[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y., Kawai S., Ito S., Horikoshi K.; "The complete genome sequence of the alkaliphilic Bacillus clausii KSM-K16."; Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.

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: 3-carboxy-2-hydroxy-4-methylpentanoate + NAD⁺ = 3-carboxy-4-methyl-2-oxopentanoate + 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

AP006627; BAD65176.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_176137.1; -.

3D structure databases

ModBase

Q5WEN4.

Enzyme and pathway databases

BioCyc

BCLA66692:ABC2641-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:0009098;	Biological process: leucine biosynthetic process (inferred from electronic annotation from HAMAP).
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.

BLOCKS

Q5WEN4.

Genome annotation databases

GeneID

3204057; -.

GenomeReviews

AP006627_GR; ABC2641.

KEGG

bcl:ABC2641; -.

NMPDR

fig|66692.3.peg.2938; -.

Phylogenomic databases

HOGENOM

Q5WEN4; -.

Genome annotation databases

CMR

Q5WEN4; ABC2641.

Other

ProtoNet

Q5WEN4.

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`	`1 364`	`364`	`3-isopropylmalate dehydrogenase.`	`PRO_0000083637`
`NP_BIND`	`76 89`	`14`	`NAD (By similarity).`
`NP_BIND`	`281 293`	`13`	`NAD (By similarity).`
`METAL`	`223 223`		`Magnesium or manganese (By similarity).`
`METAL`	`247 247`		`Magnesium or manganese (By similarity).`
`METAL`	`251 251`		`Magnesium or manganese (By similarity).`
`BINDING`	`96 96`		`Substrate (By similarity).`
`BINDING`	`106 106`		`Substrate (By similarity).`
`BINDING`	`134 134`		`Substrate (By similarity).`
`BINDING`	`223 223`		`Substrate (By similarity).`
`SITE`	`141 141`	`1`	`Important for catalysis (By similarity).`
`SITE`	`191 191`	`1`	`Important for catalysis (By similarity).`

Sequence information

Length: 364 AA [This is the length of the unprocessed precursor]

Molecular weight: 39332 Da [This is the MW of the unprocessed precursor]

CRC64: 232EC25567427128 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEKQILLLPG DGIGPEIIAE TKRVLEEIAR LYHHTFQFVE GRIGGDAIDA TGSPLPEETL 

        70         80         90        100        110        120 
DLAKGSDAIL LGAVGGPKWD GNAPEKRPEK GLLQIRKALG LYANLRPVRV LKPLMGASTL 

       130        140        150        160        170        180 
KEEVLADVDL LIVRELTGGL YFGEPRERRQ INGEDGAVDT LLYTRGEIER IVHQAFQFAR 

       190        200        210        220        230        240 
TRKKRVVSVD KANVLESSRL WREIADEVAR EYPDVTLSHM LVDNAAMQLI RDPRQFDVIV 

       250        260        270        280        290        300 
TENLFGDILS DEASMITGSL GLLPSASMNT SKVGLFEPVH GSAPDIAGTG AANPLATILS 

       310        320        330        340        350        360 
AAMMLQYSFG LADEAKAIEV AVDRVLAQGV RTKDIAKASE NAVSTTAITN AVMEALALKS 


ASSR

Q5WEN4 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