NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=9-941 / Biovar 1;
DOI=10.1128/JB.187.8.2715-2726.2005; PubMed=15805518 [NCBI, ExPASy, EBI, Israel, Japan]
Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z., Li L.-L., Kapur V., Alt D.P., Olsen S.C.;
"Completion of the genome sequence of Brucella abortus and comparison to the highly similar genomes of Brucella melitensis and Brucella suis.";
J. Bacteriol. 187:2715-2726(2005).

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 (By similarity).
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

AE017224; AAX75773.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_223134.1; -.

3D structure databases

ModBase

Q579B1.

Enzyme and pathway databases

BioCyc

BABO262698:BRUAB2_0342-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.

ProtoNet

Q579B1.

Genome annotation databases

GeneID

3341711; -.

GenomeReviews

AE017224_GR; BruAb2_0342.

KEGG

bmb:BruAb2_0342; -.

Phylogenomic databases

HOGENOM

Q579B1; -.

Genome annotation databases

CMR

Q579B1; BruAb2_0342.

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_0000250105`
`NP_BIND`	`77 90`	`14`	`NAD (By similarity).`
`NP_BIND`	`290 302`	`13`	`NAD (By similarity).`
`METAL`	`226 226`		`Magnesium or manganese (By similarity).`
`METAL`	`250 250`		`Magnesium or manganese (By similarity).`
`METAL`	`254 254`		`Magnesium or manganese (By similarity).`
`BINDING`	`97 97`		`Substrate (By similarity).`
`BINDING`	`107 107`		`Substrate (By similarity).`
`BINDING`	`135 135`		`Substrate (By similarity).`
`BINDING`	`226 226`		`Substrate (By similarity).`
`SITE`	`142 142`	`1`	`Important for catalysis (By similarity).`
`SITE`	`193 193`	`1`	`Important for catalysis (By similarity).`

Sequence information

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

Molecular weight: 39730 Da [This is the MW of the unprocessed precursor]

CRC64: 5A389C4E26E82DFF [This is a checksum on the sequence]

        10         20         30         40         50         60 
MASRKLLLLP GDGIGPEAMA EVRKVIAFLN SDLNLGFETE EGLVGGCAYD AHGQAISDAD 

        70         80         90        100        110        120 
MEKALAADSV LFGAVGGPKW DSVPYEVRPE AGLLRLRKDM QLYANLRPAI CYPALAHSSS 

       130        140        150        160        170        180 
LKPEVIEGLD ILILRELTGG VYFGEPKEII DLGNGQKRGI DTQVYDTYEI ERIADVAFEL 

       190        200        210        220        230        240 
ARTRRNKVTS MEKRNVMKSG VLWNQGVTAR HKEKHADVQL EHMLADAGGM QLVRWPKQFD 

       250        260        270        280        290        300 
VILTDNLFGD LLSDVAAMLT GSLGMLPSAS LGAADSKTGK RKALYEPVHG SAPDIAGKGI 

       310        320        330        340        350        360 
ANPIAMIASL AMCLRYSFGL VAEADRLEAA IAGVLDDGIR TADIWSEGNT KVGTTEMGDA 

       370 
ILAKFKALSA

Q579B1 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