Reviewed, UniProtKB/Swiss-Prot Q9K8E9 (LEU3_BACHD)

Names and origin

Protein names

Recommended name:
    3-isopropylmalate dehydrogenase
    EC=1.1.1.85
Alternative name(s):
    Beta-IPM dehydrogenase
      Short name=IMDH
    3-IPM-DH

Gene names

Name:	leuB
Ordered Locus Names:	BH3057

Organism

Bacillus halodurans [Complete proteome] [HAMAP]

Taxonomic identifier

86665 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	363 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (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. HAMAP MF_01033
Catalytic activity	(2R,3S)-3-isopropylmalate + NAD+ = 4-methyl-2-oxopentanoate + CO2 + NADH. HAMAP MF_01033
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. HAMAP MF_01033
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 1 subfamily.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Branched-chain amino acid biosynthesis Leucine biosynthesis
Cellular component	Cytoplasm
Ligand	Magnesium Manganese Metal-binding NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	leucine biosynthetic process Inferred from electronic annotation. Source: HAMAP oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	3-isopropylmalate dehydrogenase activity Inferred from electronic annotation. Source: HAMAP NAD or NADH binding Inferred from electronic annotation. Source: InterPro magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 363	363	3-isopropylmalate dehydrogenase HAMAP MF_01033		PRO_0000083639
Regions
	Nucleotide binding	76 – 89	14	NAD By similarity
	Nucleotide binding	281 – 293	13	NAD By similarity
Sites
	Metal binding	223	1	Magnesium or manganese By similarity
	Metal binding	247	1	Magnesium or manganese By similarity
	Metal binding	251	1	Magnesium or manganese By similarity
	Binding site	96	1	Substrate By similarity
	Binding site	106	1	Substrate By similarity
	Binding site	134	1	Substrate By similarity
	Binding site	223	1	Substrate By similarity
	Site	141	1	Important for catalysis By similarity
	Site	191	1	Important for catalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9K8E9-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 5215949FEB5A30DC	FASTA	363	39,124
	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

References

[1]

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

Cross-references

Sequence databases
EMBLGenBankDDBJ	BA000004 Genomic DNA. Translation: BAB06776.1.
PIR	A84032.
RefSeq	NP_243923.1.
3D structure databases
HSSP	HSSP built from PDB template 2AYQ based on UniProtKB P12010.
ModBase	Search...
Genome annotation databases
GeneID	891019.
GenomeReviews	Gene locus BH3057 in contig BA000004_GR.
KEGG	bha:BH3057.
NMPDR	fig|272558.1.peg.3057.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q9K8E9.
OMA	Q9K8E9. EAFDTMR.
Enzyme and pathway databases
BioCyc	BHAL272558:BH3057-MON.
BRENDA	1.1.1.85. 191865.
Family and domain databases
HAMAP	MF_01033. [Tree]
InterPro	IPR019818. IsoCit/isopropylmalate_DH_CS. IPR001804. Isocitrate/isopropylmalate_DH. IPR004429. Isopropylmalate_DH. [Graphical view]
Gene3D	G3DSA:3.40.718.10. IDH_IMDH. 1 hit.
PANTHER	PTHR11835. IDH_IMDH_dimeric. 1 hit. PTHR11835:SF13. IPMDH. 1 hit.
Pfam	PF00180. Iso_dh. 1 hit. [Graphical view]
TIGRFAMs	TIGR00169. leuB. 1 hit.
PROSITE	PS00470. IDH_IMDH. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LEU3_BACHD

Accession

Primary (citable) accession number: Q9K8E9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 19, 2002
Last sequence update:	October 1, 2000
Last modified:	June 16, 2009
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)