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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei15 – 151SubstrateBy similarity
Metal bindingi16 – 161Divalent metal cation1 Publication
Metal bindingi207 – 2071Divalent metal cation1 Publication
Metal bindingi209 – 2091Divalent metal cation1 Publication
Active sitei240 – 2401PROSITE-ProRule annotation
Metal bindingi249 – 2491Divalent metal cation1 Publication

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3003003-hydroxy-3-isohexenylglutaryl-CoA/hydroxy-methylglutaryl-CoA lyasePRO_0000430769Add
BLAST

Proteomic databases

PaxDbiQ9I2A0.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi208964.PA2011.

Structurei

Secondary structure

1
300
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 114Combined sources
Turni13 – 153Combined sources
Helixi16 – 194Combined sources
Beta strandi21 – 233Combined sources
Helixi27 – 3913Combined sources
Beta strandi43 – 497Combined sources
Turni53 – 553Combined sources
Helixi57 – 593Combined sources
Helixi62 – 687Combined sources
Beta strandi75 – 806Combined sources
Helixi84 – 929Combined sources
Beta strandi97 – 1048Combined sources
Helixi106 – 1138Combined sources
Helixi117 – 13317Combined sources
Beta strandi137 – 1437Combined sources
Turni149 – 1513Combined sources
Helixi156 – 16813Combined sources
Beta strandi172 – 18110Combined sources
Helixi185 – 19511Combined sources
Turni196 – 1983Combined sources
Helixi201 – 2033Combined sources
Beta strandi204 – 2096Combined sources
Helixi215 – 22410Combined sources
Beta strandi229 – 2335Combined sources
Helixi234 – 2363Combined sources
Helixi241 – 2433Combined sources
Helixi252 – 26110Combined sources
Helixi270 – 28415Combined sources
Helixi291 – 2999Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FTPX-ray2.40A1-300[»]
ProteinModelPortaliQ9I2A0.
SMRiQ9I2A0. Positions 1-291.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9I2A0.

Family & Domainsi

Sequence similaritiesi

Belongs to the HMG-CoA lyase family.Curated

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
EntryMethodResolution (Å)ChainPositionsPDBsum
2FTPX-ray2.40A1-300[»]
ProteinModelPortaliQ9I2A0.
SMRiQ9I2A0. Positions 1-291.
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: September 7, 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, 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.