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Database: UniProt
Entry: A0A0R1VJV5_9LACO
LinkDB: A0A0R1VJV5_9LACO
Original site: A0A0R1VJV5_9LACO 
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}.
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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
//
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