -.
DR   Proteomes; UP000029725; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR   PANTHER; PTHR11835; DECARBOXYLATING DEHYDROGENASES-ISOCITRATE, ISOPROPYLMALATE, TARTRATE; 1.
DR   PANTHER; PTHR11835:SF34; ISOCITRATE DEHYDROGENASE [NAD] SUBUNIT ALPHA, MITOCHONDRIAL; 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   Reference proteome {ECO:0000313|Proteomes:UP000029725}.
FT   DOMAIN          1..121
FT                   /note="Isopropylmalate dehydrogenase-like"
FT                   /evidence="ECO:0000259|SMART:SM01329"
SQ   SEQUENCE   132 AA;  13840 MW;  ADFA5C5D2E4936AD CRC64;
     MVQTPSLFKD AVLVMPNLYG DILSDLCAGL VGGLGLTPSG NIGSDGAIFE SVHGTAPDIA
     GKDIANPTAL LLSSVMMLKY MKMNTFANRI YSAVLDTISE GRYRTRDLGG TSSTSDFTGA
     ICDRLVLSEA SN
//
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