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Database: UniProt
Entry: A0A0G1KFS5_9BACT
LinkDB: A0A0G1KFS5_9BACT
Original site: A0A0G1KFS5_9BACT 
ID   A0A0G1KFS5_9BACT        Unreviewed;       358 AA.
AC   A0A0G1KFS5;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   13-SEP-2023, entry version 30.
DE   SubName: Full=3-isopropylmalate dehydrogenase {ECO:0000313|EMBL:KKT55137.1};
GN   ORFNames=UW45_C0009G0009 {ECO:0000313|EMBL:KKT55137.1};
OS   Parcubacteria group bacterium GW2011_GWC2_44_22.
OC   Bacteria.
OX   NCBI_TaxID=1618930 {ECO:0000313|EMBL:KKT55137.1, ECO:0000313|Proteomes:UP000034136};
RN   [1] {ECO:0000313|EMBL:KKT55137.1, ECO:0000313|Proteomes:UP000034136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family. {ECO:0000256|RuleBase:RU004443}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKT55137.1}.
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DR   EMBL; LCII01000009; KKT55137.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1KFS5; -.
DR   PATRIC; fig|1618930.3.peg.402; -.
DR   Proteomes; UP000034136; Unassembled WGS sequence.
DR   GO; GO:0003862; F:3-isopropylmalate dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR   InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR   InterPro; IPR004429; Isopropylmalate_DH.
DR   NCBIfam; TIGR00169; leuB; 1.
DR   PANTHER; PTHR42979; 3-ISOPROPYLMALATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR42979:SF1; 3-ISOPROPYLMALATE DEHYDROGENASE; 1.
DR   Pfam; PF00180; Iso_dh; 1.
DR   SMART; SM01329; Iso_dh; 1.
DR   SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW   Leucine biosynthesis {ECO:0000256|ARBA:ARBA00022430};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU004443}.
FT   DOMAIN          11..348
FT                   /note="Isopropylmalate dehydrogenase-like"
FT                   /evidence="ECO:0000259|SMART:SM01329"
SQ   SEQUENCE   358 AA;  39374 MW;  493FEF903CB23960 CRC64;
     MKTAENQKTY QIAVIGGDGI GPEITVEAVK VLEAVAKRLS CQFIFKHLLA GGEAWDKFGK
     HLPEETVAVC QQSQAILFGA VGGPVEEATK EKWAGVERNV ILGLRSEFDL FANIRPIKGE
     GADFVIVREL TSDIYFGNVK ARHLIKFDEL SSEETVDVMY YNTSEIERIL EVAFKLAGTR
     KRQVTLVDKA NVLETSKLWR RVAERLVMKY PDIQLKYMFV DNAAYQIAKN PDQFDVLVTG
     NMFGDILSDE AAVWAKSLGM IPSGSWGGSS FGMYEPAHGS APKHTGLGTA NPLATILSAA
     MLLRHSLKLL DGAFMIEQAV EKVLQQGYGT PDLQPEKVVT TKEIGDLVVK QIIPKGIN
//
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