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Protein

3-isopropylmalate dehydrogenase

Gene

leuB

Organism
Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
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.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)
  2. 3-isopropylmalate dehydratase small subunit (leuD), 3-isopropylmalate dehydratase large subunit (leuC)
  3. 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei98 – 981SubstrateUniRule annotation
Binding sitei108 – 1081SubstrateUniRule annotation
Binding sitei137 – 1371SubstrateUniRule annotation
Sitei144 – 1441Important for catalysisUniRule annotation
Sitei189 – 1891Important for catalysisUniRule annotation
Metal bindingi221 – 2211Magnesium or manganeseUniRule annotation
Binding sitei221 – 2211SubstrateUniRule annotation
Metal bindingi245 – 2451Magnesium or manganeseUniRule annotation
Metal bindingi249 – 2491Magnesium or manganeseUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi77 – 9014NADUniRule annotationAdd
BLAST
Nucleotide bindingi279 – 29113NADUniRule annotationAdd
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

BioCyciCJEJ192222:GJTS-1688-MONOMER.
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:Cj1718c
OrganismiCampylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Taxonomic identifieri192222 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter
Proteomesi
  • UP000000799 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3583583-isopropylmalate dehydrogenasePRO_0000083675Add
BLAST

Proteomic databases

PaxDbiQ9PLW0.
PRIDEiQ9PLW0.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

IntActiQ9PLW0. 6 interactions.
STRINGi192222.Cj1718c.

Structurei

Secondary structure

1
358
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 1210Combined sources
Helixi15 – 3319Combined sources
Beta strandi36 – 416Combined sources
Helixi46 – 527Combined sources
Beta strandi53 – 564Combined sources
Helixi58 – 658Combined sources
Beta strandi67 – 748Combined sources
Helixi78 – 803Combined sources
Helixi85 – 873Combined sources
Helixi89 – 10113Combined sources
Beta strandi105 – 1117Combined sources
Helixi114 – 1196Combined sources
Beta strandi120 – 1223Combined sources
Helixi124 – 1274Combined sources
Beta strandi132 – 1387Combined sources
Helixi142 – 1443Combined sources
Beta strandi148 – 1503Combined sources
Beta strandi152 – 16211Combined sources
Helixi163 – 17917Combined sources
Beta strandi182 – 1887Combined sources
Turni190 – 1923Combined sources
Helixi194 – 20613Combined sources
Helixi207 – 2093Combined sources
Beta strandi213 – 2197Combined sources
Helixi220 – 22910Combined sources
Helixi231 – 2333Combined sources
Beta strandi235 – 2395Combined sources
Helixi241 – 25515Combined sources
Helixi258 – 2603Combined sources
Beta strandi262 – 2665Combined sources
Beta strandi268 – 2703Combined sources
Beta strandi272 – 2787Combined sources
Helixi282 – 2843Combined sources
Helixi293 – 30513Combined sources
Helixi310 – 32516Combined sources
Turni331 – 3333Combined sources
Beta strandi335 – 3373Combined sources
Helixi341 – 35414Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3UDOX-ray2.30A1-358[»]
3UDUX-ray1.85A/B/C/D/E/F/G/H1-358[»]
ProteinModelPortaliQ9PLW0.
SMRiQ9PLW0. Positions 2-354.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105C0C. Bacteria.
COG0473. LUCA.
HOGENOMiHOG000021112.
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.

Q9PLW0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTYKVAVLA GDGIGPLVMK EALKILTFIA QKYNFSFEFN EAKIGGASID
60 70 80 90 100
AYGVALSDET LKLCEQSDAI LFGSVGGPKW DNLPIDQRPE RASLLPLRKH
110 120 130 140 150
FNLFANLRPC KIYESLTHAS PLKNEIIQKG VDILCVRELT GGIYFGKQDL
160 170 180 190 200
GKESAYDTEI YTKKEIERIA RIAFESARIR KKKVHLIDKA NVLASSILWR
210 220 230 240 250
EVVANVAKDY QDINLEYMYV DNAAMQIVKN PSIFDVMLCS NLFGDILSDE
260 270 280 290 300
LAAINGSLGL LSSASLNDKG FGLYEPAGGS APDIAHLNIA NPIAQILSAA
310 320 330 340 350
LMLKYSFKEE QAAQDIENAI SLALAQGKMT KDLNAKSYLN TDEMGDCILE

ILKENDNG
Length:358
Mass (Da):39,368
Last modified:October 1, 2000 - v1
Checksum:i26B811645E7FFA83
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL111168 Genomic DNA. Translation: CAL35812.1.
PIRiB81270.
RefSeqiWP_002858793.1. NC_002163.1.
YP_002345084.1. NC_002163.1.

Genome annotation databases

EnsemblBacteriaiCAL35812; CAL35812; Cj1718c.
GeneIDi905995.
KEGGicje:Cj1718c.
PATRICi20060418. VBICamJej33762_1692.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL111168 Genomic DNA. Translation: CAL35812.1.
PIRiB81270.
RefSeqiWP_002858793.1. NC_002163.1.
YP_002345084.1. NC_002163.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3UDOX-ray2.30A1-358[»]
3UDUX-ray1.85A/B/C/D/E/F/G/H1-358[»]
ProteinModelPortaliQ9PLW0.
SMRiQ9PLW0. Positions 2-354.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9PLW0. 6 interactions.
STRINGi192222.Cj1718c.

Proteomic databases

PaxDbiQ9PLW0.
PRIDEiQ9PLW0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAL35812; CAL35812; Cj1718c.
GeneIDi905995.
KEGGicje:Cj1718c.
PATRICi20060418. VBICamJej33762_1692.

Phylogenomic databases

eggNOGiENOG4105C0C. Bacteria.
COG0473. LUCA.
HOGENOMiHOG000021112.
KOiK00052.
OMAiRRPKQFD.

Enzyme and pathway databases

UniPathwayiUPA00048; UER00072.
BioCyciCJEJ192222:GJTS-1688-MONOMER.

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_CAMJE
AccessioniPrimary (citable) accession number: Q9PLW0
Secondary accession number(s): Q0P7R3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: October 1, 2000
Last modified: September 7, 2016
This is version 100 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.