ID M2XU59_GALSU Unreviewed; 373 AA.
AC M2XU59;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Isocitrate dehydrogenase (NAD+) {ECO:0000313|EMBL:EME26939.1};
DE EC=1.1.1.41 {ECO:0000313|EMBL:EME26939.1};
GN ORFNames=Gasu_55090 {ECO:0000313|EMBL:EME26939.1};
OS Galdieria sulphuraria (Red alga).
OC Eukaryota; Rhodophyta; Bangiophyceae; Galdieriales; Galdieriaceae;
OC Galdieria.
OX NCBI_TaxID=130081 {ECO:0000313|EMBL:EME26939.1, ECO:0000313|Proteomes:UP000030680};
RN [1] {ECO:0000313|Proteomes:UP000030680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=074W {ECO:0000313|Proteomes:UP000030680};
RX PubMed=23471408; DOI=10.1126/science.1231707;
RA Schonknecht G., Chen W.H., Ternes C.M., Barbier G.G., Shrestha R.P.,
RA Stanke M., Brautigam A., Baker B.J., Banfield J.F., Garavito R.M., Carr K.,
RA Wilkerson C., Rensing S.A., Gagneul D., Dickenson N.E., Oesterhelt C.,
RA Lercher M.J., Weber A.P.;
RT "Gene transfer from bacteria and archaea facilitated evolution of an
RT extremophilic eukaryote.";
RL Science 339:1207-1210(2013).
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}.
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DR EMBL; KB454540; EME26939.1; -; Genomic_DNA.
DR RefSeq; XP_005703459.1; XM_005703402.1.
DR AlphaFoldDB; M2XU59; -.
DR STRING; 130081.M2XU59; -.
DR EnsemblPlants; EME26939; EME26939; Gasu_55090.
DR GeneID; 17085884; -.
DR Gramene; EME26939; EME26939; Gasu_55090.
DR KEGG; gsl:Gasu_55090; -.
DR eggNOG; KOG0785; Eukaryota.
DR OMA; WVFFREN; -.
DR OrthoDB; 143577at2759; -.
DR Proteomes; UP000030680; 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 Oxidoreductase {ECO:0000313|EMBL:EME26939.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030680};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 40..364
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 373 AA; 40991 MW; 3071123320EFA5E6 CRC64;
MNGFVRYFKQ VKGYSKYLQN YAVDQLVSSR SLSTASQRYT VTLFPGDGIG PEISKAVQDV
FAAAELPIDW EVYHVSTKSV KPGEDLIPKE ALDAVKRNGY GLKGPLETPI GKGHKSLNLT
LRKALSLYAN VRPCVSVPGV KTKYENVNVV TVRENTEGEY SGLEHIVYPG VVEMIKLITR
QASLRVARYA FEYAKNNQRK MVTAVHKATV MKRADGLFLD CCREVAQQYP NIQYEEMLID
TCAAHLVQNP SRLDVMVMPN LYGDIISDLC AGLIGGLGLT PSGNMGEACM LAEAVHGTAP
DIAGKNAANP TALLLSSLMM VRQMKLFEKA DIIENAIYDV LKEGKVRTRD LGGTATCTDY
TLAIVDKIRK SLQ
//
