ID A0A0R1VJV5_9LACO Unreviewed; 364 AA.
AC A0A0R1VJV5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=3-isopropylmalate dehydrogenase {ECO:0000313|EMBL:KRM06078.1};
GN ORFNames=FC89_GL000945 {ECO:0000313|EMBL:KRM06078.1};
OS Liquorilactobacillus ghanensis DSM 18630.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Liquorilactobacillus.
OX NCBI_TaxID=1423750 {ECO:0000313|EMBL:KRM06078.1, ECO:0000313|Proteomes:UP000051451};
RN [1] {ECO:0000313|EMBL:KRM06078.1, ECO:0000313|Proteomes:UP000051451}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18630 {ECO:0000313|EMBL:KRM06078.1,
RC ECO:0000313|Proteomes:UP000051451};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRM06078.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AZGB01000016; KRM06078.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R1VJV5; -.
DR STRING; 1423750.FC89_GL000945; -.
DR PATRIC; fig|1423750.3.peg.969; -.
DR OrthoDB; 9806254at2; -.
DR Proteomes; UP000051451; 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 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 4: Predicted;
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 Reference proteome {ECO:0000313|Proteomes:UP000051451}.
FT DOMAIN 6..356
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 364 AA; 39826 MW; 9A87CF25AAE6FDC6 CRC64;
MLVAFKIAAI EGDGIGPEIM AATKDVINQV AAVFNLNIEI DDVCAGGQSI DRYNTPLTEE
NFQKCKDSNA ILLANIGAPQ YDNLPIEQRP ERVMYRLRGE LGLEVNVRPI FIPSSLRSCS
PLKDEIVDEG FDVVVIRDVI GGELPSPKYR GKGSGGEEAY DKDYYNEKIV QRVANWAKKY
AKLRKNNVVS LDKANGLASS ELWRKIMVRE LTAAKVDINS ILVDSGVQTF TKGVAAFDVI
VAPNLFGDIV ADELTGLSGV GNLLPDATMG QGTFGMYEPN QLHNMNQKIV GKNIANPLGL
IMAVSMMMEQ SLELPKAAKV IRQAVMNVVN RGYVPADLKT SETKMVLGTR EVTKMVCNEI
KELS
//