ID A0A0R3QW21_9BILA Unreviewed; 305 AA.
AC A0A0R3QW21;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Iso_dh domain-containing protein {ECO:0000313|WBParaSite:BTMF_0001192901-mRNA-1};
GN ORFNames=BTMF_LOCUS9957 {ECO:0000313|EMBL:VDO33784.1};
OS Brugia timori.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX NCBI_TaxID=42155 {ECO:0000313|Proteomes:UP000050602, ECO:0000313|WBParaSite:BTMF_0001192901-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:BTMF_0001192901-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDO33784.1, ECO:0000313|Proteomes:UP000280834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. {ECO:0000256|ARBA:ARBA00007769}.
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DR EMBL; UZAG01017261; VDO33784.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R3QW21; -.
DR STRING; 42155.A0A0R3QW21; -.
DR WBParaSite; BTMF_0001192901-mRNA-1; BTMF_0001192901-mRNA-1; BTMF_0001192901.
DR Proteomes; UP000050602; Unplaced.
DR Proteomes; UP000280834; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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 GO; GO:0006099; P:tricarboxylic acid cycle; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000280834};
KW Signal {ECO:0000256|SAM:SignalP};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..305
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5033240464"
FT DOMAIN 36..305
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 305 AA; 33602 MW; FC423289964AF150 CRC64;
MLLIHQRLAF LLVQTVKRCA SVRGIASTVR PQRKMKVTVI PGDGVGAELT HAVQKIVQST
GIPLEFEEVF LSEIEHSCSA SLEEVIKIVR KNNNVALKGA IKEAEETVSD PDREDINRSL
KKGLDLFAGV SNIKSLNGIK TRHQKNLDFV IIREQTEGEY SSLEHELVPG VVECLKISTE
EKSYRIAKFA FDYATKFGRH KVTAIHKANI MKLGDGLFLR TCEEVSKLYP NIKFESMIID
NCCMQLVSRP EQFDVMVMPN LYGNIVGNLG AGLVGGAGVV AGRSIGSDAV IFEPGARHAY
QQAFG
//
