Reviewed, UniProtKB/Swiss-Prot P05644 (LEU3_BACCA)

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

Bacillus caldotenax

Taxonomic identifier

1395 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	366 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
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 – 366	366	3-isopropylmalate dehydrogenase HAMAP MF_01033		PRO_0000083633
Regions
	Nucleotide binding	77 – 90	14	NAD By similarity
	Nucleotide binding	280 – 292	13	NAD By similarity
Sites
	Metal binding	223	1	Magnesium or manganese By similarity
	Metal binding	246	1	Magnesium or manganese By similarity
	Metal binding	250	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	223	1	Substrate By similarity
	Site	142	1	Important for catalysis By similarity
	Site	191	1	Important for catalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	P05644-1 [UniParc]. Last modified November 1, 1988. Version 1. Checksum: 530C88B3A60C630D	FASTA	366	39,636
	10 20 30 40 50 60 MGNYRIAVLP GDGIGKEVTS GAVEVLKAVG IRFGHEFTFE YGLIGGAAID EAGTPLPEET 70 80 90 100 110 120 VRLCRESDAV LLGAVGGPKW DDNPPHLRPE KGLLAIRKQL DLYANLRPVV CYDSLVSRSP 130 140 150 160 170 180 LKPDLVQGVD FVIVRELTGG IYFGQPSAVV ENGEEKAVDT LLYKKEEIER IVRMAFELAR 190 200 210 220 230 240 GRRKKVTSVD KANVLSSSRL WREVAEEVAN EFPDVTLEHM LVDMRMQLIR APKQFDVIVT 250 260 270 280 290 300 ENMFGDILSD EASMLSGSLG MLPSASLSAS GPSLYEPVHG SAPDIAGMNK ANPIAAILSA 310 320 330 340 350 360 AMMLRLSFGL TAEAGGRARV WQALALGSGS RLGQRRPHLS TNEMVEEIKA AVLDYTAIAQ IMTVYA

References

[1]	"The nucleotide sequence of 3-isopropylmalate dehydrogenase gene from Bacillus caldotenax." Sekiguchi T., Suda M., Ishii T., Nosoh Y., Tsuda K. Nucleic Acids Res. 15:853-853(1987) [PubMed: 3547331] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	X04762 Genomic DNA. Translation: CAA28455.1.
PIR	A26447.
3D structure databases
HSSP	HSSP built from PDB template 2AYQ based on UniProtKB P12010.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.1.1.85. 1001.
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_BACCA

Accession

Primary (citable) accession number: P05644

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	November 1, 1988
Last modified:	June 16, 2009
This is version 65 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)