NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=YCH46;
PubMed=8569539 [NCBI, ExPASy, EBI, Israel, Japan]
Sarker M.R., Akimoto S., Ugai H., Kuwahara T., Ohnishi Y.;
"Nucleotide sequence of the gene encoding beta-isopropylmalate dehydrogenase (leuB) from Bacteroides fragilis.";
Microbiol. Immunol. 39:525-529(1995).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=YCH46;
DOI=10.1073/pnas.0404172101; PubMed=15466707 [NCBI, ExPASy, EBI, Israel, Japan]
Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N., Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
"Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions regulating cell surface adaptation.";
Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(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.
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

D45169; BAA08117.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP006841; BAD50187.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

I40235; I40235.

RefSeq

YP_100721.1; -.

3D structure databases

HSSP

P00351; 1DR8. [HSSP ENTRY / PDB]

ModBase

P54354.

Enzyme and pathway databases

BioCyc

BFRA295405:BF3444-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

3084526; -.

GenomeReviews

AP006841_GR; BF3444.

KEGG

bfr:BF3444; -.

Phylogenomic databases

HOGENOM

P54354; -.

Genome annotation databases

CMR

P54354; BF3444.

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`	`1 353`	`353`	`3-isopropylmalate dehydrogenase.`	`PRO_0000083644`
`METAL`	`219 219`		`Magnesium or manganese (By similarity).`
`METAL`	`243 243`		`Magnesium or manganese (By similarity).`
`METAL`	`247 247`		`Magnesium or manganese (By similarity).`
`BINDING`	`97 97`		`Substrate (By similarity).`
`BINDING`	`107 107`		`Substrate (By similarity).`
`BINDING`	`135 135`		`Substrate (By similarity).`
`BINDING`	`219 219`		`Substrate (By similarity).`
`SITE`	`142 142`	`1`	`Important for catalysis (By similarity).`
`SITE`	`187 187`	`1`	`Important for catalysis (By similarity).`

Sequence information

Length: 353 AA [This is the length of the unprocessed precursor]

Molecular weight: 39098 Da [This is the MW of the unprocessed precursor]

CRC64: 355259EA221F4A84 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDFKIAVLAG DGIGPEISVQ GVEVMSAVCE KFGHKVNYEY AICGADAIDK VGDPFPEETY 

        70         80         90        100        110        120 
RVCKNADAVL FSAVGDPKFD NDPTAKVRPE QGLLAMRKKL GLFANIRPVQ TFKCLVHKSP 

       130        140        150        160        170        180 
LRAELVEGAD FLCIRELTGG MYFGEKYQDN DKAYDTNMYT RPEIERILKV GFEYAMKRRK 

       190        200        210        220        230        240 
HLTVVDKANV LASSRLWRQI AQEMAPQYPE VTTDYMFVDN AAMKMIQEPK FFDVMVTENT 

       250        260        270        280        290        300 
FGDILTDEGS VISGSMGLLP SASTGESTPV FEPIHGSWPQ AKGLNIANPL AQILSVAMLF 

       310        320        330        340        350 
EYFDCKAEGA LIRKAVDASL DANVRTPEIQ VEGGEKFGTK EVGAWIVDYI RKA

P54354 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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