Reviewed, UniProtKB/Swiss-Prot P87257 (LEU3B_ASPNG)

Names and origin

Protein names

Recommended name:
    3-isopropylmalate dehydrogenase B
      Short name=3-IPM-DH B
      Short name=IMDH B
    EC=1.1.1.85
Alternative name(s):
    Beta-IPM dehydrogenase B

Gene names

Name:

leu2B

Organism

Aspergillus niger

Taxonomic identifier

5061 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	371 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level.

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.
Catalytic activity	(2R,3S)-3-isopropylmalate + NAD+ = 4-methyl-2-oxopentanoate + CO2 + NADH.
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.
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the isocitrate and isopropylmalate dehydrogenases family.

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: UniProtKB-KW 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: EC 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 – 371	371	3-isopropylmalate dehydrogenase B		PRO_0000083600
Regions
	Nucleotide binding	79 – 93	15	NAD By similarity
	Nucleotide binding	296 – 308	13	NAD By similarity
Sites
	Metal binding	229	1	Magnesium or manganese By similarity
	Metal binding	254	1	Magnesium or manganese By similarity
	Metal binding	258	1	Magnesium or manganese By similarity
	Binding site	100	1	Substrate By similarity
	Binding site	110	1	Substrate By similarity
	Binding site	142	1	Substrate By similarity
	Binding site	229	1	Substrate By similarity
	Site	149	1	Important for catalysis By similarity
	Site	196	1	Important for catalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	P87257-1 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: 6A0978667BA6EA65	FASTA	371	40,126
	10 20 30 40 50 60 MSGTRAYNIL VLPGDGIGPE VMAEAIKVLR TFNSSSMQFH LQEELIGGIS IDTHGHSVTQ 70 80 90 100 110 120 PVKDAAVAAD AVLFAAVGGS KVDHIRRGLD GPEGGLLQVR KAMDIYANLR PCSVDVPSRE 130 140 150 160 170 180 IARDFSPFRQ EVIEGVDFVV VRENCGGAYF GKKVEEENYA MDEWGYSTTE IQRIARLAAE 190 200 210 220 230 240 LALRHDPPWP VISLDKANVL ASSRLWRRVV ENTISVEYPQ VKLVHQLADS ASLIMATDPR 250 260 270 280 290 300 VLNGVILADN TFGDMLSDQA GSLIGTLGVL PSASLDGLPH PGKQEKVRGL YEPTHGSAPT 310 320 330 340 350 360 IAGKNIANPT AMILCVSLMF RYSFNMENEA RQIEDAVRAV LDRGLRTPDL GGNSSTQEFG 370 DAVVAALQGK Y

References

[1]	"Isolation by genetic complementation of two differentially expressed genes for beta-isopropylmalate dehydrogenase from Aspergillus niger." Williams B.A., Sillaots S., Tsang A., Storms R. Curr. Genet. 30:305-311(1996) [PubMed: 8781173] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: A733.

Cross-references

Sequence databases
EMBL GenBank DDBJ	S83229 mRNA. Translation: AAB50828.1. U51131 mRNA. Translation: AAD10279.1.
PIR	S72210.
3D structure databases
SMR	P87257. Positions 7-367.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.1.1.85. 277.
Family and domain databases
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

LEU3B_ASPNG

Accession

Primary (citable) accession number: P87257

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	July 1, 1997
Last modified:	February 9, 2010
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)