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Database: UniProt
Entry: G2GCK5_9ACTN
LinkDB: G2GCK5_9ACTN
Original site: G2GCK5_9ACTN 
ID   G2GCK5_9ACTN            Unreviewed;       347 AA.
AC   G2GCK5;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 59.
DE   RecName: Full=3-isopropylmalate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01035};
DE            EC=1.1.1.85 {ECO:0000256|HAMAP-Rule:MF_01035};
DE   AltName: Full=3-IPM-DH {ECO:0000256|HAMAP-Rule:MF_01035};
DE   AltName: Full=Beta-IPM dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01035};
DE            Short=IMDH {ECO:0000256|HAMAP-Rule:MF_01035};
GN   Name=leuB {ECO:0000256|HAMAP-Rule:MF_01035};
GN   ORFNames=SZN_16205 {ECO:0000313|EMBL:EGX58749.1};
OS   Streptomyces zinciresistens K42.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=700597 {ECO:0000313|EMBL:EGX58749.1, ECO:0000313|Proteomes:UP000004217};
RN   [1] {ECO:0000313|EMBL:EGX58749.1, ECO:0000313|Proteomes:UP000004217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K42 {ECO:0000313|EMBL:EGX58749.1,
RC   ECO:0000313|Proteomes:UP000004217};
RA   Lin Y., Hao X., Johnstone L., Miller S.J., Wei G., Rensing C.;
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-
CC       methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-
CC       oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.
CC       {ECO:0000256|HAMAP-Rule:MF_01035}.
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, ECO:0000256|HAMAP-
CC         Rule:MF_01035};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01035};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01035};
CC       Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01035};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC       from 3-methyl-2-oxobutanoate: step 3/4. {ECO:0000256|HAMAP-
CC       Rule:MF_01035}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01035}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01035}.
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family. LeuB type 2 subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_01035}.
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:EGX58749.1}.
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DR   EMBL; AGBF01000046; EGX58749.1; -; Genomic_DNA.
DR   RefSeq; WP_007496187.1; NZ_AGBF01000046.1.
DR   AlphaFoldDB; G2GCK5; -.
DR   PATRIC; fig|700597.3.peg.3177; -.
DR   OrthoDB; 5289857at2; -.
DR   UniPathway; UPA00048; UER00072.
DR   Proteomes; UP000004217; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003862; F:3-isopropylmalate dehydrogenase activity; IEA:UniProtKB-UniRule.
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-UniRule.
DR   Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR   HAMAP; MF_01035; LeuB_type2; 1.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR   InterPro; IPR023698; LeuB_actb.
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   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01035};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW   ECO:0000256|HAMAP-Rule:MF_01035};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01035};
KW   Leucine biosynthesis {ECO:0000256|ARBA:ARBA00022430, ECO:0000256|HAMAP-
KW   Rule:MF_01035}; Magnesium {ECO:0000256|HAMAP-Rule:MF_01035};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01035};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01035};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01035};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01035,
KW   ECO:0000313|EMBL:EGX58749.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004217}.
FT   DOMAIN          6..341
FT                   /note="Isopropylmalate dehydrogenase-like"
FT                   /evidence="ECO:0000259|SMART:SM01329"
FT   BINDING         94
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01035"
FT   BINDING         104
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01035"
FT   BINDING         128
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01035"
FT   BINDING         219
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01035"
FT   BINDING         219
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01035"
FT   BINDING         243
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01035"
FT   BINDING         247
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01035"
FT   BINDING         279..291
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01035"
FT   SITE            135
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01035"
FT   SITE            186
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01035"
SQ   SEQUENCE   347 AA;  37060 MW;  44E83079C1043E73 CRC64;
     MSRSIDLAVI PGDGIGQEVV AEGLKVLSAA LPQDVKLETR EYDFGARRYH ATGETLTDAD
     LDSLKRHDAI LLGAIGDPGV PSGVLERGFL LKLRFAFDHH VNLRPSKLLP GVATPLAGQP
     EIDFVVVREG TEGPYTGNGG TIRKGTQHEV ATEVSVNTAF GVERVVRDAF ARAQARPRRK
     LALIHKNNVL TFAGHLWTDV FNRVAEEFPE VTTEYMHVDA ATIYLVTQPE RFDVIVTDNL
     FGDIITDLAA AVSGGIGVAA SGNINPDRVF PSMFEPVHGS APDIAGQGKA DPTATVLSVA
     LLLRHLGHDT EADRIEDAVS ADLAERAGRP ARSTSEIGDA LAVRVAG
//
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