NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.;
"Complete sequence of Chlorobium chlorochromatii CaD3.";
Submitted (AUG-2005) 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 (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

CP000108; ABB29151.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_380194.1; -.

3D structure databases

ModBase

Q3APC4.

Enzyme and pathway databases

BioCyc

CCHL340177:CAG_1901-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

3747646; -.

GenomeReviews

CP000108_GR; Cag_1901.

KEGG

cch:Cag_1901; -.

Phylogenomic databases

HOGENOM

Q3APC4; -.

Genome annotation databases

CMR

Q3APC4; Cag_1901.

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`	`1 352`	`352`	`3-isopropylmalate dehydrogenase.`	`PRO_0000250111`
`NP_BIND`	`76 89`	`14`	`NAD (By similarity).`
`NP_BIND`	`276 288`	`13`	`NAD (By similarity).`
`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`	`96 96`		`Substrate (By similarity).`
`BINDING`	`106 106`		`Substrate (By similarity).`
`BINDING`	`134 134`		`Substrate (By similarity).`
`BINDING`	`219 219`		`Substrate (By similarity).`
`SITE`	`141 141`	`1`	`Important for catalysis (By similarity).`
`SITE`	`187 187`	`1`	`Important for catalysis (By similarity).`

Sequence information

Length: 352 AA [This is the length of the unprocessed precursor]

Molecular weight: 38185 Da [This is the MW of the unprocessed precursor]

CRC64: 4CEC7D44CA5275FB [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNYKIVSIPG DGIGTEVVAG AVAVLRQLEK KYGFTVEIEE HLFGGASYDV HGEMLTDATL 

        70         80         90        100        110        120 
EACKNCDAVL LGAVGGPKWE NLPHEHKPEA ALLKIRKELG LFANLRPAKV YDALVDASSL 

       130        140        150        160        170        180 
KADVVRGTDF VVFRELTGGI YFGQPRGYDE NKGWNTMVYE KYEVERIARL AFEAARQRQG 

       190        200        210        220        230        240 
RVMSIDKANV LEVSQLWRNV VHAVHADYQD VELSDMYVDN AAMQIVRNPK QFDVIVTGNL 

       250        260        270        280        290        300 
FGDILSDISG MITGSLGMLP SASIGSKHAL YEPIHGSAPD IAGQNKANPI ATIASVAMMF 

       310        320        330        340        350 
EHSFKRTDIA RDIEQAIEAA LATGVRTADI AAAGDTAVST TAMTEAIISQ LK

Q3APC4 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