ID A0A0N5C7C7_STREA Unreviewed; 365 AA.
AC A0A0N5C7C7;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Isocitrate dehydrogenase [NAD] subunit, mitochondrial {ECO:0000256|RuleBase:RU361266};
OS Strongyloides papillosus (Intestinal threadworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=174720 {ECO:0000313|Proteomes:UP000046392, ECO:0000313|WBParaSite:SPAL_0001384100.1};
RN [1] {ECO:0000313|WBParaSite:SPAL_0001384100.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173,
CC ECO:0000256|RuleBase:RU361266}.
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. {ECO:0000256|ARBA:ARBA00007769,
CC ECO:0000256|RuleBase:RU361266}.
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DR AlphaFoldDB; A0A0N5C7C7; -.
DR STRING; 174720.A0A0N5C7C7; -.
DR WBParaSite; SPAL_0001384100.1; SPAL_0001384100.1; SPAL_0001384100.
DR Proteomes; UP000046392; Unplaced.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR InterPro; IPR004434; Isocitrate_DH_NAD.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR NCBIfam; TIGR00175; mito_nad_idh; 1.
DR PANTHER; PTHR11835; DECARBOXYLATING DEHYDROGENASES-ISOCITRATE, ISOPROPYLMALATE, TARTRATE; 1.
DR PANTHER; PTHR11835:SF80; ISOCITRATE DEHYDROGENASE [NAD] SUBUNIT BETA, 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 Mitochondrion {ECO:0000256|RuleBase:RU361266};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946,
KW ECO:0000256|RuleBase:RU361266};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532,
KW ECO:0000256|RuleBase:RU361266}.
FT DOMAIN 31..359
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 365 AA; 40687 MW; E3A739D15BB11BD0 CRC64;
MTSLGRVLVN IGKRSLCTST SPIDEVAKKV NVCLIPGDGV GPELTQSVQE VIKHTGIPIE
FEEVFVSGIH YKRSTRLSDV LEALRRNNNV CLKGVIQESV YNRDNELKGL NMKMRRELDL
FANVVHIKTM EGIKTRHGKE LDFIIIREQT EGEYSAIEHE SVPGVIECLK ISTRPKIERI
AKFAFDYAMK YNRKKVTCVH KANIMKLGDG LFLKICQDTA KLYPKLKFES MIVDNTCMQL
VSNPDQFDVM VMPNLYGNII DNLAAGLVGG AGVVPSKSIG SDFVMFEPGS KHSFQQALGR
DIANPTAMIL ACANLLHHIH LDTYSDALRK AVEKTIKEGK VRTRDLGGYD SSTDFTFAVI
DNYSL
//
