Reviewed, UniProtKB/Swiss-Prot P24404 (LEU3_AGRT5)

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:	Atu2791
ORF Names:	AGR_C_5067

Organism

Agrobacterium tumefaciens (strain C58 / ATCC 33970) [Complete proteome] [HAMAP]

Taxonomic identifier

176299 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Rhizobium/Agrobacterium group › Agrobacterium

Protein attributes

Sequence length	370 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. HAMAP MF_01033
Subcellular location	Cytoplasm. 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 – 370	370	3-isopropylmalate dehydrogenase HAMAP MF_01033		PRO_0000083627
Regions
	Nucleotide binding	77 – 90	14	NAD By similarity
	Nucleotide binding	290 – 302	13	NAD By similarity
Sites
	Metal binding	226	1	Magnesium or manganese By similarity
	Metal binding	250	1	Magnesium or manganese By similarity
	Metal binding	254	1	Magnesium or manganese By similarity
	Binding site	97	1	Substrate By similarity
	Binding site	107	1	Substrate By similarity
	Binding site	135	1	Substrate By similarity
	Binding site	226	1	Substrate By similarity
	Site	142	1	Important for catalysis By similarity
	Site	193	1	Important for catalysis By similarity
Experimental info
	Sequence conflict	6	1	L → V in AAA22089. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P24404-1 [UniParc]. Last modified March 27, 2002. Version 2. Checksum: BB4138D257849E0B	FASTA	370	39,659
	10 20 30 40 50 60 MTVRSLFLLP GDGIGPEAMT EVRKLIEYMN SAHNAGFTVS EGLVGGSAYD AHGVAISDAD 70 80 90 100 110 120 MEKALAADAI LFGAVGGPKW DGVPYEHRPE AGLLRLRKDL ELFANLRPAI CYPALAAASS 130 140 150 160 170 180 LKPELVEGLD ILIVRELTGG VYFGEPKQII DLGNGQKRGI DTQIYDTFEI ERIASVAFEL 190 200 210 220 230 240 ARSRDNRVCS MEKRNVMKSG VLWNQVVTET HAAKYKDVQL EHMLADAGGM QLVRKPKQFD 250 260 270 280 290 300 VIVTDNLFGD MLSDVAAMLT GSLGMLPSAS LGAPDAKTGK RKAMYEPVHG SAPDIAGKSI 310 320 330 340 350 360 ANPIAMIASF AMCLRYSFNM VDEATKLEAA IANVLDKGIR TADIMADGCR QVGTSDMGDA 370 VLAEFKALSA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Beta-isopropyl malate dehydrogenase gene of Agrobacterium tumefaciens C58: coding and primary structure." Strizhov N.I., Kryukov V.M., Bur'Yanov Y.I., Beav A.A. Dokl. Akad. Nauk SSSR 288:481-486(1986) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The genome of the natural genetic engineer Agrobacterium tumefaciens C58." Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K., Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y., Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P., Clendenning J. , Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R., Li M.-J., McClelland E., Palmieri A., Raymond C., Rouse G., Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y., Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S., Hendrick C., Zhao Z.-Y., Dolan M., Chumley F., Tingey S.V., Tomb J.-F., Gordon M.P., Olson M.V., Nester E.W. Science 294:2317-2323(2001) [PubMed: 11743193] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"Genome sequence of the plant pathogen and biotechnology agent Agrobacterium tumefaciens C58." Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B., Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K., Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C. , Allinger M., Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C., Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S. Science 294:2323-2328(2001) [PubMed: 11743194] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	M38670 Genomic DNA. Translation: AAA22089.1. AE007869 Genomic DNA. Translation: AAK88504.1.
PIR	AF2919. G97693.
RefSeq	NP_355719.1.
3D structure databases
HSSP	HSSP built from PDB template 1A05 based on UniProtKB Q56268.
ModBase	Search...
Genome annotation databases
GeneID	1134829.
GenomeReviews	Gene locus Atu2791 in contig AE007869_GR.
KEGG	atc:AGR_C_5067. atu:Atu2791.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P24404.
OMA	P24404. EAFDTMR.
Enzyme and pathway databases
BRENDA	1.1.1.85. 2199.
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_AGRT5

Accession

Primary (citable) accession number: P24404

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 1992
Last sequence update:	March 27, 2002
Last modified:	June 16, 2009
This is version 73 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)