NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-125 / C-125 / DSM 18197 / FERM 7344 / JCM 9153;
DOI=10.1093/nar/28.21.4317; PubMed=11058132 [NCBI, ExPASy, EBI, Israel, Japan]
Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
"Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis.";
Nucleic Acids Res. 28:4317-4331(2000).

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 (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

BA000004; BAB06776.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A84032; A84032.

RefSeq

NP_243923.1; -.

3D structure databases

HSSP

P12010; 2AYQ. [HSSP ENTRY / PDB]

ModBase

Q9K8E9.

Enzyme and pathway databases

BioCyc

BHAL272558:BH3057-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: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 HAMAP).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
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.

Genome annotation databases

891019; -.

BA000004_GR; BH3057.

bha:BH3057; -.

fig|272558.1.peg.3057; -.

Phylogenomic databases

HOGENOM

Q9K8E9; -.

Genome annotation databases

CMR

Q9K8E9; BH3057.

Other

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`	`1 363`	`363`	`3-isopropylmalate dehydrogenase.`	`PRO_0000083639`
`NP_BIND`	`76 89`	`14`	`NAD (By similarity).`
`NP_BIND`	`281 293`	`13`	`NAD (By similarity).`
`METAL`	`223 223`		`Magnesium or manganese (By similarity).`
`METAL`	`247 247`		`Magnesium or manganese (By similarity).`
`METAL`	`251 251`		`Magnesium or manganese (By similarity).`
`BINDING`	`96 96`		`Substrate (By similarity).`
`BINDING`	`106 106`		`Substrate (By similarity).`
`BINDING`	`134 134`		`Substrate (By similarity).`
`BINDING`	`223 223`		`Substrate (By similarity).`
`SITE`	`141 141`	`1`	`Important for catalysis (By similarity).`
`SITE`	`191 191`	`1`	`Important for catalysis (By similarity).`

Sequence information

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

Molecular weight: 39124 Da [This is the MW of the unprocessed precursor]

CRC64: 5215949FEB5A30DC [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEKQIAVLPG DGIGPEVTDA AIEVLQAVAD RFGHTFSYKK ALLGGCAIDE VGTPLPEETL 

        70         80         90        100        110        120 
DVCRHADGIL LGAVGGPKWD TLPGHLRPEK GLLGLRKGLN LFANLRPVTV YDSLADASTL 

       130        140        150        160        170        180 
KNDVIDGVDL LIVRELTGGL YFGEPRERRG EGETEEVVDT LLYTRGEMRR IIRKAFELAM 

       190        200        210        220        230        240 
VRNKHVTSVD KANVLESSRM WREVANEVAQ EFPEVTLEHM LVDNAAMQLI RRPKQFDVLV 

       250        260        270        280        290        300 
TENLFGDILS DEASMVTGSL GMLPSASLTS DGPGLYEPIH GSAPDIAGKG VANPLATIAS 

       310        320        330        340        350        360 
CAMMLKYSFG LHEEAKTIED AIEAVLKQGY RTADIAKPGE ESSSTKAITD AVVEAIQASV 


DIS

Q9K8E9 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