NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=VF5;
DOI=10.1038/32831; PubMed=9537320 [NCBI, ExPASy, EBI, Israel, Japan]
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
Nature 392:353-358(1998).

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. 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

AE000657; AAC06564.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

C70322; C70322.

RefSeq

NP_213167.1; -.

3D structure databases

HSSP

P00351; 1DPZ. [HSSP ENTRY / PDB]

ModBase

O66607.

Enzyme and pathway databases

BioCyc

AAEO224324:AQ_244-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

O66607.

Genome annotation databases

1192841; -.

AE000657_GR; aq_244.

aae:aq_244; -.

fig|224324.1.peg.182; -.

Phylogenomic databases

HOGENOM

O66607; -.

Genome annotation databases

CMR

O66607; aq_244.

Other

ProtoNet

O66607.

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`	`1 364`	`364`	`3-isopropylmalate dehydrogenase.`	`PRO_0000083629`
`NP_BIND`	`77 90`	`14`	`NAD (By similarity).`
`NP_BIND`	`281 293`	`13`	`NAD (By similarity).`
`METAL`	`224 224`		`Magnesium or manganese (By similarity).`
`METAL`	`248 248`		`Magnesium or manganese (By similarity).`
`METAL`	`252 252`		`Magnesium or manganese (By similarity).`
`BINDING`	`97 97`		`Substrate (By similarity).`
`BINDING`	`107 107`		`Substrate (By similarity).`
`BINDING`	`135 135`		`Substrate (By similarity).`
`BINDING`	`224 224`		`Substrate (By similarity).`
`SITE`	`142 142`	`1`	`Important for catalysis (By similarity).`
`SITE`	`192 192`	`1`	`Important for catalysis (By similarity).`

Sequence information

Length: 364 AA [This is the length of the unprocessed precursor]

Molecular weight: 40714 Da [This is the MW of the unprocessed precursor]

CRC64: 56B528C760712FAC [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKKYKIAVLK GDGIGPEIVE QALRVLDKIG EIYGVEFEYR EGLIGGEAID KTGDPLPEET 

        70         80         90        100        110        120 
LKICKESDAI LLGAVGGPKW DNLPTDKRPE KGLLRIRKEL DLYANLRPAK VWDALISSSP 

       130        140        150        160        170        180 
LKEEVVKGTD MIVIRELTSG IYYGEPRGIF EENGKRYAIN TMKYTEDEIR RIVRKGFEIA 

       190        200        210        220        230        240 
RKRRKKLTSV DKANVLEVSA LWRQIVEEEK ENYPDVELEH LYIDNCAMQL VRRPTSFDVI 

       250        260        270        280        290        300 
VTGNIFGDIL SDEAGVVVGS LGMLPSASIG DRYALYEPVH GSAPDIAGKG IANPIATILS 

       310        320        330        340        350        360 
AAMMLKYSFN MDKAHDLIEK AIEETLNQGY RTPDIYSEGC IKVGTKEITD KILENLERLK 


DAYT

O66607 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