LIUE_PSEAE
ID LIUE_PSEAE Reviewed; 300 AA.
AC Q9I2A0;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=3-hydroxy-3-isohexenylglutaryl-CoA/hydroxy-methylglutaryl-CoA lyase {ECO:0000303|PubMed:19459965, ECO:0000303|PubMed:19597963};
DE Short=HIHG-CoA lyase {ECO:0000303|PubMed:19597963};
DE Short=HMG-CoA lyase {ECO:0000303|PubMed:19459965};
DE EC=4.1.3.26 {ECO:0000269|PubMed:19597963};
DE EC=4.1.3.4 {ECO:0000269|PubMed:19459965, ECO:0000269|PubMed:19597963};
DE AltName: Full=(S)-3-hydroxy-3-methylglutaryl-CoA acetoacetate-lyase {ECO:0000303|PubMed:19459965};
DE AltName: Full=3-hydroxy-3-(4-methylpent-3-en-1-yl)glutaryl-CoA acetate-lyase {ECO:0000303|PubMed:19459965};
GN Name=liuE {ECO:0000303|PubMed:19459965};
GN OrderedLocusNames=PA2011 {ECO:0000303|PubMed:19459965};
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, COFACTOR, AND SUBSTRATE SPECIFICITY.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=19459965; DOI=10.1111/j.1574-6968.2009.01624.x;
RA Chavez-Aviles M., Diaz-Perez A.L., Reyes-de la Cruz H., Campos-Garcia J.;
RT "The Pseudomonas aeruginosa liuE gene encodes the 3-hydroxy-3-
RT methylglutaryl coenzyme A lyase, involved in leucine and acyclic terpene
RT catabolism.";
RL FEMS Microbiol. Lett. 296:117-123(2009).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=19597963; DOI=10.1007/s11033-009-9611-6;
RA Chavez-Aviles M., Diaz-Perez A.L., Campos-Garcia J.;
RT "The bifunctional role of LiuE from Pseudomonas aeruginosa, displays
RT additionally HIHG-CoA lyase enzymatic activity.";
RL Mol. Biol. Rep. 37:1787-1791(2010).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH SODIUM IONS.
RA Xiao T., Evdokimova E., Liu Y., Kudritska M., Savchenko A., Pai E.F.,
RA Edwards A.;
RT "Crystal Structure of hydroxymethylglutaryl-CoA lyase from Pseudomonas
RT aeruginosa.";
RL Submitted (JAN-2006) to the PDB data bank.
CC -!- FUNCTION: Involved in the L-leucine, isovalerate and acyclic
CC monoterpene catabolism. Catalyzes the cleavage of 3-hydroxy-3-
CC methylglutaryl-CoA (HMG-CoA) to yield acetyl-CoA and acetoacetate. It
CC can also catalyze the cleavage of 3-hydroxy-3-isohexenylglutaryl-CoA
CC (HIHG_CoA) to yield 7-methyl-3-oxooct-6-enoyl-CoA and acetate.
CC {ECO:0000269|PubMed:19459965, ECO:0000269|PubMed:19597963}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-hydroxy-3-(4-methylpent-3-en-1-yl)glutaryl-CoA = 7-methyl-3-
CC oxooct-6-enoyl-CoA + acetate; Xref=Rhea:RHEA:23084,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:57341, ChEBI:CHEBI:71410; EC=4.1.3.26;
CC Evidence={ECO:0000269|PubMed:19459965, ECO:0000269|PubMed:19597963};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-hydroxy-3-methylglutaryl-CoA = acetoacetate + acetyl-CoA;
CC Xref=Rhea:RHEA:24404, ChEBI:CHEBI:13705, ChEBI:CHEBI:43074,
CC ChEBI:CHEBI:57288; EC=4.1.3.4;
CC Evidence={ECO:0000269|PubMed:19597963};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:19459965};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:19459965};
CC Note=Divalent cations such as magnesium or manganese.
CC {ECO:0000269|PubMed:19459965};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=100 uM for HMG-CoA (at pH 6.7 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:19459965};
CC Vmax=21.7 umol/min/mg enzyme (at pH 6.7 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:19459965};
CC pH dependence:
CC Optimum pH is 7. {ECO:0000269|PubMed:19459965};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:19459965};
CC -!- PATHWAY: Metabolic intermediate metabolism; (S)-3-hydroxy-3-
CC methylglutaryl-CoA degradation; acetoacetate from (S)-3-hydroxy-3-
CC methylglutaryl-CoA: step 1/1. {ECO:0000305}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19459965}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to utilize L-
CC leucine, isovalerate or acyclic terpenes as carbon source.
CC {ECO:0000269|PubMed:19459965}.
CC -!- SIMILARITY: Belongs to the HMG-CoA lyase family. {ECO:0000305}.
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DR EMBL; AE004091; AAG05399.1; -; Genomic_DNA.
DR PIR; H83394; H83394.
DR RefSeq; NP_250701.1; NC_002516.2.
DR RefSeq; WP_003088593.1; NZ_QZGE01000026.1.
DR PDB; 2FTP; X-ray; 2.40 A; A=1-300.
DR PDBsum; 2FTP; -.
DR AlphaFoldDB; Q9I2A0; -.
DR SMR; Q9I2A0; -.
DR STRING; 287.DR97_5837; -.
DR PaxDb; Q9I2A0; -.
DR PRIDE; Q9I2A0; -.
DR DNASU; 878857; -.
DR EnsemblBacteria; AAG05399; AAG05399; PA2011.
DR GeneID; 878857; -.
DR KEGG; pae:PA2011; -.
DR PATRIC; fig|208964.12.peg.2095; -.
DR PseudoCAP; PA2011; -.
DR HOGENOM; CLU_022138_3_2_6; -.
DR InParanoid; Q9I2A0; -.
DR OMA; FHNTRGT; -.
DR PhylomeDB; Q9I2A0; -.
DR BioCyc; MetaCyc:MON-16069; -.
DR BioCyc; PAER208964:G1FZ6-2049-MON; -.
DR BRENDA; 4.1.3.26; 8015.
DR UniPathway; UPA00896; UER00863.
DR EvolutionaryTrace; Q9I2A0; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0047445; F:3-hydroxy-3-isohexenylglutaryl-CoA lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0004419; F:hydroxymethylglutaryl-CoA lyase activity; IMP:PseudoCAP.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008300; P:isoprenoid catabolic process; IMP:PseudoCAP.
DR GO; GO:0046951; P:ketone body biosynthetic process; IBA:GO_Central.
DR GO; GO:0006552; P:leucine catabolic process; IMP:PseudoCAP.
DR GO; GO:0006629; P:lipid metabolic process; IBA:GO_Central.
DR GO; GO:0046247; P:terpene catabolic process; IMP:PseudoCAP.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000138; HMG_CoA_lyase_AS.
DR InterPro; IPR043594; HMGL.
DR InterPro; IPR000891; PYR_CT.
DR PANTHER; PTHR42738; PTHR42738; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR PROSITE; PS01062; HMG_COA_LYASE; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Lyase; Magnesium; Manganese; Metal-binding;
KW Reference proteome.
FT CHAIN 1..300
FT /note="3-hydroxy-3-isohexenylglutaryl-CoA/hydroxy-
FT methylglutaryl-CoA lyase"
FT /id="PRO_0000430769"
FT DOMAIN 7..274
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
FT ACT_SITE 240
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10115"
FT BINDING 15
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 16
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000305|Ref.4"
FT BINDING 207
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000305|Ref.4"
FT BINDING 209
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000305|Ref.4"
FT BINDING 249
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000305|Ref.4"
FT STRAND 8..11
FT /evidence="ECO:0007829|PDB:2FTP"
FT TURN 13..15
FT /evidence="ECO:0007829|PDB:2FTP"
FT HELIX 16..19
FT /evidence="ECO:0007829|PDB:2FTP"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:2FTP"
FT HELIX 27..39
FT /evidence="ECO:0007829|PDB:2FTP"
FT STRAND 43..49
FT /evidence="ECO:0007829|PDB:2FTP"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:2FTP"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:2FTP"
FT HELIX 62..68
FT /evidence="ECO:0007829|PDB:2FTP"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:2FTP"
FT HELIX 84..92
FT /evidence="ECO:0007829|PDB:2FTP"
FT STRAND 97..104
FT /evidence="ECO:0007829|PDB:2FTP"
FT HELIX 106..113
FT /evidence="ECO:0007829|PDB:2FTP"
FT HELIX 117..133
FT /evidence="ECO:0007829|PDB:2FTP"
FT STRAND 137..143
FT /evidence="ECO:0007829|PDB:2FTP"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:2FTP"
FT HELIX 156..168
FT /evidence="ECO:0007829|PDB:2FTP"
FT STRAND 172..181
FT /evidence="ECO:0007829|PDB:2FTP"
FT HELIX 185..195
FT /evidence="ECO:0007829|PDB:2FTP"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:2FTP"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:2FTP"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:2FTP"
FT HELIX 215..224
FT /evidence="ECO:0007829|PDB:2FTP"
FT STRAND 229..233
FT /evidence="ECO:0007829|PDB:2FTP"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:2FTP"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:2FTP"
FT HELIX 252..261
FT /evidence="ECO:0007829|PDB:2FTP"
FT HELIX 270..284
FT /evidence="ECO:0007829|PDB:2FTP"
FT HELIX 291..299
FT /evidence="ECO:0007829|PDB:2FTP"
SQ SEQUENCE 300 AA; 31837 MW; 55ABE12688FCBE90 CRC64;
MNLPKKVRLV EVGPRDGLQN EKQPIEVADK IRLVDDLSAA GLDYIEVGSF VSPKWVPQMA
GSAEVFAGIR QRPGVTYAAL APNLKGFEAA LESGVKEVAV FAAASEAFSQ RNINCSIKDS
LERFVPVLEA ARQHQVRVRG YISCVLGCPY DGDVDPRQVA WVARELQQMG CYEVSLGDTI
GVGTAGATRR LIEAVASEVP RERLAGHFHD TYGQALANIY ASLLEGIAVF DSSVAGLGGC
PYAKGATGNV ASEDVLYLLN GLEIHTGVDM HALVDAGQRI CAVLGKSNGS RAAKALLAKA
