NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1007/s00203-004-0742-9; PubMed=15551059 [NCBI, ExPASy, EBI, Israel, Japan]
Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F., Reinhardt R.;
"The genome sequence of an anaerobic aromatic-degrading denitrifying bacterium, strain EbN1.";
Arch. Microbiol. 183:27-36(2005).

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

CR555306; CAI08818.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_159719.1; -.

3D structure databases

ModBase

Q5P1J6.

Enzyme and pathway databases

BioCyc

ASP76114:EBA4760-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

Q5P1J6.

Genome annotation databases

GeneID

3182723; -.

GenomeReviews

CR555306_GR; AZOSEA26930.

KEGG

eba:ebA4760; -.

NMPDR

fig|76114.4.peg.2590; -.

Phylogenomic databases

HOGENOM

Q5P1J6; -.

Genome annotation databases

CMR

Q5P1J6; AZOSEA26930.

Other

ProtoNet

Q5P1J6.

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`	`1 350`	`350`	`3-isopropylmalate dehydrogenase.`	`PRO_0000083630`
`NP_BIND`	`70 83`	`14`	`NAD (By similarity).`
`NP_BIND`	`275 287`	`13`	`NAD (By similarity).`
`METAL`	`217 217`		`Magnesium or manganese (By similarity).`
`METAL`	`241 241`		`Magnesium or manganese (By similarity).`
`METAL`	`245 245`		`Magnesium or manganese (By similarity).`
`BINDING`	`90 90`		`Substrate (By similarity).`
`BINDING`	`100 100`		`Substrate (By similarity).`
`BINDING`	`128 128`		`Substrate (By similarity).`
`BINDING`	`217 217`		`Substrate (By similarity).`
`SITE`	`135 135`	`1`	`Important for catalysis (By similarity).`
`SITE`	`185 185`	`1`	`Important for catalysis (By similarity).`

Sequence information

Length: 350 AA [This is the length of the unprocessed precursor]

Molecular weight: 37964 Da [This is the MW of the unprocessed precursor]

CRC64: 6A1DA475C7D1AF1E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKICILPGDG IGPEITAEAV RVIEALDLKF EMEEALLGGA AVDATGDPYP EATRKLAREA 

        70         80         90        100        110        120 
DAVLLGAVGG PKWDTLPREQ RPERGLLGIR KDLGLFANLR PAILYPELAN ASSLKPEVVA 

       130        140        150        160        170        180 
GLDILIVREL TGDIYFGQPR GLEVRDGERF GFNTMHYSES EIRRIGRVAF EAARKRNRRL 

       190        200        210        220        230        240 
CSVDKMNVLE TTQLWRDVMI ELAAEYPDVE LSHMLVDNAA MQLVRAPKQF DVMVTGNMFG 

       250        260        270        280        290        300 
DILSDEASML TGSIGMLPSA SLDANNKGLY EPSHGSAPDI AGQGIANPLA TILSVAMMLR 

       310        320        330        340        350 
YTFNQENGAL RIENAVKKVL AQGLRTGDIF EPGTTKVGTK QMGDAVLAAL

Q5P1J6 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