NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1128/JB.01927-05; PubMed=16885469 [NCBI, ExPASy, EBI, Israel, Japan]
Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J., Parkhill J., Temple L.M.;
"Comparison of the genome sequence of the poultry pathogen Bordetella avium with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals extensive diversity in surface structures associated with host interaction.";
J. Bacteriol. 188:6002-6015(2006).

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

AM167904; CAJ49878.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_786782.1; -.

3D structure databases

ModBase

Q2KYL5.

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

Q2KYL5.

Genome annotation databases

GeneID

6266667; -.

GenomeReviews

AM167904_GR; BAV2268.

KEGG

bav:BAV2268; -.

NMPDR

fig|521.1.peg.157; -.

Phylogenomic databases

HOGENOM

Q2KYL5; -.

Genome annotation databases

CMR

Q2KYL5; BAV2268.

Other

ProtoNet

Q2KYL5.

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`	`1 358`	`358`	`3-isopropylmalate dehydrogenase.`	`PRO_0000250102`
`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`	`92 92`		`Substrate (By similarity).`
`BINDING`	`102 102`		`Substrate (By similarity).`
`BINDING`	`130 130`		`Substrate (By similarity).`
`BINDING`	`224 224`		`Substrate (By similarity).`
`SITE`	`137 137`	`1`	`Important for catalysis (By similarity).`
`SITE`	`192 192`	`1`	`Important for catalysis (By similarity).`

Sequence information

Length: 358 AA [This is the length of the unprocessed precursor]

Molecular weight: 38511 Da [This is the MW of the unprocessed precursor]

CRC64: E4572D228DAF8339 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTQKIAVLPG DGIGPEIVEQ AVRVLQALNL PLELQEAKVG GAAFDAFEHP LPPATLGLAK 

        70         80         90        100        110        120 
SSHAVLFGAV GDWKYDSLPR EFRPEQAILG LRRALGLFAN LRPAILYPEL ASASSLKPEI 

       130        140        150        160        170        180 
VAGLDIIIIR ELTGDIYFGT PRGVRSAPDG VFSGEREGYD TMRYAESEVR RIAHVGFETA 

       190        200        210        220        230        240 
RKRNKKLCSV DKANVLETSQ FWRDIVIEVA REYPDVELSH MYVDNAAMQL VRNPRQFDVI 

       250        260        270        280        290        300 
VTGNLFGDIL SDEAAMLTGS IGMLPSASLN ASGQGLYEPS HGSAPDIAGQ GIANPLATIL 

       310        320        330        340        350 
SAAMLLRYSL NQPAQADRIE AAVRKVLAQG LRTADIHEAG TTKVSTSQMG DAVLKALA

Q2KYL5 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