Reviewed, UniProtKB/Swiss-Prot Q9AQC8 (LEU3_BUCUL)

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

Organism

Buchnera aphidicola subsp. Uroleucon rurale

Taxonomic identifier

168386 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	126 AA.
Sequence status	Fragment.
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
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 – 126	›126	3-isopropylmalate dehydrogenase HAMAP MF_01033		PRO_0000083669
Regions
	Nucleotide binding	48 – 60	13	NAD By similarity
Sites
	Metal binding	14	1	Magnesium or manganese By similarity
	Metal binding	18	1	Magnesium or manganese By similarity
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	Q9AQC8-1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 89456A26BAF250E1	FASTA	126	13,438
	10 20 30 40 50 60 NQFDILLCSN LFGDIISDEC AVITGSIGML PSASFNEKNF GLYEPAGGSA PDIAGKNIAN 70 80 90 100 110 120 PIAQILSLSM LVRYGMKLKK IADKIDKSVA SALKAGYRTA DISNNNSYLK TNEMGDVISD FLINGK

References

[1]	"Vertical transmission of biosynthetic plasmids in aphid endosymbionts (Buchnera)." Wernegreen J.J., Moran N.A. J. Bacteriol. 183:785-790(2001) [PubMed: 11133977] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF201382 Genomic DNA. Translation: AAG53464.1.
3D structure databases
HSSP	HSSP built from PDB template 1CNZ based on UniProtKB P37412.
ModBase	Search...
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]
PROSITE	PS00470. IDH_IMDH. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LEU3_BUCUL

Accession

Primary (citable) accession number: Q9AQC8

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 19, 2002
Last sequence update:	June 1, 2001
Last modified:	June 16, 2009
This is version 42 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)