ID   C9R9R2_AMMDK            Unreviewed;       353 AA.
AC   C9R9R2;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   SubName: Full=3-isopropylmalate dehydrogenase {ECO:0000313|EMBL:ACX53041.1};
DE            EC=1.1.1.85 {ECO:0000313|EMBL:ACX53041.1};
GN   OrderedLocusNames=Adeg_1962 {ECO:0000313|EMBL:ACX53041.1};
OS   Ammonifex degensii (strain DSM 10501 / KC4).
OC   Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Ammonifex.
OX   NCBI_TaxID=429009 {ECO:0000313|EMBL:ACX53041.1, ECO:0000313|Proteomes:UP000002620};
RN   [1] {ECO:0000313|EMBL:ACX53041.1, ECO:0000313|Proteomes:UP000002620}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10501 / KC4 {ECO:0000313|Proteomes:UP000002620};
RG   US DOE Joint Genome Institute;
RA   Kerfeld C., Goodner B., Huber H., Stetter K., Lucas S., Copeland A.,
RA   Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L.,
RA   Pitluck S., Saunders E., Brettin T., Detter J.C., Han C., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Ovchinnikova G., Richardson P.;
RT   "Complete sequence of chromosome of Ammonifex degensii KC4.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
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};
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DR   EMBL; CP001785; ACX53041.1; -; Genomic_DNA.
DR   RefSeq; WP_015739918.1; NC_013385.1.
DR   AlphaFoldDB; C9R9R2; -.
DR   STRING; 429009.Adeg_1962; -.
DR   KEGG; adg:Adeg_1962; -.
DR   eggNOG; COG0473; Bacteria.
DR   HOGENOM; CLU_031953_0_1_9; -.
DR   OrthoDB; 9806254at2; -.
DR   Proteomes; UP000002620; Chromosome.
DR   GO; GO:0003862; F:3-isopropylmalate dehydrogenase 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; PTHR43275; D-MALATE DEHYDROGENASE [DECARBOXYLATING]; 1.
DR   PANTHER; PTHR43275:SF1; D-MALATE DEHYDROGENASE [DECARBOXYLATING]; 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   4: Predicted;
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Oxidoreductase {ECO:0000313|EMBL:ACX53041.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002620}.
FT   DOMAIN          4..346
FT                   /note="Isopropylmalate dehydrogenase-like"
FT                   /evidence="ECO:0000259|SMART:SM01329"
SQ   SEQUENCE   353 AA;  39254 MW;  9AD62CA350B26385 CRC64;
     MTYRIAVIPG DGTGPEQVRE GLKVLEAVAQ LEGFKYETVV YDFGGERYLR TGETLPDSAI
     EELKQFHAIY LGAIGHPDVK PGILEKGILL RLRFELDQYI NLRPVKLYPG VETPLKDKGP
     EDIDFVVVRE NTEGLYCGAG GFLRRGTKDE VALQISINTY KGVERCVRYA FEYCRKRNKK
     KKVTLCGKTN VLTYAFDLWE RVFHAVGEEY PDITRDYAHV DAICMWMVKN PEWFDVIVTD
     NMFGDIITDL GAIIQGGLGI AAGANINPQG VSMFEPIGGS APKYAGKNQI NPLAAILALA
     MLLEHLGEER AAARIERAVQ EVCSKHLKSL AAGRMGYTTS EVGDLVVRYL DLK
//