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Database: UniProt
Entry: L0A848_DEIPD
LinkDB: L0A848_DEIPD
Original site: L0A848_DEIPD 
ID   L0A848_DEIPD            Unreviewed;       333 AA.
AC   L0A848;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Isocitrate/isopropylmalate dehydrogenase {ECO:0000313|EMBL:AFZ69235.1};
GN   OrderedLocusNames=Deipe_3811 {ECO:0000313|EMBL:AFZ69235.1};
OS   Deinococcus peraridilitoris (strain DSM 19664 / LMG 22246 / CIP 109416 /
OS   KR-200).
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=937777 {ECO:0000313|EMBL:AFZ69235.1, ECO:0000313|Proteomes:UP000010467};
RN   [1] {ECO:0000313|Proteomes:UP000010467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19664 / LMG 22246 / CIP 109416 / KR-200
RC   {ECO:0000313|Proteomes:UP000010467};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Lu M.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Pukall R., Steenblock K., Brambilla E., Klenk H.-P.,
RA   Eisen J.A.;
RT   "Complete sequence of chromosome of Deinococcus peraridilitoris DSM
RT   19664.";
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family. {ECO:0000256|ARBA:ARBA00007769}.
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DR   EMBL; CP003382; AFZ69235.1; -; Genomic_DNA.
DR   RefSeq; WP_015237531.1; NC_019793.1.
DR   AlphaFoldDB; L0A848; -.
DR   STRING; 937777.Deipe_3811; -.
DR   KEGG; dpd:Deipe_3811; -.
DR   PATRIC; fig|937777.3.peg.3823; -.
DR   eggNOG; COG0473; Bacteria.
DR   HOGENOM; CLU_031953_0_1_0; -.
DR   OrthoDB; 56663at2; -.
DR   Proteomes; UP000010467; Chromosome.
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   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   Reference proteome {ECO:0000313|Proteomes:UP000010467}.
FT   DOMAIN          5..328
FT                   /note="Isopropylmalate dehydrogenase-like"
FT                   /evidence="ECO:0000259|SMART:SM01329"
SQ   SEQUENCE   333 AA;  35675 MW;  508D9D8438F07C1D CRC64;
     MAKHTICLIE GDGIGHEVIP AARRVLEAMG LDLEFTEAQA GYEHFLETGT SVPDRTLETV
     MAADATLFGA ATSPSHKVPG FFGAIRFMRR KLDLFANVRP ARSHPVPGSF EHVDLVLVRE
     NTEGLYVEQE RRYGDTAIAD AVITRGASQR IGEYALNLAR RRRNKLAVVH KANVLPVTQG
     LFLSTIMEEA KRNYGDVQAY DVIVDACAMH LVRHPQSFDV IVATNLFGDI LSDLTAGLTG
     GLGIAPSGNI GLEHAVFESV HGSAPDIAGQ GVSNPTATVL SAAMLLDHLG EAEAARKLET
     AVDTVLQEGP RTRDLGGSAS TAQFTDALIA RVK
//
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