ID A0A0M3K1H4_ANISI Unreviewed; 656 AA.
AC A0A0M3K1H4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 2.
DT 13-SEP-2023, entry version 26.
DE RecName: Full=Isocitrate dehydrogenase [NAD] subunit, mitochondrial {ECO:0000256|RuleBase:RU361266};
GN ORFNames=ASIM_LOCUS14128 {ECO:0000313|EMBL:VDK51564.1};
OS Anisakis simplex (Herring worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Anisakidae; Anisakis;
OC Anisakis simplex complex.
OX NCBI_TaxID=6269 {ECO:0000313|Proteomes:UP000036680, ECO:0000313|WBParaSite:ASIM_0001471801-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:ASIM_0001471801-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDK51564.1, ECO:0000313|Proteomes:UP000267096}
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 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 EMBL; UYRR01031628; VDK51564.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M3K1H4; -.
DR WBParaSite; ASIM_0001471801-mRNA-1; ASIM_0001471801-mRNA-1; ASIM_0001471801.
DR Proteomes; UP000036680; Unplaced.
DR Proteomes; UP000267096; Unassembled WGS sequence.
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 InterPro; IPR024326; RRP7_C.
DR NCBIfam; TIGR00175; mito_nad_idh; 1.
DR PANTHER; PTHR11835; DECARBOXYLATING DEHYDROGENASES-ISOCITRATE, ISOPROPYLMALATE, TARTRATE; 1.
DR PANTHER; PTHR11835:SF60; ISOCITRATE DEHYDROGENASE [NAD] SUBUNIT GAMMA, MITOCHONDRIAL; 1.
DR Pfam; PF00180; Iso_dh; 1.
DR Pfam; PF12923; RRP7; 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 Reference proteome {ECO:0000313|Proteomes:UP000267096};
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 298..611
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
FT REGION 80..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 630..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..115
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 656 AA; 73757 MW; FD0C2EB01511A06C CRC64;
MTNTNLRCVF VTKRQLFECN TGEPPIRLAH CESGMARALR QVLTMVLKAV KKLKSAKHEG
RSKKRTISKG EKQLNDDIEH EIFDKTNNDE SEESQKLTKR VGDKRKKLKR TEQTLKKRKR
SQDETIVDDG IESSSEQCKT SAEDVRSVKI SNEEEFDATK LRGLLLKYRL SDIHSASRCL
FLKVDQSDPS ALLVHNIPPF IAVVKYVSEY RKAIVSPDEL QQRVDKFFEV YDKKVVEEKR
KAKKMHNVPD EEGWITVTRS RFKPVPAAVV VKNKDDLLKL TKNKKKLTPL GKYGGRHTVT
VLPGDGIGPE MVSHLERIFR FANVPVDFEE VPLTTDSGQD DFEHALVSVK RNGVALKGNI
ETQFDDPSFT SRNVELRRRL DLFANVLHCS SIPTIRSKHQ NIDIVLIREN TEGEYSGLEH
EAVHGVVESI KIITRYNIER IARFAFEYAL LNNRKRVTCI HKANIQKLGD GLFLQVCREM
ASREYPSIQL DSMIVDNASM QLVSKPQQFD VMLMPNLYGN IISNIACGLV GGPGLVSGIN
IGCKYAVFET GTRNTGKELA GKDLANPTAF LCAGVDMLRY LHLQQHADLI SNALFKVGAL
LHRVCDYIRA LYPPPPPAYP PELYPPPPPI AYPPGRAYPP PPPGPPPPII PITGIS
//