ID D2VQ70_NAEGR Unreviewed; 361 AA.
AC D2VQ70;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Isocitrate dehydrogenase {ECO:0000313|EMBL:EFC40994.1};
GN ORFNames=NAEGRDRAFT_80807 {ECO:0000313|EMBL:EFC40994.1};
OS Naegleria gruberi (Amoeba).
OC Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC Vahlkampfiidae; Naegleria.
OX NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671};
RN [1] {ECO:0000313|EMBL:EFC40994.1, ECO:0000313|Proteomes:UP000006671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC40994.1,
RC ECO:0000313|Proteomes:UP000006671};
RX PubMed=20211133; DOI=10.1016/j.cell.2010.01.032;
RA Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B., Carpenter M.L.,
RA Field M.C., Kuo A., Paredez A., Chapman J., Pham J., Shu S., Neupane R.,
RA Cipriano M., Mancuso J., Tu H., Salamov A., Lindquist E., Shapiro H.,
RA Lucas S., Grigoriev I.V., Cande W.Z., Fulton C., Rokhsar D.S., Dawson S.C.;
RT "The genome of Naegleria gruberi illuminates early eukaryotic
RT versatility.";
RL Cell 140:631-642(2010).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. {ECO:0000256|ARBA:ARBA00007769}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GG738888; EFC40994.1; -; Genomic_DNA.
DR RefSeq; XP_002673738.1; XM_002673692.1.
DR AlphaFoldDB; D2VQ70; -.
DR STRING; 5762.D2VQ70; -.
DR EnsemblProtists; EFC40994; EFC40994; NAEGRDRAFT_80807.
DR GeneID; 8855701; -.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_80807; -.
DR eggNOG; KOG0785; Eukaryota.
DR InParanoid; D2VQ70; -.
DR OMA; CVRPCRY; -.
DR OrthoDB; 143577at2759; -.
DR Proteomes; UP000006671; 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 GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
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: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 Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000006671};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 32..357
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 361 AA; 39121 MW; D8D0265279FDB2E9 CRC64;
MFKRASSSLL RSAFTTQQQR FFSTQSSLLQ QKITATLFPG HGIGPEISAA VVKILDAAGA
NISWETHDIG VPQPGSVDLI SPEALASVRK NKVGLKGPLA TPIGKGYRSL NITLRQALEL
YANVRPAVSI PAIKTGYPHV DVVVVRENTE GEYSGLEHEV VPGVVESLKV ITQKSSMRIA
EYAFRYASEN SRKKVTAVHK ANIMKMSDGL FLECCREVAK KYPNIKYEEV IVDACCMKLV
RYPQEFDVCV TPNLYGDILS DLCAGLIGGL GLTPSGNFGE HASVFEAVHG TAPDIAGQDK
ANPTALLLSA LMMLRHLQMH DTAARIEKSV MKVLTEGKVL TGDLGGKSTC SEYTNEIIKN
L
//
