[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 10895 / NRRL Y-1056 / CBS 109.51; Mohr C., Philippsen P.; "Isolation of the Ashbya gossypii LEU2 gene and its use as a marker gene in transformation experiments."; Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 10895 / NRRL Y-1056 / CBS 109.51; Revuelta J.L.; "AgLEU2 gene."; Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 10895 / NRRL Y-1056 / CBS 109.51; DOI=10.1126/science.1095781; PubMed=15001715 [NCBI, ExPASy, EBI, Israel, Japan] Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., Gaffney T.D., Philippsen P.; "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces cerevisiae genome."; Science 304:304-307(2004).

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: (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.
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

AJ006406; CAA07006.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ001115; CAA04541.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE016814; AAS50354.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_982530.1; -.

3D structure databases

HSSP

P12010; 2AYQ. [HSSP ENTRY / PDB]

ModBase

O60027.

Enzyme and pathway databases

BioCyc

AGOS-XXX-01:AGOS-XXX-01-000175-MON; -.

Organism-specific databases

AGD

AAL012C; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from InterPro).
GO:0003862;	Molecular function: 3-isopropylmalate dehydrogenase activity (inferred from electronic annotation from InterPro).
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 InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

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.

Genome annotation databases

4618651; -.

fig|33169.1.peg.175; -.

Phylogenomic databases

HOGENOM

O60027; -.

Other

ProtoNet

O60027.

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`	`1 372`	`372`	`3-isopropylmalate dehydrogenase.`	`PRO_0000083598`
`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: 372 AA [This is the length of the unprocessed precursor]

Molecular weight: 39309 Da [This is the MW of the unprocessed precursor]

CRC64: 84C96C221B0C438D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAAVKRIVVL PGDHIGREVV EEAVKVLGAV EQSLSDVHFD FQYHLVGGAA IDATGSALPD 

        70         80         90        100        110        120 
EALGAAKEAD AVLLGAVGGP KWQGGAVRPE QGLLKLRQEL GVYANLRPCN FAADSLLELS 

       130        140        150        160        170        180 
PLRPEIARDT DIMVVRELLG GSYFGERHED EGDGVAWDTD KYTVKEVQRI ARMAGFLALQ 

       190        200        210        220        230        240 
HDPPLPVWSL DKANVLASSR LWRKTVEETF QSEFPNVQLQ HQLIDSAAMI LVKNPRAFNG 

       250        260        270        280        290        300 
VVVTSNMFGD IISDEASVIP GSLGLLPSAS LASLPDSKSA FGLYEPCHGS APDLPAGKAN 

       310        320        330        340        350        360 
PIGCILSAAM MLKLSLNMVA AGEAVEQAVQ EVLDSGVRTG DLLGSSSTSE VGDAIALAVK 

       370 
EALRRQSAAG LS

O60027 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