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UniProtKB/Swiss-Prot entry P30125


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

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Entry information
Entry name LEU3_ECOLI
Primary accession number P30125
Secondary accession number P78043
Integrated into Swiss-Prot on April 1, 1993
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    November 4, 2008 (Entry version 84)
Name and origin of the protein
Protein name 3-isopropylmalate dehydrogenase
Synonyms EC 1.1.1.85
Beta-IPM dehydrogenase
IMDH
3-IPM-DH
Gene name
Name: leuB
OrderedLocusNames: b0073, JW5807
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=8119295 [NCBI, ExPASy, EBI, Israel, Japan]
Kirino H., Aoki M., Aoshima M., Hayashi Y., Ohba M., Yamagishi A., Wakagi T., Oshima T.;
"Hydrophobic interaction at the subunit interface contributes to the thermostability of 3-isopropylmalate dehydrogenase from an extreme thermophile, Thermus thermophilus.";
Eur. J. Biochem. 220:275-281(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12;
DOI=10.1093/nar/20.13.3305; PubMed=1630901 [NCBI, ExPASy, EBI, Israel, Japan]
Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A.;
"Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region.";
Nucleic Acids Res. 20:3305-3308(1992).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
PROTEIN SEQUENCE OF 2-13.
STRAIN=K12 / EMG2;
DOI=10.1002/elps.1150180807; PubMed=9298646 [NCBI, ExPASy, EBI, Israel, Japan]
Link A.J., Robison K., Church G.M.;
"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.";
Electrophoresis 18:1259-1313(1997).
[6]
3D-STRUCTURE MODELING.
DOI=10.1093/protein/9.8.663; PubMed=8875643 [NCBI, ExPASy, EBI, Israel, Japan]
Magyar C., Szilagyi A., Zavodszy P.;
"Relationship between thermal stability and 3-D structure in a homology model of 3-isopropylmalate dehydrogenase from Escherichia coli.";
Protein Eng. 9:663-670(1996).
[7]
X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS), AND SUBUNIT.
DOI=10.1006/jmbi.1996.0797; PubMed=9086278 [NCBI, ExPASy, EBI, Israel, Japan]
Wallon G., Kryger G., Lovett S.T., Oshima T., Ringe D., Petsko G.A.;
"Crystal structures of Escherichia coli and Salmonella typhimurium 3-isopropylmalate dehydrogenase and comparison with their thermophilic counterpart from Thermus thermophilus.";
J. Mol. Biol. 266:1016-1031(1997).
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
D17631; BAA04537.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC73184.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAB96642.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A64729; A64729.
RefSeq AP_000737.1; -.
NP_414615.4; -.
3D structure databases
PDB
1CM7; X-ray; 2.06 A; A/B=1-363.[ExPASy / RCSB / EBI]
PDBsum 1CM7; -.
ModBase P30125.
Enzyme and pathway databases
BioCyc EcoCyc:3-ISOPROPYLMALDEHYDROG-MON; -.
MetaCyc:3-ISOPROPYLMALDEHYDROG-MON; -.
Organism-specific databases
EchoBASE EB1537; -.
EcoGene EG11577; leuB.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0003862; Molecular function: 3-isopropylmalate dehydrogenase activity (inferred from electronic annotation from HAMAP).
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 HAMAP).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
HAMAP MF_01033; -; 1.
PBIL [Tree]
InterPro IPR004429; 3-isopropylmalate_DHase.
IPR001804; IsoCit_IM_DHase.
Graphical view of domain structure.
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.
BLOCKS P30125.
ProtoNet P30125.
Genome annotation databases
GeneID 944798; -.
GenomeReviews U00096_GR; b0073.
AP009048_GR; JW5807.
KEGG ecj:JW5807; -.
eco:b0073; -.
Phylogenomic databases
HOGENOM P30125; -.
Genome annotation databases
CMR P30125; b0073.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; Complete proteome; Cytoplasm; Direct protein sequencing; Leucine biosynthesis; Magnesium; Manganese; Metal-binding; NAD; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   363  362     3-isopropylmalate dehydrogenase. PRO_0000083691
NP_BIND   78    91  14     NAD (By similarity). 
NP_BIND   285   297  13     NAD (By similarity). 
METAL   227   227        Magnesium or manganese (By similarity). 
METAL   251   251        Magnesium or manganese (By similarity). 
METAL   255   255        Magnesium or manganese (By similarity). 
BINDING   99    99        Substrate (By similarity). 
BINDING   109   109        Substrate (By similarity). 
BINDING   138   138        Substrate (By similarity). 
BINDING   227   227        Substrate (By similarity). 
SITE   145   145  1     Important for catalysis (By similarity). 
SITE   195   195  1     Important for catalysis (By similarity). 
STRAND   3    13  11      
HELIX   16    34  19      
STRAND   37    42  6      
HELIX   47    53  7      
STRAND   54    57  4      
HELIX   59    66  8      
STRAND   68    75  8      
STRAND   86    89  4      
HELIX   90   101  12      
STRAND   106   112  7      
TURN   118   120  3      
STRAND   121   123  3      
HELIX   125   128  4      
STRAND   133   139  7      
HELIX   143   145  3      
STRAND   148   153  6      
HELIX   156   158  3      
STRAND   160   168  9      
HELIX   169   184  16      
TURN   185   187  3      
STRAND   188   194  7      
TURN   196   198  3      
HELIX   200   212  13      
HELIX   213   215  3      
STRAND   219   225  7      
HELIX   226   235  10      
HELIX   237   239  3      
STRAND   241   245  5      
HELIX   247   261  15      
STRAND   268   272  5      
STRAND   278   284  7      
HELIX   288   290  3      
HELIX   299   311  13      
HELIX   316   331  16      
STRAND   336   338  3      
HELIX   348   359  12      
Sequence information
Length: 363 AA [This is the length of the unprocessed precursor] Molecular weight: 39517 Da [This is the MW of the unprocessed precursor] CRC64: 125EC1034FE1A3B5 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSKNYHIAVL PGDGIGPEVM TQALKVLDAV RNRFAMRITT SHYDVGGAAI DNHGQPLPPA 

        70         80         90        100        110        120 
TVEGCEQADA VLFGSVGGPK WEHLPPDQQP ERGALLPLRK HFKLFSNLRP AKLYQGLEAF 

       130        140        150        160        170        180 
CPLRADIAAN GFDILCVREL TGGIYFGQPK GREGSGQYEK AFDTEVYHRF EIERIARIAF 

       190        200        210        220        230        240 
ESARKRRHKV TSIDKANVLQ SSILWREIVN EIATEYPDVE LAHMYIDNAT MQLIKDPSQF 

       250        260        270        280        290        300 
DVLLCSNLFG DILSDECAMI TGSMGMLPSA SLNEQGFGLY EPAGGSAPDI AGKNIANPIA 

       310        320        330        340        350        360 
QILSLALLLR YSLDADDAAC AIERAINRAL EEGIRTGDLA RGAAAVSTDE MGDIIARYVA 


EGV 

P30125 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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