ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P87257

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name LEU3B_ASPNG
Primary accession number P87257
Secondary accession numbers None
Integrated into Swiss-Prot on May 30, 2000
Sequence was last modified on July 1, 1997 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 54)
Name and origin of the protein
Protein name 3-isopropylmalate dehydrogenase B
Synonyms 3-IPM-DH B
IMDH B
EC 1.1.1.85
Beta-IPM dehydrogenase B
Gene name
Name: leu2B
From
Aspergillus niger [TaxID: 5061] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; Eurotiomycetidae; Eurotiales; Trichocomaceae; mitosporic Trichocomaceae; Aspergillus.
Protein existence 2: Evidence at transcript level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=A733;
DOI=10.1007/s002940050137; PubMed=8781173 [NCBI, ExPASy, EBI, Israel, Japan]
Williams B.A., Sillaots S., Tsang A., Storms R.;
"Isolation by genetic complementation of two differentially expressed genes for beta-isopropylmalate dehydrogenase from Aspergillus niger.";
Curr. Genet. 30:305-311(1996).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
S83229; AAB50828.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U51131; AAD10279.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S72210; S72210.
3D structure databases
HSSP P12010; 2AYQ. [HSSP ENTRY / PDB]
ModBase P87257.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from InterPro).
GO:0003862; Molecular function: 3-isopropylmalate dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0000287; Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0030145; Molecular function: manganese ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0009098; Biological process: leucine biosynthetic process (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR004429; 3-isopropylmalate_DHase.
IPR001804; IsoCit_IM_DHase.
Graphical view of domain structure.
Gene3D G3DSA:3.40.718.10; IDH_IMDH; 1.
PANTHER PTHR11835; IDH_IMDH_dimeric; 1.
PTHR11835:SF13; IPMDH; 1.
Pfam PF00180; Iso_dh; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR00169; leuB; 1.
PROSITE PS00470; IDH_IMDH; 1.
ProtoNet P87257.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; Cytoplasm; Leucine biosynthesis; Magnesium; Manganese; Metal-binding; NAD; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   371  371     3-isopropylmalate dehydrogenase B. PRO_0000083600
NP_BIND   79    93  15     NAD (By similarity). 
NP_BIND   296   308  13     NAD (By similarity). 
METAL   229   229        Magnesium or manganese (By similarity). 
METAL   254   254        Magnesium or manganese (By similarity). 
METAL   258   258        Magnesium or manganese (By similarity). 
BINDING   100   100        Substrate (By similarity). 
BINDING   110   110        Substrate (By similarity). 
BINDING   142   142        Substrate (By similarity). 
BINDING   229   229        Substrate (By similarity). 
SITE   149   149  1     Important for catalysis (By similarity). 
SITE   196   196  1     Important for catalysis (By similarity). 
Sequence information
Length: 371 AA [This is the length of the unprocessed precursor] Molecular weight: 40126 Da [This is the MW of the unprocessed precursor] CRC64: 6A0978667BA6EA65 [This is a checksum on the sequence] 
        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
P87257 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by ca flag CBR Canada Mirror sites: Australia Brazil China Korea Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!