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Database: UniProt
Entry: Q2LWI5_SYNAS
LinkDB: Q2LWI5_SYNAS
Original site: Q2LWI5_SYNAS 
ID   Q2LWI5_SYNAS            Unreviewed;       360 AA.
AC   Q2LWI5;
DT   21-FEB-2006, integrated into UniProtKB/TrEMBL.
DT   21-FEB-2006, sequence version 1.
DT   27-MAR-2024, entry version 95.
DE   SubName: Full=3-isopropylmalate dehydrogenase {ECO:0000313|EMBL:ABC78447.1};
DE            EC=1.1.1.85 {ECO:0000313|EMBL:ABC78447.1};
GN   ORFNames=SYN_00088 {ECO:0000313|EMBL:ABC78447.1};
OS   Syntrophus aciditrophicus (strain SB).
OC   Bacteria; Thermodesulfobacteriota; Syntrophia; Syntrophales; Syntrophaceae;
OC   Syntrophus.
OX   NCBI_TaxID=56780 {ECO:0000313|EMBL:ABC78447.1, ECO:0000313|Proteomes:UP000001933};
RN   [1] {ECO:0000313|EMBL:ABC78447.1, ECO:0000313|Proteomes:UP000001933}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB {ECO:0000313|EMBL:ABC78447.1,
RC   ECO:0000313|Proteomes:UP000001933};
RX   PubMed=17442750; DOI=10.1073/pnas.0610456104;
RA   McInerney M.J., Rohlin L., Mouttaki H., Kim U., Krupp R.S.,
RA   Rios-Hernandez L., Sieber J., Struchtemeyer C.G., Bhattacharyya A.,
RA   Campbell J.W., Gunsalus R.P.;
RT   "The genome of Syntrophus aciditrophicus: life at the thermodynamic limit
RT   of microbial growth.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:7600-7605(2007).
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; CP000252; ABC78447.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2LWI5; -.
DR   STRING; 56780.SYN_00088; -.
DR   KEGG; sat:SYN_00088; -.
DR   eggNOG; COG0473; Bacteria.
DR   HOGENOM; CLU_031953_0_1_7; -.
DR   InParanoid; Q2LWI5; -.
DR   Proteomes; UP000001933; 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:ABC78447.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001933}.
FT   DOMAIN          11..353
FT                   /note="Isopropylmalate dehydrogenase-like"
FT                   /evidence="ECO:0000259|SMART:SM01329"
SQ   SEQUENCE   360 AA;  39367 MW;  238CAA15EE45B961 CRC64;
     MQEDSMGTEF HVGVIPGDGT GPEVVAEGIK VLNAAASRYG FGLKYTTYDL GGERYKRTGE
     TLPDSVIREL KQHKAIFLGA IGHPEVAPGI LEKGILLRAR FELDQYINLR PVKLYEGVDT
     PLKNKGPEEI DFVVVRENTE GLYAGAGGVL KRGTADEVAI QESINTRKGV ERCIRFAFDI
     TRKRNKGKKL TLCGKTNVLT FAFDLWERTF YEVAKDYPDI ATDYAHVDAT CMWMVKNPEW
     FDVIVTDNMF GDIITDLGAM IQGGMGVAAG GNINPEGVSM FEPIGGSAPK YTGRNVINPL
     AAIMAGAMML DFLGQEEAAQ CIETSVQKAI RNDLTSMDAG KMGMGTKEVG DLISRYVLEK
//
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