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
//