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Database: UniProt
Entry: B1XZD8_LEPCP
LinkDB: B1XZD8_LEPCP
Original site: B1XZD8_LEPCP 
ID   B1XZD8_LEPCP            Unreviewed;       343 AA.
AC   B1XZD8;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   SubName: Full=Isocitrate dehydrogenase (NAD(+)) {ECO:0000313|EMBL:ACB36501.1};
DE            EC=1.1.1.41 {ECO:0000313|EMBL:ACB36501.1};
GN   OrderedLocusNames=Lcho_4250 {ECO:0000313|EMBL:ACB36501.1};
OS   Leptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix
OS   discophora (strain SP-6)).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Leptothrix.
OX   NCBI_TaxID=395495 {ECO:0000313|EMBL:ACB36501.1, ECO:0000313|Proteomes:UP000001693};
RN   [1] {ECO:0000313|EMBL:ACB36501.1, ECO:0000313|Proteomes:UP000001693}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51168 / LMG 8142 / SP-6
RC   {ECO:0000313|Proteomes:UP000001693};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA   Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Lykidis A., Emerson D., Richardson P.;
RT   "Complete sequence of Leptothrix cholodnii SP-6.";
RL   Submitted (MAR-2008) 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; CP001013; ACB36501.1; -; Genomic_DNA.
DR   RefSeq; WP_012349242.1; NC_010524.1.
DR   AlphaFoldDB; B1XZD8; -.
DR   STRING; 395495.Lcho_4250; -.
DR   KEGG; lch:Lcho_4250; -.
DR   eggNOG; COG0473; Bacteria.
DR   HOGENOM; CLU_031953_0_1_4; -.
DR   OrthoDB; 5289857at2; -.
DR   Proteomes; UP000001693; 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:ACB36501.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001693}.
FT   DOMAIN          4..336
FT                   /note="Isopropylmalate dehydrogenase-like"
FT                   /evidence="ECO:0000259|SMART:SM01329"
SQ   SEQUENCE   343 AA;  36659 MW;  1389365267C8A3F7 CRC64;
     MSQTIPATLI PGDGIGPEIV EATLAALDAL GAPFEWDRQI AGLEGVTTAG DPLPQATLDS
     IRRTRLALKG PLETPSGGGY RSSNVRLREE FKLYANLRPA LTIVPGGRYD KIDLVVVREN
     LEGLYIGHEH FVQIDDDPHA VAMATGINTR AGCRHILEYA FEHAIATGRK KVTIVHKANI
     MKALTGIFKE TAEQMYEAKY KDRIAMDTII VDACAMKLVL NPWQFDVLVT TNLFGDILSD
     LVAGLVGGLG MAPGANIGAD AAIFEAVHGS APDIAGQNKA NPTALLLAAA MMLDHVKLTD
     MATRLRQAID ATLNIDLVRT GDLGGSASTT VFTQALVNRI RNG
//
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