NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=DSM 319;
DOI=10.1007/s002530050155; PubMed=7764969 [NCBI, ExPASy, EBI, Israel, Japan]
Meinhardt F., Busskamp M., Wittchen K.D.;
"Cloning and sequencing of the leu C and npr M genes and a putative spo IV gene from Bacillus megaterium DSM319.";
Appl. Microbiol. Biotechnol. 41:344-351(1994).

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.
SUBCELLULAR LOCATION: Cytoplasm.
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

X65184; CAA46295.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

I40226; I40226.

3D structure databases

HSSP

P12010; 2AYQ. [HSSP ENTRY / PDB]

ModBase

P41019.

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.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; Cytoplasm; Leucine biosynthesis; Magnesium; Manganese; Metal-binding; NAD; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 367`	`367`	`3-isopropylmalate dehydrogenase.`	`PRO_0000083641`
`NP_BIND`	`74 87`	`14`	`NAD (By similarity).`
`NP_BIND`	`278 290`	`13`	`NAD (By similarity).`
`METAL`	`220 220`		`Magnesium or manganese (By similarity).`
`METAL`	`244 244`		`Magnesium or manganese (By similarity).`
`METAL`	`248 248`		`Magnesium or manganese (By similarity).`
`BINDING`	`94 94`		`Substrate (By similarity).`
`BINDING`	`104 104`		`Substrate (By similarity).`
`BINDING`	`132 132`		`Substrate (By similarity).`
`BINDING`	`220 220`		`Substrate (By similarity).`
`SITE`	`139 139`	`1`	`Important for catalysis (By similarity).`
`SITE`	`188 188`	`1`	`Important for catalysis (By similarity).`

Sequence information

Length: 367 AA [This is the length of the unprocessed precursor]

Molecular weight: 39942 Da [This is the MW of the unprocessed precursor]

CRC64: DC04D48E0EEAB0DD [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTKKVAVLPG DGGQSNQRRC CRLKAIGERL RHQFEFTYGL IGGAAIDEAG SSSSRSTIET 

        70         80         90        100        110        120 
CNEADAVLLG SVGGPKWDRF PSHLRPEKGL LAIRKELDLY ANLRPVTFYD SLADASPLKK 

       130        140        150        160        170        180 
EYIEGVDFII VRELTGGLYF GKPSDRRTEG NKETVVDTLF YKRTEIERII ASIDTAVNRR 

       190        200        210        220        230        240 
KKVTSVDKAN VLESSRVWRE VAEEVAKDYP DVELEHMLVD SAAMQLIRNP KYFDVVVTEN 

       250        260        270        280        290        300 
MFGDILSDEA SMLTGSLGML PSASLTADGP SLYEPVHGSA PDIAGQNKAN PIAAAILSAA 

       310        320        330        340        350        360 
MLLRHSFGLE KEAAVIEQAV ESVLHAGHRT ADLADGNHYL GTDKMVEVIT AVIANDSAIS 


SIMTASR

P41019 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