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Database: UniProt
Entry: A0A1C6SXC7_9ACTN
LinkDB: A0A1C6SXC7_9ACTN
Original site: A0A1C6SXC7_9ACTN 
ID   A0A1C6SXC7_9ACTN        Unreviewed;       344 AA.
AC   A0A1C6SXC7;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=3-isopropylmalate dehydrogenase {ECO:0000313|EMBL:SCL34148.1};
GN   ORFNames=GA0074692_3757 {ECO:0000313|EMBL:SCL34148.1};
OS   Micromonospora pallida.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=145854 {ECO:0000313|EMBL:SCL34148.1, ECO:0000313|Proteomes:UP000198959};
RN   [1] {ECO:0000313|EMBL:SCL34148.1, ECO:0000313|Proteomes:UP000198959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43817 {ECO:0000313|EMBL:SCL34148.1,
RC   ECO:0000313|Proteomes:UP000198959};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) 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};
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DR   EMBL; FMHW01000002; SCL34148.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C6SXC7; -.
DR   STRING; 145854.GA0074692_3757; -.
DR   OrthoDB; 5289857at2; -.
DR   Proteomes; UP000198959; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; 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}.
FT   DOMAIN          3..338
FT                   /note="Isopropylmalate dehydrogenase-like"
FT                   /evidence="ECO:0000259|SMART:SM01329"
SQ   SEQUENCE   344 AA;  36043 MW;  CEA05DAD42B36551 CRC64;
     MARIAVVAGD GIGPEVVTQA LKVVDAVLPG VVETTEYDLG AARYHRTGEV LPDSVLTELA
     GHDAILLGAV GDPSVPPGVL ERGLLLKLRF DFDQYVNLRP SRLWAGTTGP LATVKPGEVD
     LVVVREGTEG LYAGAGGALH RDTPAEVATE ESLNTRHGVE RVIRDAFARA ARRERRKVTL
     VHKTNVLTHA GSLWARAFAA VAAEHPDVTT EYQHVDAAAM FLVTQPQRYD VVVTDNLFGD
     ILTDIAAAVT GGIGLAASGS INPDGRYPSM FEPVHGSAPD IAGKGLADPV AAVLSAALLL
     EQLGHADAAV RVTEAVATEL ANRTPGEPLR TDEVGDRLAG YAAG
//
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