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Protein

3-isopropylmalate dehydrogenase

Gene

leuB

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
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.

Catalytic activityi

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

Cofactori

Mg2+, Mn2+Note: Binds 1 Mg2+ or Mn2+ ion per subunit.

Pathwayi: L-leucine biosynthesis

This protein is involved in step 3 of the subpathway that synthesizes L-leucine from 3-methyl-2-oxobutanoate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. 2-isopropylmalate synthase (leuA), 2-isopropylmalate synthase (leuA)
  2. 3-isopropylmalate dehydratase small subunit (leuD), 3-isopropylmalate dehydratase large subunit 2 (leuC2), 3-isopropylmalate dehydratase small subunit 2 (leuD2), 3-isopropylmalate dehydratase large subunit (leuC), 3-isopropylmalate dehydratase large subunit 1 (leuC1), 3-isopropylmalate dehydratase small subunit 1 (leuD1), 3-isopropylmalate dehydratase large subunit (leuC), 3-isopropylmalate dehydratase small subunit (leuD)
  3. 3-isopropylmalate dehydrogenase (leuB), 3-isopropylmalate dehydrogenase (leuB)
  4. Probable branched-chain-amino-acid aminotransferase (ilvE)
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei95 – 951SubstrateBy similarity
Binding sitei105 – 1051SubstrateBy similarity
Binding sitei134 – 1341SubstrateBy similarity
Sitei141 – 1411Important for catalysisBy similarity
Sitei187 – 1871Important for catalysisBy similarity
Metal bindingi219 – 2191Magnesium or manganeseBy similarity
Binding sitei219 – 2191SubstrateBy similarity
Metal bindingi243 – 2431Magnesium or manganeseBy similarity
Metal bindingi247 – 2471Magnesium or manganeseBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi74 – 8714NADBy similarityAdd
BLAST
Nucleotide bindingi275 – 28713NADBy similarityAdd
BLAST

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 dehydrogenase (EC:1.1.1.85)
Alternative name(s):
3-IPM-DH
Beta-IPM dehydrogenase
Short name:
IMDH
Gene namesi
Name:leuB
Ordered Locus Names:TM_0556
OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Taxonomic identifieri243274 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
Proteomesi
  • UP000008183 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3543543-isopropylmalate dehydrogenasePRO_0000083771Add
BLAST

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi243274.TM0556.

Structurei

Secondary structure

354
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1 – 99Combined sources
Helixi11 – 3020Combined sources
Beta strandi33 – 386Combined sources
Helixi43 – 497Combined sources
Beta strandi50 – 534Combined sources
Helixi55 – 639Combined sources
Beta strandi64 – 718Combined sources
Helixi75 – 773Combined sources
Helixi86 – 894Combined sources
Helixi91 – 977Combined sources
Beta strandi102 – 1087Combined sources
Helixi111 – 1166Combined sources
Beta strandi117 – 1193Combined sources
Helixi121 – 1244Combined sources
Beta strandi129 – 1357Combined sources
Helixi139 – 1413Combined sources
Beta strandi143 – 1486Combined sources
Beta strandi153 – 1564Combined sources
Helixi161 – 17616Combined sources
Turni177 – 1793Combined sources
Beta strandi180 – 1867Combined sources
Turni188 – 1903Combined sources
Helixi192 – 20514Combined sources
Beta strandi211 – 2177Combined sources
Helixi218 – 22710Combined sources
Helixi229 – 2313Combined sources
Beta strandi233 – 2375Combined sources
Helixi239 – 24911Combined sources
Beta strandi252 – 2543Combined sources
Helixi256 – 2583Combined sources
Beta strandi260 – 27415Combined sources
Turni278 – 2847Combined sources
Helixi289 – 30315Combined sources
Helixi306 – 32116Combined sources
Helixi327 – 3293Combined sources
Helixi333 – 3353Combined sources
Helixi339 – 35315Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VLCX-ray1.90A1-354[»]
ProteinModelPortaliQ9WZ26.
SMRiQ9WZ26. Positions 1-354.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9WZ26.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105C0C. Bacteria.
COG0473. LUCA.
InParanoidiQ9WZ26.
KOiK00052.
OMAiRRPKQFD.

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.

Q9WZ26-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKIAVLPGDG IGPEVVREAL KVLEVVEKKT GKTFEKVFGH IGGDAIDRFG
60 70 80 90 100
EPLPEETKKI CLEADAIFLG SVGGPKWDDL PPEKRPEIGG LLALRKMLNL
110 120 130 140 150
YANIRPIKVY RSLVHVSPLK EKVIGSGVDL VTVRELSYGV YYGQPRGLDE
160 170 180 190 200
EKGFDTMIYD RKTVERIART AFEIAKNRRK KVTSVDKANV LYSSMLWRKV
210 220 230 240 250
VNEVAREYPD VELTHIYVDN AAMQLILKPS QFDVILTTNM FGDILSDESA
260 270 280 290 300
ALPGSLGLLP SASFGDKNLY EPAGGSAPDI AGKNIANPIA QILSLAMMLE
310 320 330 340 350
HSFGMVEEAR KIERAVELVI EEGYRTRDIA EDPEKAVSTS QMGDLICKKL

EEIW
Length:354
Mass (Da):39,190
Last modified:November 1, 1999 - v1
Checksum:i2C93ACBF888A0D38
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD35641.1.
PIRiB72363.
RefSeqiNP_228366.1. NC_000853.1.
WP_004081326.1. NZ_CP011107.1.

Genome annotation databases

EnsemblBacteriaiAAD35641; AAD35641; TM_0556.
GeneIDi897614.
KEGGitma:TM0556.
tmi:THEMA_01895.
tmw:THMA_0569.
PATRICi23936019. VBITheMar51294_0564.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD35641.1.
PIRiB72363.
RefSeqiNP_228366.1. NC_000853.1.
WP_004081326.1. NZ_CP011107.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VLCX-ray1.90A1-354[»]
ProteinModelPortaliQ9WZ26.
SMRiQ9WZ26. Positions 1-354.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243274.TM0556.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD35641; AAD35641; TM_0556.
GeneIDi897614.
KEGGitma:TM0556.
tmi:THEMA_01895.
tmw:THMA_0569.
PATRICi23936019. VBITheMar51294_0564.

Phylogenomic databases

eggNOGiENOG4105C0C. Bacteria.
COG0473. LUCA.
InParanoidiQ9WZ26.
KOiK00052.
OMAiRRPKQFD.

Enzyme and pathway databases

UniPathwayiUPA00048; UER00072.

Miscellaneous databases

EvolutionaryTraceiQ9WZ26.

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_THEMA
AccessioniPrimary (citable) accession number: Q9WZ26
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: September 7, 2016
This is version 124 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, Reference 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.