[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=CBS 8195; Turakainen H., Korhola M.; "Cloning, sequencing and use as a chromosomal probe of the LEU2 gene from the sour dough yeast Candida milleri."; Submitted (MAR-2004) 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.
SIMILARITY: Belongs to the isocitrate and isopropylmalate dehydrogenases family.

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

AY571337; AAS77418.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

Q6PY58.

Family and domain databases

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`	`1 363`	`363`	`3-isopropylmalate dehydrogenase.`	`PRO_0000083605`
`NP_BIND`	`79 90`	`12`	`NAD (By similarity).`
`NP_BIND`	`289 300`	`12`	`NAD (By similarity).`
`METAL`	`225 225`		`Magnesium or manganese (By similarity).`
`METAL`	`250 250`		`Magnesium or manganese (By similarity).`
`METAL`	`254 254`		`Magnesium or manganese (By similarity).`
`BINDING`	`97 97`		`Substrate (By similarity).`
`BINDING`	`107 107`		`Substrate (By similarity).`
`BINDING`	`136 136`		`Substrate (By similarity).`
`BINDING`	`225 225`		`Substrate (By similarity).`
`SITE`	`143 143`	`1`	`Important for catalysis (By similarity).`
`SITE`	`192 192`	`1`	`Important for catalysis (By similarity).`

Sequence information

Length: 363 AA [This is the length of the unprocessed precursor]

Molecular weight: 39017 Da [This is the MW of the unprocessed precursor]

CRC64: 69C4AA375FE444DE [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSTTKTIVVL PGDHVGTEIT EEATKVLNAI AEKRPNIKFD FQHHLIGGAA IDATGVPLPD 

        70         80         90        100        110        120 
EALEASKKAD AVLLGAVGGP KWGTGDVRPE QGLLKIRKEL GLYANLRPCN FAFDSLLDMS 

       130        140        150        160        170        180 
PLKPEYARGT DFTVVRELVC GIYFGKRKED TGDGVTWDSE QYSVPEVQRI TRMAASLALQ 

       190        200        210        220        230        240 
HNPPLPIWSL DKANVLASSR LWRKTVEETI KNEFPTLSVQ HQLIDSAAMI LVKNPTKLNG 

       250        260        270        280        290        300 
LVITSNMFGD IISDEASVIP GSLGLLPSAS LASPPDTNKA FGLYEPCHGS APDLPKGKVN 

       310        320        330        340        350        360 
PVATILSVAM MLKLSLDMVE EGIAVEKAVR KVIDNGIRTA DLRGTNSTTE VGDAIAAAVK 


EFL

Q6PY58 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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