ID D6CLU1_THIA3 Unreviewed; 343 AA.
AC D6CLU1;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE SubName: Full=Isocitrate dehydrogenase [NAD] subunit 2 (Isocitric dehydrogenase) (NAD(+)-specific ICDH) {ECO:0000313|EMBL:CAZ89519.1};
DE EC=1.1.1.41 {ECO:0000313|EMBL:CAZ89519.1};
GN Name=idh2 {ECO:0000313|EMBL:CAZ89519.1};
GN OrderedLocusNames=THI_2911 {ECO:0000313|EMBL:CAZ89519.1};
OS Thiomonas arsenitoxydans (strain DSM 22701 / CIP 110005 / 3As).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Thiomonas.
OX NCBI_TaxID=426114 {ECO:0000313|EMBL:CAZ89519.1, ECO:0000313|Proteomes:UP000002372};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=3As;
RA Genoscope - CEA;
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002372}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22701 / CIP 110005 / 3As
RC {ECO:0000313|Proteomes:UP000002372};
RX PubMed=20195515; DOI=10.1371/journal.pgen.1000859;
RA Arsene-Ploetze F., Koechler S., Marchal M., Coppee J.Y., Chandler M.,
RA Bonnefoy V., Brochier-Armanet C., Barakat M., Barbe V.,
RA Battaglia-Brunet F., Bruneel O., Bryan C.G., Cleiss-Arnold J.,
RA Cruveiller S., Erhardt M., Heinrich-Salmeron A., Hommais F., Joulian C.,
RA Krin E., Lieutaud A., Lievremont D., Michel C., Muller D., Ortet P.,
RA Proux C., Siguier P., Roche D., Rouy Z., Salvignol G., Slyemi D., Talla E.,
RA Weiss S., Weissenbach J., Medigue C., Bertin P.N.;
RT "Structure, function, and evolution of the Thiomonas spp. genome.";
RL PLoS Genet. 6:E1000859-E1000859(2010).
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. {ECO:0000256|ARBA:ARBA00007769}.
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DR EMBL; FP475956; CAZ89519.1; -; Genomic_DNA.
DR RefSeq; WP_013106793.1; NZ_CTRL01000050.1.
DR AlphaFoldDB; D6CLU1; -.
DR KEGG; thi:THI_2911; -.
DR eggNOG; COG0473; Bacteria.
DR HOGENOM; CLU_031953_0_1_4; -.
DR OrthoDB; 5289857at2; -.
DR Proteomes; UP000002372; Chromosome.
DR GO; GO:0004449; F:isocitrate dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
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: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 Oxidoreductase {ECO:0000313|EMBL:CAZ89519.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002372}.
FT DOMAIN 4..336
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 343 AA; 36498 MW; 5C5AF77E6ED4B108 CRC64;
MTPSIPATLI AGDGIGPEIM EATLAALDAL GDPFDWDAQV AGLGGVKTAG DPLPAATLAS
IRTTRLALKG PLETPSGGGY RSSNVRLREA FKLYANMRPT KTLIPGGRYD NIDLLVFREN
VEGLYMGYEH YIPIDGDPHA VAIATGVNTR QGARNILDYT FRTAIALGRK KVTVVHKANI
MKALTGIFLE TAYMLHKEKY ADQIALDDVI VDACCMKLVI NPWQFDTLVT TNLFGDILSD
LAAGLVGGLG MAPGANIGED AAIFEAVHGS APDIAGKGIA NPIALMLAAA LMLDHVDLHD
KANRLRQAIS DTLNVDHIRT GDLGGRANTQ RFTDAIVSRI KNG
//