ID   D8GNA9_CLOLD            Unreviewed;       336 AA.
AC   D8GNA9;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=Isocitrate dehydrogenase, NAD-dependent {ECO:0000313|EMBL:ADK13733.1};
DE            EC=1.1.1.41 {ECO:0000313|EMBL:ADK13733.1};
GN   OrderedLocusNames=CLJU_c06630 {ECO:0000313|EMBL:ADK13733.1};
OS   Clostridium ljungdahlii (strain ATCC 55383 / DSM 13528 / PETC).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=748727 {ECO:0000313|EMBL:ADK13733.1, ECO:0000313|Proteomes:UP000001656};
RN   [1] {ECO:0000313|EMBL:ADK13733.1, ECO:0000313|Proteomes:UP000001656}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 55383 / DSM 13528 / PETC
RC   {ECO:0000313|Proteomes:UP000001656};
RX   PubMed=20616070; DOI=10.1073/pnas.1004716107;
RA   Kopke M., Held C., Hujer S., Liesegang H., Wiezer A., Wollherr A.,
RA   Ehrenreich A., Liebl W., Gottschalk G., Durre P.;
RT   "Clostridium ljungdahlii represents a microbial production platform based
RT   on syngas.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:13087-13092(2010).
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; CP001666; ADK13733.1; -; Genomic_DNA.
DR   RefSeq; WP_013237333.1; NZ_LITS01000021.1.
DR   AlphaFoldDB; D8GNA9; -.
DR   STRING; 748727.CLJU_c06630; -.
DR   KEGG; clj:CLJU_c06630; -.
DR   PATRIC; fig|748727.19.peg.1364; -.
DR   eggNOG; COG0473; Bacteria.
DR   HOGENOM; CLU_031953_0_1_9; -.
DR   OrthoDB; 9806254at2; -.
DR   Proteomes; UP000001656; 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:ADK13733.1}.
FT   DOMAIN          4..328
FT                   /note="Isopropylmalate dehydrogenase-like"
FT                   /evidence="ECO:0000259|SMART:SM01329"
SQ   SEQUENCE   336 AA;  36388 MW;  4548AABFA4466EA0 CRC64;
     MTHKVTLIKG DGIGPEICEA VKKVINKSGA DIDWEILEAG ASILDKYGTP IPDNIIESIK
     KNKVALKAPV TTPVGKGFKS VNVTLRKKLN LYANIRPIKT YSGVKCRYDN VDLVIFRENT
     EDLYAGIEHM INDEIAESVK IISKKASERI VEAAFQYAIK NGRKKVTAVH KANIMKLSDG
     LFLKTAEKVA EKYKGIQFES VIVDAMSMKL VLNPEDYDVL VMPNLYGDIL SDMASGLIGG
     LGLVPGANIG EDAAVFEAAH GSAPDIAGQN KANPTAIILS GVMMLNYLGE TEAANKIEIA
     IESVLREGKY LTEDLGGNAT TTVFTKAIIE KIENCN
//