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

 F4ARR8_GLAS4            Unreviewed;       366 AA.
F4ARR8;
28-JUN-2011, integrated into UniProtKB/TrEMBL.
28-JUN-2011, sequence version 1.
27-SEP-2017, entry version 48.
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};
OrderedLocusNames=Glaag_1084 {ECO:0000313|EMBL:AEE22045.1};
Glaciecola sp. (strain 4H-3-7+YE-5).
Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
Alteromonadaceae; Glaciecola.
NCBI_TaxID=983545 {ECO:0000313|EMBL:AEE22045.1, ECO:0000313|Proteomes:UP000006544};
[1] {ECO:0000313|EMBL:AEE22045.1, ECO:0000313|Proteomes:UP000006544}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=4H-3-7+YE-5 {ECO:0000313|EMBL:AEE22045.1,
ECO:0000313|Proteomes:UP000006544};
PubMed=21705587; DOI=10.1128/JB.05468-11;
US DOE Joint Genome Institute;
Klippel B., Lochner A., Bruce D.C., Davenport K.W., Detter C.,
Goodwin L.A., Han J., Han S., Land M.L., Mikhailova N., Nolan M.,
Pennacchio L., Pitluck S., Tapia R., Woyke T., Wiebusch S., Basner A.,
Abe F., Horikoshi K., Keller M., Antranikian G.;
"Complete genome sequence of the marine, cellulose and xylan degrading
bacterium Glaciecola sp. 4H-3-7+YE-5.";
J. Bacteriol. 193:4547-4548(2011).
[2]
NUCLEOTIDE SEQUENCE.
STRAIN=4H-3-7+YE-5;
US DOE Joint Genome Institute;
Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L.,
Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
Hauser L., Kyrpides N., Ivanova N., Mikhailova N., Pagani I.,
Piela B., Lochner A., Antranikian F.I., Woyke T.;
"Complete sequence of chromosome of Glaciecola sp. 4H-3-7+YE-5.";
Submitted (FEB-2011) 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}.
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EMBL; CP002526; AEE22045.1; -; Genomic_DNA.
RefSeq; WP_008305671.1; NC_015497.1.
ProteinModelPortal; F4ARR8; -.
STRING; 983545.Glaag_1084; -.
EnsemblBacteria; AEE22045; AEE22045; Glaag_1084.
KEGG; gag:Glaag_1084; -.
eggNOG; ENOG4105C0C; Bacteria.
eggNOG; COG0473; LUCA.
KO; K00052; -.
OrthoDB; POG091H01YH; -.
UniPathway; UPA00048; UER00072.
Proteomes; UP000006544; Chromosome.
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:UP000006544};
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, ECO:0000313|EMBL:AEE22045.1}.
DOMAIN 5 357 Iso_dh. {ECO:0000259|SMART:SM01329}.
NP_BIND 77 90 NAD. {ECO:0000256|HAMAP-Rule:MF_01033}.
NP_BIND 284 296 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 98 98 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01033}.
BINDING 108 108 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01033}.
BINDING 137 137 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01033}.
BINDING 226 226 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01033}.
SITE 144 144 Important for catalysis.
{ECO:0000256|HAMAP-Rule:MF_01033}.
SITE 194 194 Important for catalysis.
{ECO:0000256|HAMAP-Rule:MF_01033}.
SEQUENCE 366 AA; 39331 MW; A2E71E961825C00B CRC64;
MSNYNIAVLA GDGIGPEVMQ EAKKVLSVVE QQFNVSFTLN EFDVGGIAID NHGKALPDAT
LKGCEDAQAI LFGSIGGPKW DSLPLEERPE RAALLALRGH FDLFSNLRPA KIYPGLESLS
PLRADIAASG FDVLVVRELT SGIYFGQPKG IEGEGEEQFA YDTMRYSKKE IRRIAISAFE
AAQKRGKKVT SVDKANVLVC SRLWREVTEE VAKDYPEVTL EHIYIDNATM QLLRYPGDFD
VMLCSNLFGD IISDECAMIT GSMGLLPSAS INSENFGLYE PAGGSAPDIA GKGIANPIAQ
ILSASMLLRF SLNLTDAADA IDAAVVKTLA DGVLTGELLS PEKRDQAKST SEVGDYIANI
IASANA


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