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Database: UniProt
Entry: A0A0C1UBH6_9ACTN
LinkDB: A0A0C1UBH6_9ACTN
Original site: A0A0C1UBH6_9ACTN 
ID   A0A0C1UBH6_9ACTN        Unreviewed;       326 AA.
AC   A0A0C1UBH6;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=3-isopropylmalate dehydrogenase {ECO:0000313|EMBL:KIE49038.1};
DE            EC=1.1.1.85 {ECO:0000313|EMBL:KIE49038.1};
GN   ORFNames=MB54_05895 {ECO:0000313|EMBL:KIE49038.1};
OS   marine actinobacterium MedAcidi-G2B.
OC   Bacteria; Actinomycetota; Actinomycetes.
OX   NCBI_TaxID=1550401 {ECO:0000313|EMBL:KIE49038.1, ECO:0000313|Proteomes:UP000031352};
RN   [1] {ECO:0000313|EMBL:KIE49038.1, ECO:0000313|Proteomes:UP000031352}
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:KIE49038.1}.
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DR   EMBL; JUEO01000015; KIE49038.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C1UBH6; -.
DR   STRING; 1550401.MB54_05895; -.
DR   Proteomes; UP000031352; 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:KIE49038.1}.
FT   DOMAIN          4..321
FT                   /note="Isopropylmalate dehydrogenase-like"
FT                   /evidence="ECO:0000259|SMART:SM01329"
SQ   SEQUENCE   326 AA;  34924 MW;  647D181826E3C129 CRC64;
     MSHRIGIIGG DGIGPEVIAE GLKVISATGV KLETITYDLG GARYGRDGTV LPDEVIEEWR
     DLDALYLGAV GTPELPPGLI ERGLLLKMRF ALDLYVNLRP FTYEENNIDF SVVRENTEGS
     YAGEGGVLRQ GTANEIATQG SVNTRMGVER CIRFAFDLAA RRRGHLTLVH KTNVLTFAGD
     LWERTFNEVA DEYPEVETAY NHVDAACIYF VQSPEQYDVI VTDNLFGDIL TDLGGAISGG
     IGMAASANLN PSRTGPSMFE PVHGSAPDIA GQGVANPTAA ILSGAMMLDF LGENHAAHRI
     KEVCADPEVQ VQGTAAIGDA IAERVS
//
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