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3-isopropylmalate dehydrogenase (EC 1.1.1.85) (3-IPM-DH) (Beta-IPM dehydrogenase) (IMDH)

 A0A0L6JDR9_9RHIZ        Unreviewed;       369 AA.
A0A0L6JDR9;
11-NOV-2015, integrated into UniProtKB/TrEMBL.
11-NOV-2015, sequence version 1.
27-SEP-2017, entry version 14.
RecName: Full=3-isopropylmalate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01033};
EC=1.1.1.85 {ECO:0000256|HAMAP-Rule:MF_01033};
AltName: Full=3-IPM-DH {ECO:0000256|HAMAP-Rule:MF_01033};
AltName: Full=Beta-IPM dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01033};
Short=IMDH {ECO:0000256|HAMAP-Rule:MF_01033};
Name=leuB {ECO:0000256|HAMAP-Rule:MF_01033};
ORFNames=AKJ13_04840 {ECO:0000313|EMBL:KNY23810.1};
Methylobacterium sp. ARG-1.
Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
Methylobacteriaceae; Methylobacterium.
NCBI_TaxID=1692501 {ECO:0000313|EMBL:KNY23810.1, ECO:0000313|Proteomes:UP000036734};
[1] {ECO:0000313|Proteomes:UP000036734}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ARG-1 {ECO:0000313|Proteomes:UP000036734};
Hirst R., James-Pederson M., Tai A.;
"Draft Genome Sequence of Methylobacterium sp. Strain ARG-1 Isolated
from the White-Rot Fungus, Armillaria gallica.";
Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-
methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-
oxopentanoate. The product decarboxylates to 4-methyl-2
oxopentanoate. {ECO:0000256|HAMAP-Rule:MF_01033,
ECO:0000256|RuleBase:RU004445, ECO:0000256|SAAS:SAAS00571560}.
-!- CATALYTIC ACTIVITY: (2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-
2-oxopentanoate + CO(2) + NADH. {ECO:0000256|HAMAP-Rule:MF_01033,
ECO:0000256|RuleBase:RU004445, ECO:0000256|SAAS:SAAS00571562}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|RuleBase:RU004445};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000256|RuleBase:RU004445};
Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit.
{ECO:0000256|RuleBase:RU004445};
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000256|SAAS:SAAS00611795};
-!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-
leucine from 3-methyl-2-oxobutanoate: step 3/4.
{ECO:0000256|HAMAP-Rule:MF_01033, ECO:0000256|RuleBase:RU004445,
ECO:0000256|SAAS:SAAS00571573}.
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01033,
ECO:0000256|RuleBase:RU004445, ECO:0000256|SAAS:SAAS00571561}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01033,
ECO:0000256|SAAS:SAAS00571576}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:KNY23810.1}.
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EMBL; LHCD01000003; KNY23810.1; -; Genomic_DNA.
RefSeq; WP_050732335.1; NZ_LHCD01000003.1.
EnsemblBacteria; KNY23810; KNY23810; AKJ13_04840.
PATRIC; fig|1692501.3.peg.3436; -.
UniPathway; UPA00048; UER00072.
Proteomes; UP000036734; Unassembled WGS sequence.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0003862; F:3-isopropylmalate dehydrogenase activity; IEA:UniProtKB-UniRule.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0051287; F:NAD binding; IEA:InterPro.
GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniRule.
HAMAP; MF_01033; LeuB_type1; 1.
InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
InterPro; IPR024084; IsoPropMal-DH-like_dom.
InterPro; IPR004429; Isopropylmalate_DH.
Pfam; PF00180; Iso_dh; 1.
SMART; SM01329; Iso_dh; 1.
TIGRFAMs; TIGR00169; leuB; 1.
PROSITE; PS00470; IDH_IMDH; 1.
3: Inferred from homology;
Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01033,
ECO:0000256|RuleBase:RU004445, ECO:0000256|SAAS:SAAS00571574};
Branched-chain amino acid biosynthesis {ECO:0000256|HAMAP-
Rule:MF_01033, ECO:0000256|RuleBase:RU004445,
ECO:0000256|SAAS:SAAS00571574};
Complete proteome {ECO:0000313|Proteomes:UP000036734};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01033,
ECO:0000256|SAAS:SAAS00571563};
Leucine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01033,
ECO:0000256|RuleBase:RU004445, ECO:0000256|SAAS:SAAS00571574};
Magnesium {ECO:0000256|HAMAP-Rule:MF_01033,
ECO:0000256|SAAS:SAAS00571572};
Manganese {ECO:0000256|HAMAP-Rule:MF_01033,
ECO:0000256|SAAS:SAAS00571566};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_01033,
ECO:0000256|RuleBase:RU004445, ECO:0000256|SAAS:SAAS00571558};
NAD {ECO:0000256|HAMAP-Rule:MF_01033, ECO:0000256|RuleBase:RU004445,
ECO:0000256|SAAS:SAAS00571565};
Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01033,
ECO:0000256|SAAS:SAAS00571564}.
DOMAIN 5 360 Iso_dh. {ECO:0000259|SMART:SM01329}.
NP_BIND 77 90 NAD. {ECO:0000256|HAMAP-Rule:MF_01033}.
NP_BIND 289 301 NAD. {ECO:0000256|HAMAP-Rule:MF_01033}.
METAL 226 226 Magnesium or manganese.
{ECO:0000256|HAMAP-Rule:MF_01033}.
METAL 250 250 Magnesium or manganese.
{ECO:0000256|HAMAP-Rule:MF_01033}.
METAL 254 254 Magnesium or manganese.
{ECO:0000256|HAMAP-Rule:MF_01033}.
BINDING 97 97 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01033}.
BINDING 107 107 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01033}.
BINDING 135 135 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01033}.
BINDING 226 226 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01033}.
SITE 142 142 Important for catalysis.
{ECO:0000256|HAMAP-Rule:MF_01033}.
SITE 193 193 Important for catalysis.
{ECO:0000256|HAMAP-Rule:MF_01033}.
SEQUENCE 369 AA; 38738 MW; 3B56E9ABD08FB349 CRC64;
MASYKLLLLP GDGIGPEVAG GMQVVLDALK ETGLATFETE TDLVGGCALD AHGSPLSDET
LARARAADAI LLGAVGGPKW AGVAYENRPE AGLLRLRKDL ELFANLRPAI CYPALADASA
LKRELVEGLD IMIVRELTGG VYFGEPKEIT TLPDGSKRAV DTQVYTTGEI ERIAHVAFDL
AAKRSGRVAS AEKHNVMKSG VLWKEVVTKV HAEHYAQIEL EHVLADNCAM QLVRRPKQFD
VLVTDNLFGD VLSDLAAMLT GSLGMLPSAS LGAVDDSGVR RALYEPCHGS APDIAGQDKA
NPIAMIGSLT MCLRYSFGLG EAADALDGAV MDALASGART ADIAGEGTNP MGTRAMANAV
ADALRARVG


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