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Protein

3-hydroxy-3-isohexenylglutaryl-CoA/hydroxy-methylglutaryl-CoA lyase

Gene

liuE

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Involved in the L-leucine, isovalerate and acyclic monoterpene catabolism. Catalyzes the cleavage of 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA) to yield acetyl-CoA and acetoacetate. It can also catalyze the cleavage of 3-hydroxy-3-isohexenylglutaryl-CoA (HIHG_CoA) to yield 7-methyl-3-oxooct-6-enoyl-CoA and acetate.2 Publications

Catalytic activityi

3-hydroxy-3-(4-methylpent-3-en-1-yl)glutaryl-CoA = 7-methyl-3-oxooct-6-enoyl-CoA + acetate.2 Publications
(S)-3-hydroxy-3-methylglutaryl-CoA = acetyl-CoA + acetoacetate.1 Publication

Cofactori

Mg2+1 Publication, Mn2+1 PublicationNote: Divalent cations such as magnesium or manganese.1 Publication

Kineticsi

  1. KM=100 µM for HMG-CoA (at pH 6.7 and 37 degrees Celsius)1 Publication
  1. Vmax=21.7 µmol/min/mg enzyme (at pH 6.7 and 37 degrees Celsius)1 Publication

pH dependencei

Optimum pH is 7.1 Publication

Temperature dependencei

Optimum temperature is 37 degrees Celsius.1 Publication

Pathwayi: (S)-3-hydroxy-3-methylglutaryl-CoA degradation

This protein is involved in step 1 of the subpathway that synthesizes acetoacetate from (S)-3-hydroxy-3-methylglutaryl-CoA.Curated
Proteins known to be involved in this subpathway in this organism are:
  1. 3-hydroxy-3-isohexenylglutaryl-CoA/hydroxy-methylglutaryl-CoA lyase (liuE)
This subpathway is part of the pathway (S)-3-hydroxy-3-methylglutaryl-CoA degradation, which is itself part of Metabolic intermediate metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes acetoacetate from (S)-3-hydroxy-3-methylglutaryl-CoA, the pathway (S)-3-hydroxy-3-methylglutaryl-CoA degradation and in Metabolic intermediate metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei15SubstrateBy similarity1
Metal bindingi16Divalent metal cation1 Publication1
Metal bindingi207Divalent metal cation1 Publication1
Metal bindingi209Divalent metal cation1 Publication1
Active sitei240PROSITE-ProRule annotation1
Metal bindingi249Divalent metal cation1 Publication1

GO - Molecular functioni

  • 3-hydroxy-3-isohexenylglutaryl-CoA lyase activity Source: UniProtKB-EC
  • hydroxymethylglutaryl-CoA lyase activity Source: PseudoCAP
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

Keywordsi

Molecular functionLyase
LigandMagnesium, Manganese, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16069
PAER208964:G1FZ6-2049-MONOMER
BRENDAi4.1.3.26 8015
UniPathwayi
UPA00896;UER00863

Names & Taxonomyi

Protein namesi
Recommended name:
3-hydroxy-3-isohexenylglutaryl-CoA/hydroxy-methylglutaryl-CoA lyase2 Publications (EC:4.1.3.261 Publication, EC:4.1.3.42 Publications)
Short name:
HIHG-CoA lyase1 Publication
Short name:
HMG-CoA lyase1 Publication
Alternative name(s):
(S)-3-hydroxy-3-methylglutaryl-CoA acetoacetate-lyase1 Publication
3-hydroxy-3-(4-methylpent-3-en-1-yl)glutaryl-CoA acetate-lyase1 Publication
Gene namesi
Name:liuE1 Publication
Ordered Locus Names:PA20111 Publication
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000002438 Componenti: Chromosome

Organism-specific databases

PseudoCAPiPA2011

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene are unable to utilize L-leucine, isovalerate or acyclic terpenes as carbon source.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004307691 – 3003-hydroxy-3-isohexenylglutaryl-CoA/hydroxy-methylglutaryl-CoA lyaseAdd BLAST300

Proteomic databases

PaxDbiQ9I2A0

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi208964.PA2011

Structurei

Secondary structure

1300
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ9I2A0
SMRiQ9I2A0
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9I2A0

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini7 – 274Pyruvate carboxyltransferasePROSITE-ProRule annotationAdd BLAST268

Sequence similaritiesi

Belongs to the HMG-CoA lyase family.Curated

Phylogenomic databases

eggNOGiENOG4105CBH Bacteria
COG0119 LUCA
HOGENOMiHOG000219757
InParanoidiQ9I2A0
KOiK01640
OMAiFGGCPMA
PhylomeDBiQ9I2A0

Family and domain databases

Gene3Di3.20.20.70, 1 hit
InterProiView protein in InterPro
IPR013785 Aldolase_TIM
IPR000138 HMG_CoA_lyase_AS
IPR000891 PYR_CT
PfamiView protein in Pfam
PF00682 HMGL-like, 1 hit
PROSITEiView protein in PROSITE
PS01062 HMG_COA_LYASE, 1 hit
PS50991 PYR_CT, 1 hit

Sequencei

Sequence statusi: Complete.

Q9I2A0-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNLPKKVRLV EVGPRDGLQN EKQPIEVADK IRLVDDLSAA GLDYIEVGSF
60 70 80 90 100
VSPKWVPQMA GSAEVFAGIR QRPGVTYAAL APNLKGFEAA LESGVKEVAV
110 120 130 140 150
FAAASEAFSQ RNINCSIKDS LERFVPVLEA ARQHQVRVRG YISCVLGCPY
160 170 180 190 200
DGDVDPRQVA WVARELQQMG CYEVSLGDTI GVGTAGATRR LIEAVASEVP
210 220 230 240 250
RERLAGHFHD TYGQALANIY ASLLEGIAVF DSSVAGLGGC PYAKGATGNV
260 270 280 290 300
ASEDVLYLLN GLEIHTGVDM HALVDAGQRI CAVLGKSNGS RAAKALLAKA
Length:300
Mass (Da):31,837
Last modified:March 1, 2001 - v1
Checksum:i55ABE12688FCBE90
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004091 Genomic DNA Translation: AAG05399.1
PIRiH83394
RefSeqiNP_250701.1, NC_002516.2
WP_003088593.1, NC_002516.2

Genome annotation databases

EnsemblBacteriaiAAG05399; AAG05399; PA2011
GeneIDi878857
KEGGipae:PA2011
PATRICifig|208964.12.peg.2095

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004091 Genomic DNA Translation: AAG05399.1
PIRiH83394
RefSeqiNP_250701.1, NC_002516.2
WP_003088593.1, NC_002516.2

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2FTPX-ray2.40A1-300[»]
ProteinModelPortaliQ9I2A0
SMRiQ9I2A0
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi208964.PA2011

Proteomic databases

PaxDbiQ9I2A0

Protocols and materials databases

DNASUi878857
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG05399; AAG05399; PA2011
GeneIDi878857
KEGGipae:PA2011
PATRICifig|208964.12.peg.2095

Organism-specific databases

PseudoCAPiPA2011

Phylogenomic databases

eggNOGiENOG4105CBH Bacteria
COG0119 LUCA
HOGENOMiHOG000219757
InParanoidiQ9I2A0
KOiK01640
OMAiFGGCPMA
PhylomeDBiQ9I2A0

Enzyme and pathway databases

UniPathwayi
UPA00896;UER00863

BioCyciMetaCyc:MONOMER-16069
PAER208964:G1FZ6-2049-MONOMER
BRENDAi4.1.3.26 8015

Miscellaneous databases

EvolutionaryTraceiQ9I2A0

Family and domain databases

Gene3Di3.20.20.70, 1 hit
InterProiView protein in InterPro
IPR013785 Aldolase_TIM
IPR000138 HMG_CoA_lyase_AS
IPR000891 PYR_CT
PfamiView protein in Pfam
PF00682 HMGL-like, 1 hit
PROSITEiView protein in PROSITE
PS01062 HMG_COA_LYASE, 1 hit
PS50991 PYR_CT, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiLIUE_PSEAE
AccessioniPrimary (citable) accession number: Q9I2A0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 29, 2014
Last sequence update: March 1, 2001
Last modified: February 28, 2018
This is version 91 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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