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., Di Bartolo G., Trong S., Kellar K., Schmutz J., Larimer F., Land M., Ivanova N., Richardson P.;
"Complete sequence of Dechloromonas aromatica RCB.";
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.
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

CP000089; AAZ48504.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_286974.1; -.

3D structure databases

ModBase

Q479H7.

Enzyme and pathway databases

BioCyc

DARO159087:DARO_3775-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

Q479H7.

Genome annotation databases

GeneID

3567508; -.

GenomeReviews

CP000089_GR; Daro_3775.

KEGG

dar:Daro_3775; -.

NMPDR

fig|159087.4.peg.3660; -.

Phylogenomic databases

HOGENOM

Q479H7; -.

Genome annotation databases

CMR

Q479H7; Daro_3775.

Other

ProtoNet

Q479H7.

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 2.`	`PRO_0000083684`
`NP_BIND`	`74 87`	`14`	`NAD (By similarity).`
`NP_BIND`	`279 291`	`13`	`NAD (By similarity).`
`METAL`	`221 221`		`Magnesium or manganese (By similarity).`
`METAL`	`245 245`		`Magnesium or manganese (By similarity).`
`METAL`	`249 249`		`Magnesium or manganese (By similarity).`
`BINDING`	`94 94`		`Substrate (By similarity).`
`BINDING`	`104 104`		`Substrate (By similarity).`
`BINDING`	`132 132`		`Substrate (By similarity).`
`BINDING`	`221 221`		`Substrate (By similarity).`
`SITE`	`139 139`	`1`	`Important for catalysis (By similarity).`
`SITE`	`189 189`	`1`	`Important for catalysis (By similarity).`

Sequence information

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

Molecular weight: 38855 Da [This is the MW of the unprocessed precursor]

CRC64: CA577A4C48616AAB [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKICVIPGDG IGVEICAEAV RVIDALKDIH GLKIEYEYGL LGGAAYDQTG RPLPVETLRL 

        70         80         90        100        110        120 
ADEANAILLG AVGGPKWDKL PAESRPERGL LGIRKYLGLN ANLRPIKVYP ELANASTLRP 

       130        140        150        160        170        180 
EVVSGLDMMI VRELTGDIYF GQPRGIRTSG FERVGYNTME YSESEIALIA EMAFRIARQR 

       190        200        210        220        230        240 
SGKVMSVDKM NVLECMQLWR DVVTKVGERF PDVTLDHMLV DNAAMQLVKN PKQFDVLLTG 

       250        260        270        280        290        300 
NMFGDILSDE AAMLTGSIGM LPSASLNVED KGMYEPCHGS APDIAGQGVA NPLGMILSAA 

       310        320        330        340        350 
MMFRYSLGRP DMADAIESAV QTVLTNGART RDIFQAGDRL VSTSEMGGLV EAALRRIS

Q479H7 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