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Database: UniProt
Entry: A0A097IFK9_9CORY
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ID   A0A097IFK9_9CORY        Unreviewed;       339 AA.
AC   A0A097IFK9;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 41.
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=CDOO_06385 {ECO:0000313|EMBL:AIT60926.1};
OS   Corynebacterium doosanense CAU 212 = DSM 45436.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=558173 {ECO:0000313|EMBL:AIT60926.1, ECO:0000313|Proteomes:UP000029914};
RN   [1] {ECO:0000313|EMBL:AIT60926.1, ECO:0000313|Proteomes:UP000029914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CAU 212 {ECO:0000313|EMBL:AIT60926.1,
RC   ECO:0000313|Proteomes:UP000029914};
RA   Schaffert L., Albersmeier A., Kalinowski J., Ruckert C.;
RT   "Complete genome sequence of Corynebacterium doosanense CAU 212(T) (=DSM
RT   45436(T)), isolated from activated sludge.";
RL   Submitted (SEP-2013) 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}.
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DR   EMBL; CP006764; AIT60926.1; -; Genomic_DNA.
DR   RefSeq; WP_018022558.1; NZ_CP006764.1.
DR   AlphaFoldDB; A0A097IFK9; -.
DR   STRING; 558173.CDOO_06385; -.
DR   KEGG; cdo:CDOO_06385; -.
DR   eggNOG; COG0473; Bacteria.
DR   HOGENOM; CLU_031953_0_1_11; -.
DR   OrthoDB; 5289857at2; -.
DR   UniPathway; UPA00048; UER00072.
DR   Proteomes; UP000029914; Chromosome.
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:AIT60926.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029914}.
FT   DOMAIN          2..333
FT                   /note="Isopropylmalate dehydrogenase-like"
FT                   /evidence="ECO:0000259|SMART:SM01329"
FT   BINDING         88
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01035"
FT   BINDING         98
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01035"
FT   BINDING         122
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01035"
FT   BINDING         212
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01035"
FT   BINDING         212
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01035"
FT   BINDING         236
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01035"
FT   BINDING         240
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01035"
FT   BINDING         272..284
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01035"
FT   SITE            129
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01035"
FT   SITE            179
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01035"
SQ   SEQUENCE   339 AA;  35919 MW;  55E806DBF5227AE9 CRC64;
     MKLAVIGGDG IGPEVTAEAL KVLRAVRDDI DTTEFNLGAD RYLETGDILT DEDLESLKSF
     DAILLGAIGA PGRVAPGILE RELLLKLRFA LDHHVNLRPA KLYPSSTSPL ANPGEIDFVV
     VREGTEGLYA GNGGTLRKGT AHEVASEVSQ NTRYGAERVV RDAFERAMGR RKHVTLVHKT
     NVLVNAGDLW QRTVNDVAAE YPEVTVDYHH IDAATIYMVT DPARYDVIVT DNLFGDILTD
     LAGAVTGGIG LAASGNIDAT RANPSMFEPV HGSAPDIAGQ GIADPSAAIL SAALLLRHVG
     DEENAARVEA AVAADVSSRG DSPVRTTEVG DRIAAALTR
//
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