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Protein

3-isopropylmalate dehydrogenase

Gene

leuB

Organism
Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 / E264)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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 annotation

Catalytic activityi

(2R,3S)-3-isopropylmalate + NAD+ = 4-methyl-2-oxopentanoate + CO2 + NADH.UniRule annotation

Cofactori

Mg2+UniRule annotation, Mn2+UniRule annotationNote: Binds 1 Mg2+ or Mn2+ ion per subunit.UniRule annotation

Pathwayi: L-leucine biosynthesis

This protein is involved in step 3 of the subpathway that synthesizes L-leucine from 3-methyl-2-oxobutanoate.UniRule annotation
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. 2-isopropylmalate synthase (leuA-1), 2-isopropylmalate synthase (leuA-2)
  2. 3-isopropylmalate dehydratase small subunit (leuD), 3-isopropylmalate dehydratase large subunit (leuC), 3-isopropylmalate dehydratase small subunit (leuD), 3-isopropylmalate dehydratase large subunit (leuC)
  3. 3-isopropylmalate dehydrogenase (leuB), 3-isopropylmalate dehydrogenase (leuB)
  4. no protein annotated in this organism
This subpathway is part of the pathway L-leucine biosynthesis, which is itself part of Amino-acid biosynthesis.
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 keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei90SubstrateUniRule annotation1
Binding sitei100SubstrateUniRule annotation1
Binding sitei128SubstrateUniRule annotation1
Sitei135Important for catalysisUniRule annotation1
Sitei190Important for catalysisUniRule annotation1
Metal bindingi222Magnesium or manganeseUniRule annotation1
Binding sitei222SubstrateUniRule annotation1
Metal bindingi246Magnesium or manganeseUniRule annotation1
Metal bindingi250Magnesium or manganeseUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi280 – 292NADUniRule annotationAdd BLAST13

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Amino-acid biosynthesis, Branched-chain amino acid biosynthesis, Leucine biosynthesis

Keywords - Ligandi

Magnesium, Manganese, Metal-binding, NAD

Enzyme and pathway databases

UniPathwayiUPA00048; UER00072.

Names & Taxonomyi

Protein namesi
Recommended name:
3-isopropylmalate dehydrogenaseUniRule annotation (EC:1.1.1.85UniRule annotation)
Alternative name(s):
3-IPM-DHUniRule annotation
Beta-IPM dehydrogenaseUniRule annotation
Short name:
IMDHUniRule annotation
Gene namesi
Name:leuBUniRule annotation
Ordered Locus Names:BTH_II0674
OrganismiBurkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 / E264)
Taxonomic identifieri271848 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group
Proteomesi
  • UP000001930 Componenti: Chromosome II

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002501091 – 3553-isopropylmalate dehydrogenaseAdd BLAST355

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

Secondary structure

1355
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 9Combined sources8
Helixi11 – 25Combined sources15
Beta strandi26 – 28Combined sources3
Beta strandi31 – 34Combined sources4
Helixi39 – 45Combined sources7
Beta strandi46 – 49Combined sources4
Helixi51 – 59Combined sources9
Beta strandi60 – 67Combined sources8
Helixi71 – 73Combined sources3
Helixi78 – 80Combined sources3
Helixi84 – 92Combined sources9
Beta strandi97 – 103Combined sources7
Helixi106 – 111Combined sources6
Beta strandi112 – 114Combined sources3
Helixi116 – 119Combined sources4
Beta strandi123 – 129Combined sources7
Turni134 – 136Combined sources3
Beta strandi141 – 144Combined sources4
Turni149 – 152Combined sources4
Beta strandi153 – 163Combined sources11
Helixi164 – 179Combined sources16
Turni180 – 182Combined sources3
Beta strandi183 – 189Combined sources7
Turni191 – 193Combined sources3
Helixi195 – 208Combined sources14
Beta strandi214 – 220Combined sources7
Helixi221 – 230Combined sources10
Helixi232 – 234Combined sources3
Beta strandi236 – 240Combined sources5
Helixi242 – 256Combined sources15
Helixi259 – 261Combined sources3
Beta strandi263 – 267Combined sources5
Beta strandi273 – 277Combined sources5
Turni283 – 287Combined sources5
Helixi294 – 306Combined sources13
Helixi311 – 326Combined sources16
Helixi332 – 334Combined sources3
Helixi344 – 353Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4IWHX-ray1.75A/B1-355[»]
4XXVX-ray1.70A/B1-355[»]
ProteinModelPortaliQ2T7H6.
SMRiQ2T7H6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 1 subfamily.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000021112.
KOiK00052.
OMAiDTMHYSE.
OrthoDBiPOG091H01YH.

Family and domain databases

Gene3Di3.40.718.10. 1 hit.
HAMAPiMF_01033. LeuB_type1. 1 hit.
InterProiIPR019818. IsoCit/isopropylmalate_DH_CS.
IPR001804. Isocitrate/isopropylmalate_DH.
IPR024084. IsoPropMal-DH-like_dom.
IPR004429. Isopropylmalate_DH.
[Graphical view]
PANTHERiPTHR11835. PTHR11835. 1 hit.
PfamiPF00180. Iso_dh. 1 hit.
[Graphical view]
SMARTiSM01329. Iso_dh. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00169. leuB. 1 hit.
PROSITEiPS00470. IDH_IMDH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q2T7H6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKIAVLPGDG IGPEIVNEAV KVLNALDEKF ELEHAPVGGA GYEASGHPLP
60 70 80 90 100
DATLALAKEA DAILFGAVGD WKYDSLERAL RPEQAILGLR KHLELFANFR
110 120 130 140 150
PAICYPQLVD ASPLKPELVA GLDILIVREL NGDIYFGQPR GVRAAPDGPF
160 170 180 190 200
AGEREGFDTM RYSEPEVRRI AHVAFQAAQK RAKKLLSVDK SNVLETSQFW
210 220 230 240 250
RDVMIDVSKE YADVELSHMY VDNAAMQLAK APKQFDVIVT GNMFGDILSD
260 270 280 290 300
EASMLTGSIG MLPSASLDKN NKGLYEPSHG SAPDIAGKGI ANPLATILSA
310 320 330 340 350
AMLLRYSLNR AEQADRIERA VKTVLEQGYR TGDIATPGCR QVGTAAMGDA

VVAAL
Length:355
Mass (Da):38,242
Last modified:January 24, 2006 - v1
Checksum:iCE8C13AF0007C5E4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000085 Genomic DNA. Translation: ABC35976.1.
RefSeqiWP_009895843.1. NZ_CM000439.1.

Genome annotation databases

EnsemblBacteriaiABC35976; ABC35976; BTH_II0674.
KEGGibte:BTH_II0674.
PATRICi19298864. VBIBurTha36512_0762.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000085 Genomic DNA. Translation: ABC35976.1.
RefSeqiWP_009895843.1. NZ_CM000439.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4IWHX-ray1.75A/B1-355[»]
4XXVX-ray1.70A/B1-355[»]
ProteinModelPortaliQ2T7H6.
SMRiQ2T7H6.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABC35976; ABC35976; BTH_II0674.
KEGGibte:BTH_II0674.
PATRICi19298864. VBIBurTha36512_0762.

Phylogenomic databases

HOGENOMiHOG000021112.
KOiK00052.
OMAiDTMHYSE.
OrthoDBiPOG091H01YH.

Enzyme and pathway databases

UniPathwayiUPA00048; UER00072.

Family and domain databases

Gene3Di3.40.718.10. 1 hit.
HAMAPiMF_01033. LeuB_type1. 1 hit.
InterProiIPR019818. IsoCit/isopropylmalate_DH_CS.
IPR001804. Isocitrate/isopropylmalate_DH.
IPR024084. IsoPropMal-DH-like_dom.
IPR004429. Isopropylmalate_DH.
[Graphical view]
PANTHERiPTHR11835. PTHR11835. 1 hit.
PfamiPF00180. Iso_dh. 1 hit.
[Graphical view]
SMARTiSM01329. Iso_dh. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00169. leuB. 1 hit.
PROSITEiPS00470. IDH_IMDH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLEU3_BURTA
AccessioniPrimary (citable) accession number: Q2T7H6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2006
Last sequence update: January 24, 2006
Last modified: November 2, 2016
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.