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Database: UniProt
Entry: A0A0H3J597_CLOPA
LinkDB: A0A0H3J597_CLOPA
Original site: A0A0H3J597_CLOPA 
ID   A0A0H3J597_CLOPA        Unreviewed;       357 AA.
AC   A0A0H3J597;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   RecName: Full=3-isopropylmalate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01033};
DE            EC=1.1.1.85 {ECO:0000256|HAMAP-Rule:MF_01033};
DE   AltName: Full=3-IPM-DH {ECO:0000256|HAMAP-Rule:MF_01033};
DE   AltName: Full=Beta-IPM dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01033};
DE            Short=IMDH {ECO:0000256|HAMAP-Rule:MF_01033};
GN   Name=leuB2 {ECO:0000313|EMBL:AJA52325.1};
GN   Synonyms=leuB {ECO:0000256|HAMAP-Rule:MF_01033};
GN   ORFNames=CLPA_c22670 {ECO:0000313|EMBL:AJA52325.1}, CP6013_00912
GN   {ECO:0000313|EMBL:KRU11665.1};
OS   Clostridium pasteurianum DSM 525 = ATCC 6013.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1262449 {ECO:0000313|EMBL:AJA52325.1, ECO:0000313|Proteomes:UP000030905};
RN   [1] {ECO:0000313|EMBL:AJA52325.1, ECO:0000313|Proteomes:UP000030905}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 525 {ECO:0000313|EMBL:AJA52325.1}, and DSM 525 / ATCC 6013
RC   {ECO:0000313|Proteomes:UP000030905};
RX   PubMed=25700415;
RA   Poehlein A., Grosse-Honebrink A., Zhang Y., Minton N.P., Daniel R.;
RT   "Complete Genome Sequence of the Nitrogen-Fixing and Solvent-Producing
RT   Clostridium pasteurianum DSM 525.";
RL   Genome Announc. 3:e01591-e01514(2015).
RN   [2] {ECO:0000313|EMBL:KRU11665.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 6013 {ECO:0000313|EMBL:KRU11665.1};
RA   Pyne M.E., Utturkar S.M., Brown S.D., Moo-Young M., Chung D.A., Chou P.C.;
RT   "Improved Draft Genome Sequence of Clostridium pasteurianum Strain ATCC
RT   6013 (DSM 525) Using a Hybrid Next-Generation Sequencing Approach.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:KRU11665.1, ECO:0000313|Proteomes:UP000028042}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6013 {ECO:0000313|EMBL:KRU11665.1,
RC   ECO:0000313|Proteomes:UP000028042};
RX   PubMed=25103768;
RA   Pyne M.E., Utturkar S., Brown S.D., Moo-Young M., Chung D.A., Chou C.P.;
RT   "Improved Draft Genome Sequence of Clostridium pasteurianum Strain ATCC
RT   6013 (DSM 525) Using a Hybrid Next-Generation Sequencing Approach.";
RL   Genome Announc. 2:0-0(0).
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_01033, ECO:0000256|RuleBase:RU004445}.
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_01033, ECO:0000256|RuleBase:RU004445};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01033,
CC         ECO:0000256|RuleBase:RU004445};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01033,
CC         ECO:0000256|RuleBase:RU004445};
CC       Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01033, ECO:0000256|RuleBase:RU004445};
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|ARBA:ARBA00004762,
CC       ECO:0000256|HAMAP-Rule:MF_01033, ECO:0000256|RuleBase:RU004445}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC       Rule:MF_01033, ECO:0000256|RuleBase:RU004445}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01033}.
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family. LeuB type 1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008319, ECO:0000256|HAMAP-Rule:MF_01033}.
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DR   EMBL; CP009268; AJA52325.1; -; Genomic_DNA.
DR   EMBL; JPGY02000001; KRU11665.1; -; Genomic_DNA.
DR   RefSeq; WP_003441655.1; NZ_JPGY02000001.1.
DR   AlphaFoldDB; A0A0H3J597; -.
DR   SMR; A0A0H3J597; -.
DR   GeneID; 76626666; -.
DR   KEGG; cpae:CPAST_c22670; -.
DR   KEGG; cpat:CLPA_c22670; -.
DR   PATRIC; fig|1262449.3.peg.723; -.
DR   eggNOG; COG0473; Bacteria.
DR   UniPathway; UPA00048; UER00072.
DR   Proteomes; UP000028042; Unassembled WGS sequence.
DR   Proteomes; UP000030905; 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_01033; LeuB_type1; 1.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR   InterPro; IPR004429; Isopropylmalate_DH.
DR   NCBIfam; TIGR00169; leuB; 1.
DR   PANTHER; PTHR42979; 3-ISOPROPYLMALATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR42979:SF1; 3-ISOPROPYLMALATE DEHYDROGENASE; 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|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_01033};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW   ECO:0000256|HAMAP-Rule:MF_01033};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01033};
KW   Leucine biosynthesis {ECO:0000256|ARBA:ARBA00022430, ECO:0000256|HAMAP-
KW   Rule:MF_01033};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01033};
KW   Manganese {ECO:0000256|HAMAP-Rule:MF_01033};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01033};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01033};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_01033}; Reference proteome {ECO:0000313|Proteomes:UP000030905}.
FT   DOMAIN          5..353
FT                   /note="Isopropylmalate dehydrogenase-like"
FT                   /evidence="ECO:0000259|SMART:SM01329"
FT   BINDING         77..90
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01033"
FT   BINDING         97
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01033"
FT   BINDING         107
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01033"
FT   BINDING         136
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01033"
FT   BINDING         224
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01033"
FT   BINDING         224
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01033"
FT   BINDING         248
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01033"
FT   BINDING         252
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01033"
FT   BINDING         282..294
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01033"
FT   SITE            143
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01033"
FT   SITE            192
FT                   /note="Important for catalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01033"
SQ   SEQUENCE   357 AA;  38925 MW;  39F343516E4D1C39 CRC64;
     MKEFKIAVIP GDGIGPDIVR EAVKIMTKVG EKYDTKFNFV EVKAGGDAID AYGEPLPKET
     IDVCKSSAAV LLGAVGGPKW DNLEGSKRPE RALLGLRGAL GLYANLRPAK VYNVLKSASP
     LKNEIIDEGV DLLVVRELIG GIYFGDRGTK EVNGVETAFD TEKYNVDEVK RIAHSAFKAA
     MKRRKKVTSV DKANVLDASR LWRKTVNEVS KEYPEVELSH LYVDNTAMQL VRKPSQFDVI
     LTNNIFGDIL SDEASMITGS IGMLASSSIR EDSFGMYEPI HGSAPDIAGL DIANPLAQIL
     SAAMLMEYSL DMSEAARDVE AAVEKVLNEG YRTADIYIEG TKKVGTSEMG NLVLERL
//
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