Reviewed, UniProtKB/Swiss-Prot Q5P1J6 (LEU3_AZOSE)

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:	AZOSEA26930
ORF Names:	ebA4760

Organism

Azoarcus sp. (strain EbN1) (Aromatoleum aromaticum (strain EbN1)) [Complete proteome] [HAMAP]

Taxonomic identifier

76114 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Rhodocyclales › Rhodocyclaceae › Aromatoleum

Protein attributes

Sequence length	350 AA.
Sequence status	Complete.
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. HAMAP MF_01033
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. HAMAP MF_01033
Subcellular location	Cytoplasm By similarity HAMAP MF_01033.
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 – 350	350	3-isopropylmalate dehydrogenase HAMAP MF_01033		PRO_0000083630
Regions
	Nucleotide binding	70 – 83	14	NAD By similarity
	Nucleotide binding	275 – 287	13	NAD By similarity
Sites
	Metal binding	217	1	Magnesium or manganese By similarity
	Metal binding	241	1	Magnesium or manganese By similarity
	Metal binding	245	1	Magnesium or manganese By similarity
	Binding site	90	1	Substrate By similarity
	Binding site	100	1	Substrate By similarity
	Binding site	128	1	Substrate By similarity
	Binding site	217	1	Substrate By similarity
	Site	135	1	Important for catalysis By similarity
	Site	185	1	Important for catalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5P1J6-1 [UniParc]. Last modified January 4, 2005. Version 1. Checksum: 6A1DA475C7D1AF1E	FASTA	350	37,964
	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

References

[1]	"The genome sequence of an anaerobic aromatic-degrading denitrifying bacterium, strain EbN1." Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F., Reinhardt R. Arch. Microbiol. 183:27-36(2005) [PubMed: 15551059] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR555306 Genomic DNA. Translation: CAI08818.1.
RefSeq	YP_159719.1.
3D structure databases
SMR	Q5P1J6. Positions 2-350.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5P1J6.
Genome annotation databases
GeneID	3182723.
GenomeReviews	Gene locus AZOSEA26930 in contig CR555306_GR.
KEGG	eba:ebA4760.
NMPDR	fig|76114.4.peg.2590.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0473.
HOGENOM	HBG518924.
OMA	MSYQIAV.
Enzyme and pathway databases
BioCyc	ASP76114:EBA4760-MONOMER.
Family and domain databases
HAMAP	MF_01033. LeuB_type1. [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_AZOSE

Accession

Primary (citable) accession number: Q5P1J6

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 10, 2006
Last sequence update:	January 4, 2005
Last modified:	February 9, 2010
This is version 40 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)