3-isopropylmalate dehydrogenase - Buchnera aphidicola subsp. Acyrthosiphon pisum

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Reviewed, UniProtKB/Swiss-Prot P56933 (LEU3_BUCAI)

Last modified June 16, 2009. Version 62. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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:	BUpL05

Encoded on

Plasmid pLeu (pBAp1)

Organism

Buchnera aphidicola subsp. Acyrthosiphon pisum (Acyrthosiphon pisum symbiotic bacterium) [Complete proteome] [HAMAP]

Taxonomic identifier

118099 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

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Protein attributes

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

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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. HAMAP MF_01033
Sequence similarities	Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 1 subfamily.

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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 Plasmid
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...

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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_0000083655

Regions

Nucleotide binding

78 – 91

NAD By similarity

Nucleotide binding

285 – 297

NAD By similarity

Sites

Metal binding

227

Magnesium or manganese By similarity

Metal binding

251

Magnesium or manganese By similarity

Metal binding

255

Magnesium or manganese By similarity

Binding site

Substrate By similarity

Binding site

109

Substrate By similarity

Binding site

138

Substrate By similarity

Binding site

227

Substrate By similarity

Site

145

Important for catalysis By similarity

Site

195

Important for catalysis By similarity

Experimental info

Sequence conflict

101

H → Y in CAB56191. Ref.1

Sequence conflict

186

R → K in CAB56191. Ref.1

Sequence conflict

200

Q → R in CAB56191. Ref.1

Sequence conflict

206 – 207

RE → GK in CAB56191. Ref.1

Sequence conflict

363

E → K Ref.1

Sequence conflict

363

E → K Ref.2

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Sequences

Sequence

Length

Mass (Da)

Tools

P56933-1 [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: AB7D6DCF8FFD8D70
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FASTA

363

40,479

        10         20         30         40         50         60 
MKKNYRIAVL SGDGIGPEVM QEACKILNVL KKYFFLSLEI QKFNIGGIAI EREGVALPKT 

        70         80         90        100        110        120 
TLLGCENSDS ILLGSVGGKK WDNLPVEQRP ERAALLPLRK HFNLFSNLRP AKLYPELKCL 

       130        140        150        160        170        180 
SPLRSDIVKN GFDILCVREL TGGIYFGEPK GFVNKNNTKY AFDTEIYHEY EIIRIAHLAF 

       190        200        210        220        230        240 
KLARSRKKKV CSIDKSNVLQ SSILWREVVE SVSKKYPDVH LSHLYIDNAA MQIIKDPNQF 

       250        260        270        280        290        300 
DVLLCSNLFG DIISDECATI TGSIGMLPSA SFNEKNFGLY EPAGGSAPDI EGKNIANPIA 

       310        320        330        340        350        360 
QILSLSMLVR YGMNLNQIAD KIDKAVNNVL KKGYRTSDIS HDNNFLKTDE MGDLIVDSLI 


NGE

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular characterization of the Leucine plasmid from Buchnera aphidicola, primary endosymbiont of the aphid Acyrthosiphon pisum." Soler T., Latorre A., Sabater B., Silva F.J. Curr. Microbiol. 40:264-268(2000) [PubMed: 10688696] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"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].
[3]	"Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS." Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H. Nature 407:81-86(2000) [PubMed: 10993077] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Tokyo 1998.

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Cross-references

Sequence databases
	AJ006878 Genomic DNA. Translation: CAB56191.1. AF197457 Genomic DNA. Translation: AAG31405.1. AP001071 Genomic DNA. Translation: BAA95424.1.
RefSeq	NP_057969.1.
3D structure databases
HSSP	HSSP built from PDB template 1CNZ based on UniProtKB P37412.
ModBase	Search...
Genome annotation databases
GeneID	1109450.
GenomeReviews	Gene locus BUpL05 in contig AP001071_GR.
KEGG	buc:BUpL05.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P56933.
OMA	P56933. EAFDTMR.
Enzyme and pathway databases
BioCyc	BSP107806:BUPL05-MON.
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...

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Entry information

Entry name

LEU3_BUCAI

Accession

Primary (citable) accession number: P56933
Secondary accession number(s): Q9EVG0, Q9KGP9, Q9R6R4

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	December 1, 2000
Last modified:	June 16, 2009
This is version 62 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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

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Relevant documents

Buchnera aphidicola (subsp. Acyrthosiphon pisum)

Buchnera aphidicola (subsp. Acyrthosiphon pisum): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents