UniProtKB - P30125 (LEU3_ECOLI)
Protein
3-isopropylmalate dehydrogenase
Gene
leuB
Organism
Escherichia coli (strain K12)
Status
Functioni
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.UniRule annotation1 Publication
Catalytic activityi
- (2R,3S)-3-isopropylmalate + NAD+ = 4-methyl-2-oxopentanoate + CO2 + NADHUniRule annotation1 PublicationEC:1.1.1.85UniRule annotation1 Publication
Cofactori
Mg2+UniRule annotation1 Publication, Mn2+UniRule annotation1 PublicationNote: Binds 1 Mg2+ or Mn2+ ion per subunit.UniRule annotation
Activity regulationi
Requires K+ ions for optimum activity.1 Publication
Kineticsi
kcat is 69 sec(-1).1 Publication
- KM=105 µM for 3-isopropylmalate (at 40 degrees Celsius)1 Publication
- KM=321 µM for NAD (at 40 degrees Celsius)1 Publication
pH dependencei
Optimum pH is 7.6.1 Publication
Temperature dependencei
Optimum temperature is 70 degrees Celsius.1 Publication
: L-leucine biosynthesis Pathwayi
This protein is involved in step 3 of the subpathway that synthesizes L-leucine from 3-methyl-2-oxobutanoate.UniRule annotation1 PublicationProteins known to be involved in the 4 steps of the subpathway in this organism are:
- 2-isopropylmalate synthase (leuA), 2-isopropylmalate synthase (leuA)
- 3-isopropylmalate dehydratase small subunit (leuD), 3-isopropylmalate dehydratase small subunit (leuD), 3-isopropylmalate dehydratase large subunit (leuC), 3-isopropylmalate dehydratase large subunit (leuC)
- 3-isopropylmalate dehydrogenase (leuB), 3-isopropylmalate dehydrogenase (leuB)
- Branched-chain-amino-acid aminotransferase (ilvE), Branched-chain-amino-acid aminotransferase (ilvE)
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-leucine from 3-methyl-2-oxobutanoate, the pathway L-leucine biosynthesis and in Amino-acid biosynthesis.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 99 | SubstrateUniRule annotation | 1 | |
Binding sitei | 109 | SubstrateUniRule annotation | 1 | |
Binding sitei | 138 | SubstrateUniRule annotation | 1 | |
Sitei | 145 | Important for catalysisUniRule annotation | 1 | |
Sitei | 195 | Important for catalysisUniRule annotation | 1 | |
Metal bindingi | 227 | Magnesium or manganeseUniRule annotation | 1 | |
Binding sitei | 227 | SubstrateUniRule annotation | 1 | |
Metal bindingi | 251 | Magnesium or manganeseUniRule annotation | 1 | |
Metal bindingi | 255 | Magnesium or manganeseUniRule annotation | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 78 – 91 | NADUniRule annotationAdd BLAST | 14 | |
Nucleotide bindingi | 285 – 297 | NADUniRule annotationAdd BLAST | 13 |
GO - Molecular functioni
- 3-isopropylmalate dehydrogenase activity Source: EcoCyc
- magnesium ion binding Source: EcoCyc
- manganese ion binding Source: EcoCyc
- metal ion binding Source: EcoCyc
- NAD binding Source: InterPro
GO - Biological processi
- branched-chain amino acid biosynthetic process Source: UniProtKB-KW
- cellular response to amino acid starvation Source: EcoliWiki
- leucine biosynthetic process Source: EcoCyc
Keywordsi
Molecular function | Oxidoreductase |
Biological process | Amino-acid biosynthesis, Branched-chain amino acid biosynthesis, Leucine biosynthesis |
Ligand | Magnesium, Manganese, Metal-binding, NAD |
Enzyme and pathway databases
BioCyci | EcoCyc:3-ISOPROPYLMALDEHYDROG-MONOMER MetaCyc:3-ISOPROPYLMALDEHYDROG-MONOMER |
BRENDAi | 1.1.1.85, 2026 |
UniPathwayi | UPA00048;UER00072 |
Names & Taxonomyi
Protein namesi | Recommended name: 3-isopropylmalate dehydrogenase1 PublicationUniRule annotation (EC:1.1.1.85UniRule annotation1 Publication)Alternative name(s): 3-IPM-DHUniRule annotation Beta-IPM dehydrogenaseUniRule annotation Short name: IMDHUniRule annotation |
Gene namesi | Name:leuBUniRule annotation Ordered Locus Names:b0073, JW5807 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm UniRule annotation
Cytosol
- cytosol Source: EcoCyc
Keywords - Cellular componenti
CytoplasmPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed2 Publications | |||
ChainiPRO_0000083691 | 2 – 363 | 3-isopropylmalate dehydrogenaseAdd BLAST | 362 |
Proteomic databases
jPOSTi | P30125 |
PaxDbi | P30125 |
PRIDEi | P30125 |
Interactioni
Subunit structurei
Homodimer.
UniRule annotation1 PublicationProtein-protein interaction databases
BioGRIDi | 4259727, 8 interactors 849199, 2 interactors |
IntActi | P30125, 2 interactors |
STRINGi | 511145.b0073 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P30125 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P30125 |
Family & Domainsi
Sequence similaritiesi
Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 1 subfamily.UniRule annotationCurated
Phylogenomic databases
eggNOGi | COG0473, Bacteria |
HOGENOMi | CLU_031953_0_3_6 |
InParanoidi | P30125 |
PhylomeDBi | P30125 |
Family and domain databases
HAMAPi | MF_01033, LeuB_type1, 1 hit |
InterProi | View protein in InterPro IPR019818, IsoCit/isopropylmalate_DH_CS IPR024084, IsoPropMal-DH-like_dom IPR004429, Isopropylmalate_DH |
PANTHERi | PTHR42979, PTHR42979, 1 hit |
Pfami | View protein in Pfam PF00180, Iso_dh, 1 hit |
SMARTi | View protein in SMART SM01329, Iso_dh, 1 hit |
TIGRFAMsi | TIGR00169, leuB, 1 hit |
PROSITEi | View protein in PROSITE PS00470, IDH_IMDH, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P30125-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MSKNYHIAVL PGDGIGPEVM TQALKVLDAV RNRFAMRITT SHYDVGGAAI
60 70 80 90 100
DNHGQPLPPA TVEGCEQADA VLFGSVGGPK WEHLPPDQQP ERGALLPLRK
110 120 130 140 150
HFKLFSNLRP AKLYQGLEAF CPLRADIAAN GFDILCVREL TGGIYFGQPK
160 170 180 190 200
GREGSGQYEK AFDTEVYHRF EIERIARIAF ESARKRRHKV TSIDKANVLQ
210 220 230 240 250
SSILWREIVN EIATEYPDVE LAHMYIDNAT MQLIKDPSQF DVLLCSNLFG
260 270 280 290 300
DILSDECAMI TGSMGMLPSA SLNEQGFGLY EPAGGSAPDI AGKNIANPIA
310 320 330 340 350
QILSLALLLR YSLDADDAAC AIERAINRAL EEGIRTGDLA RGAAAVSTDE
360
MGDIIARYVA EGV
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 2 | S → D AA sequence (PubMed:9003442).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D17631 Genomic DNA Translation: BAA04537.1 U00096 Genomic DNA Translation: AAC73184.2 AP009048 Genomic DNA Translation: BAB96642.1 |
PIRi | A64729 |
RefSeqi | NP_414615.4, NC_000913.3 WP_000042353.1, NZ_STEB01000010.1 |
Genome annotation databases
EnsemblBacteriai | AAC73184; AAC73184; b0073 BAB96642; BAB96642; BAB96642 |
GeneIDi | 57730874 944798 |
KEGGi | ecj:JW5807 eco:b0073 |
PATRICi | fig|1411691.4.peg.2208 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D17631 Genomic DNA Translation: BAA04537.1 U00096 Genomic DNA Translation: AAC73184.2 AP009048 Genomic DNA Translation: BAB96642.1 |
PIRi | A64729 |
RefSeqi | NP_414615.4, NC_000913.3 WP_000042353.1, NZ_STEB01000010.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1CM7 | X-ray | 2.06 | A/B | 1-363 | [»] | |
SMRi | P30125 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4259727, 8 interactors 849199, 2 interactors |
IntActi | P30125, 2 interactors |
STRINGi | 511145.b0073 |
Proteomic databases
jPOSTi | P30125 |
PaxDbi | P30125 |
PRIDEi | P30125 |
Genome annotation databases
EnsemblBacteriai | AAC73184; AAC73184; b0073 BAB96642; BAB96642; BAB96642 |
GeneIDi | 57730874 944798 |
KEGGi | ecj:JW5807 eco:b0073 |
PATRICi | fig|1411691.4.peg.2208 |
Organism-specific databases
EchoBASEi | EB1537 |
Phylogenomic databases
eggNOGi | COG0473, Bacteria |
HOGENOMi | CLU_031953_0_3_6 |
InParanoidi | P30125 |
PhylomeDBi | P30125 |
Enzyme and pathway databases
UniPathwayi | UPA00048;UER00072 |
BioCyci | EcoCyc:3-ISOPROPYLMALDEHYDROG-MONOMER MetaCyc:3-ISOPROPYLMALDEHYDROG-MONOMER |
BRENDAi | 1.1.1.85, 2026 |
Miscellaneous databases
EvolutionaryTracei | P30125 |
PROi | PR:P30125 |
Family and domain databases
HAMAPi | MF_01033, LeuB_type1, 1 hit |
InterProi | View protein in InterPro IPR019818, IsoCit/isopropylmalate_DH_CS IPR024084, IsoPropMal-DH-like_dom IPR004429, Isopropylmalate_DH |
PANTHERi | PTHR42979, PTHR42979, 1 hit |
Pfami | View protein in Pfam PF00180, Iso_dh, 1 hit |
SMARTi | View protein in SMART SM01329, Iso_dh, 1 hit |
TIGRFAMsi | TIGR00169, leuB, 1 hit |
PROSITEi | View protein in PROSITE PS00470, IDH_IMDH, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | LEU3_ECOLI | |
Accessioni | P30125Primary (citable) accession number: P30125 Secondary accession number(s): P78043 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 1, 1993 |
Last sequence update: | January 23, 2007 | |
Last modified: | April 7, 2021 | |
This is version 175 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families