NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1159/000079829; PubMed=15383718 [NCBI, ExPASy, EBI, Israel, Japan]
Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.;
"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential.";
J. Mol. Microbiol. Biotechnol. 7:204-211(2004).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1186/gb-2004-5-10-r77; PubMed=15461803 [NCBI, ExPASy, EBI, Israel, Japan]
Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species.";
Genome Biol. 5:RESEARCH077.1-RESEARCH077.12(2004).

Comments

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.
CATALYTIC ACTIVITY: (2R,3S)-3-isopropylmalate + NAD⁺ = 4-methyl-2-oxopentanoate + CO₂ + NADH.
COFACTOR: Binds 1 magnesium or manganese ion per subunit (By similarity).
PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 3/4 .
SUBUNIT: Homodimer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 1 subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AE017333; AAU41825.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CP000002; AAU24463.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_080101.1; -.
YP_092518.1; -.

3D structure databases

ModBase

Q65GI9.

Enzyme and pathway databases

BioCyc

BLIC279010:BL00612-MON; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0003862;	Molecular function: 3-isopropylmalate dehydrogenase activity (inferred from electronic annotation from HAMAP).
GO:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0030145;	Molecular function: manganese ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0009098;	Biological process: leucine biosynthetic process (inferred from electronic annotation from HAMAP).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

HAMAP

MF_01033; -; 1.
PBIL [Tree]

InterPro

IPR004429; 3-isopropylmalate_DHase.
IPR001804; IsoCit_IM_DHase.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.718.10; IDH_IMDH; 1.

PANTHER

PTHR11835; IDH_IMDH_dimeric; 1.
PTHR11835:SF13; IPMDH; 1.

Pfam

PF00180; Iso_dh; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR00169; leuB; 1.

PROSITE

PS00470; IDH_IMDH; 1.

Genome annotation databases

GeneID

3028335; -.
3098436; -.

GenomeReviews

CP000002_GR; BL00612.
AE017333_GR; BLi02957.

KEGG

bld:BLi02957; -.
bli:BL00612; -.

NMPDR

fig|279010.5.peg.3307; -.

Phylogenomic databases

HOGENOM

Q65GI9; -.

Genome annotation databases

CMR

Q65GI9; BLi02957.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; Complete proteome; Cytoplasm; Leucine biosynthesis; Magnesium; Manganese; Metal-binding; NAD; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 370`	`370`	`3-isopropylmalate dehydrogenase.`	`PRO_0000083640`
`NP_BIND`	`76 89`	`14`	`NAD (By similarity).`
`NP_BIND`	`282 294`	`13`	`NAD (By similarity).`
`METAL`	`224 224`		`Magnesium or manganese (By similarity).`
`METAL`	`248 248`		`Magnesium or manganese (By similarity).`
`METAL`	`252 252`		`Magnesium or manganese (By similarity).`
`BINDING`	`96 96`		`Substrate (By similarity).`
`BINDING`	`106 106`		`Substrate (By similarity).`
`BINDING`	`134 134`		`Substrate (By similarity).`
`BINDING`	`224 224`		`Substrate (By similarity).`
`SITE`	`141 141`	`1`	`Important for catalysis (By similarity).`
`SITE`	`192 192`	`1`	`Important for catalysis (By similarity).`

Sequence information

Length: 370 AA [This is the length of the unprocessed precursor]

Molecular weight: 39850 Da [This is the MW of the unprocessed precursor]

CRC64: 9F23133E6AECED1C [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKKRIALLPG DGIGPEVLDA AVDVLKSVAE HYQHEFEFEY GLIGGAAIDE AGAPLPEETV 

        70         80         90        100        110        120 
AACKAADAIL LGAVGGPKWD QNPSELRPEK GLLAIRKQLD LFANLRPVKV FESLAGASPL 

       130        140        150        160        170        180 
KTEYIEGVDF VIVRELTGGL YFGKPSEQYV NQNGEEEAVD TLFYKKSEME RVIREAFQMA 

       190        200        210        220        230        240 
QSRKGKVTSV DKANVLESSK LWRKTAEEVA KEFPDVKLEH MLVDNAAMQL IYAPGQFDII 

       250        260        270        280        290        300 
VTENMFGDIL SDEASMLTGS LGMLPSASLS SSGLHLYEPV HGSAPDIAGQ NIANPLAAIL 

       310        320        330        340        350        360 
SAAMMLRTSF GLEAEAQAVE HAVDQVLRAG KRTKDLAKGS EHCTTQSITG EVKAALADDN 

       370 
AISNIMTAYV

Q65GI9 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools