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Database: UniProt
Entry: A0A0C1U937_9ACTN
LinkDB: A0A0C1U937_9ACTN
Original site: A0A0C1U937_9ACTN 
ID   A0A0C1U937_9ACTN        Unreviewed;       332 AA.
AC   A0A0C1U937;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=3-isopropylmalate dehydrogenase {ECO:0000313|EMBL:KIE49329.1};
DE            EC=1.1.1.85 {ECO:0000313|EMBL:KIE49329.1};
GN   ORFNames=MB53_05725 {ECO:0000313|EMBL:KIE49329.1};
OS   marine actinobacterium MedAcidi-G2A.
OC   Bacteria; Actinomycetota; Actinomycetes.
OX   NCBI_TaxID=1550400 {ECO:0000313|EMBL:KIE49329.1, ECO:0000313|Proteomes:UP000031257};
RN   [1] {ECO:0000313|EMBL:KIE49329.1, ECO:0000313|Proteomes:UP000031257}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mizuno C.M., Rodriguez-Valera F., Ghai R.;
RT   "Novel reconstructed genomes of marine planktonic Acidimicrobiales.";
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentanoate
CC         + CO2 + NADH; Xref=Rhea:RHEA:32271, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:17865, ChEBI:CHEBI:35121, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.1.1.85;
CC         Evidence={ECO:0000256|ARBA:ARBA00000624};
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};
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:KIE49329.1}.
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DR   EMBL; JUEN01000029; KIE49329.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C1U937; -.
DR   STRING; 1550400.MB53_05725; -.
DR   Proteomes; UP000031257; Unassembled WGS sequence.
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   GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-KW.
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   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022430};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW   Leucine biosynthesis {ECO:0000256|ARBA:ARBA00022430};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Oxidoreductase {ECO:0000313|EMBL:KIE49329.1}.
FT   DOMAIN          4..326
FT                   /note="Isopropylmalate dehydrogenase-like"
FT                   /evidence="ECO:0000259|SMART:SM01329"
SQ   SEQUENCE   332 AA;  36128 MW;  C6BDB260CCA73773 CRC64;
     MVHKIGVIGG DGIGPEVIKE GLKVIQAAGV KLDLYEYDLG GARYLKDETI LPESILQEWK
     GLDALYLGAV GTPEVPPGVI ERGLLLKMRF ELDLYINLRP FIVAATDENL GHDFTVIREN
     TEGTYAGEGG FLRRNTPNEI ATQGSVNTRH GVERCIRFAF SLAQSRDRRH LTLVHKTNVL
     TFSGDLWERT FEEVARDFPE VQTEYNHVDA ACIYMVQDPQ RYDVIVTDNL FGDILTDLGG
     AVSGGIGLAC SANLNPERNS PSMFEPVHGS APDIVGTGQA NPTAAILSGA LMLNFLNETE
     AAQKIEQACA NPETQNGTTS QIGEAIANLV EK
//
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