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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: Annotation score: 5 out of 5-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

  • isoprenoid catabolic process Source: PseudoCAP
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Magnesium, Manganese, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16069.
BRENDAi4.1.3.26. 8015.
UniPathwayiUPA00896; 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
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi8 – 11Combined sources4
Turni13 – 15Combined sources3
Helixi16 – 19Combined sources4
Beta strandi21 – 23Combined sources3
Helixi27 – 39Combined sources13
Beta strandi43 – 49Combined sources7
Turni53 – 55Combined sources3
Helixi57 – 59Combined sources3
Helixi62 – 68Combined sources7
Beta strandi75 – 80Combined sources6
Helixi84 – 92Combined sources9
Beta strandi97 – 104Combined sources8
Helixi106 – 113Combined sources8
Helixi117 – 133Combined sources17
Beta strandi137 – 143Combined sources7
Turni149 – 151Combined sources3
Helixi156 – 168Combined sources13
Beta strandi172 – 181Combined sources10
Helixi185 – 195Combined sources11
Turni196 – 198Combined sources3
Helixi201 – 203Combined sources3
Beta strandi204 – 209Combined sources6
Helixi215 – 224Combined sources10
Beta strandi229 – 233Combined sources5
Helixi234 – 236Combined sources3
Helixi241 – 243Combined sources3
Helixi252 – 261Combined sources10
Helixi270 – 284Combined sources15
Helixi291 – 299Combined sources9

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...

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
Contains 1 pyruvate carboxyltransferase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105CBH. Bacteria.
COG0119. LUCA.
HOGENOMiHOG000219757.
InParanoidiQ9I2A0.
KOiK01640.
OMAiEAFAQKN.
PhylomeDBiQ9I2A0.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR000138. HMG_CoA_lyase_AS.
IPR000891. PYR_CT.
[Graphical view]
PfamiPF00682. HMGL-like. 1 hit.
[Graphical view]
PROSITEiPS01062. HMG_COA_LYASE. 1 hit.
PS50991. PYR_CT. 1 hit.
[Graphical view]

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. NZ_ASJY01000287.1.

Genome annotation databases

EnsemblBacteriaiAAG05399; AAG05399; PA2011.
GeneIDi878857.
KEGGipae:PA2011.
PATRICi19838429. VBIPseAer58763_2095.

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. NZ_ASJY01000287.1.

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.
PATRICi19838429. VBIPseAer58763_2095.

Organism-specific databases

PseudoCAPiPA2011.

Phylogenomic databases

eggNOGiENOG4105CBH. Bacteria.
COG0119. LUCA.
HOGENOMiHOG000219757.
InParanoidiQ9I2A0.
KOiK01640.
OMAiEAFAQKN.
PhylomeDBiQ9I2A0.

Enzyme and pathway databases

UniPathwayiUPA00896; UER00863.
BioCyciMetaCyc:MONOMER-16069.
BRENDAi4.1.3.26. 8015.

Miscellaneous databases

EvolutionaryTraceiQ9I2A0.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR000138. HMG_CoA_lyase_AS.
IPR000891. PYR_CT.
[Graphical view]
PfamiPF00682. HMGL-like. 1 hit.
[Graphical view]
PROSITEiPS01062. HMG_COA_LYASE. 1 hit.
PS50991. PYR_CT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLIUE_PSEAE
AccessioniPrimary (citable) accession number: Q9I2A0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 29, 2014
Last sequence update: March 1, 2001
Last modified: November 2, 2016
This is version 86 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.