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Database: UniProt
Entry: A0A0M3K1H4_ANISI
LinkDB: A0A0M3K1H4_ANISI
Original site: A0A0M3K1H4_ANISI 
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
//
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