NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=USDA 110;
DOI=10.1093/dnares/9.6.189; PubMed=12597275 [NCBI, ExPASy, EBI, Israel, Japan]
Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
"Complete genomic sequence of nitrogen-fixing symbiotic bacterium Bradyrhizobium japonicum USDA110.";
DNA Res. 9:189-197(2002).

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: 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

BA000040; BAC45679.1; ALT_INIT; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_767054.1; -.

3D structure databases

HSSP

Q56268; 1A05. [HSSP ENTRY / PDB]

ModBase

Q89XA0.

Enzyme and pathway databases

BioCyc

BJAP224911:BLL0414-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

Q89XA0.

Genome annotation databases

GeneID

1054690; -.

GenomeReviews

BA000040_GR; bll0414.

KEGG

bja:bll0414; -.

NMPDR

fig|224911.1.peg.414; -.

Phylogenomic databases

HOGENOM

Q89XA0; -.

Genome annotation databases

CMR

Q89XA0; bll0414.

Other

ProtoNet

Q89XA0.

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`	`1 379`	`379`	`3-isopropylmalate dehydrogenase 1.`	`PRO_0000250104`
`NP_BIND`	`293 305`	`13`	`NAD (By similarity).`
`METAL`	`230 230`		`Magnesium or manganese (By similarity).`
`METAL`	`254 254`		`Magnesium or manganese (By similarity).`
`METAL`	`258 258`		`Magnesium or manganese (By similarity).`
`BINDING`	`101 101`		`Substrate (By similarity).`
`BINDING`	`111 111`		`Substrate (By similarity).`
`BINDING`	`139 139`		`Substrate (By similarity).`
`BINDING`	`230 230`		`Substrate (By similarity).`
`SITE`	`146 146`	`1`	`Important for catalysis (By similarity).`
`SITE`	`197 197`	`1`	`Important for catalysis (By similarity).`

Sequence information

Length: 379 AA [This is the length of the unprocessed precursor]

Molecular weight: 40723 Da [This is the MW of the unprocessed precursor]

CRC64: 0B418C546FC8D01C [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNTLSNTITV AVVGGEGIGP EVTDQSHRIL KWFSDRRGAP VILREAQYGL IPYLATGKVL 

        70         80         90        100        110        120 
PDDTVEAMEE ADAILWGATG GPETTEVPPA ARKAGSLLSL RSKYDLYANL RPIVANPALA 

       130        140        150        160        170        180 
DSAPLKAAVL KDVDFIIIRE LTSGIYFGEP RGIETLPDGQ RRGFNTQQYT TSQIRRVART 

       190        200        210        220        230        240 
AFELARTRKG RVCSVDKANV LETSVLWREE VTALHEAEFS DVELTHLYVD NAAMQIVRAP 

       250        260        270        280        290        300 
SQFDVMVTCN IFGDILSDCA AMASGSLGML PSVSLGPPDR LGRRKALYEP VHGSAPDIAG 

       310        320        330        340        350        360 
KGIANPLGSI LSVAMMLRIT LHRPEDAALL EKAVDTALAA GARTADIAEP GAKRLSTQEM 

       370 
GDAVLNALDK VVGKEREHA

Q89XA0 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