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Database: UniProt
Entry: Q3JWU6_BURP1
LinkDB: Q3JWU6_BURP1
Original site: Q3JWU6_BURP1 
ID   Q3JWU6_BURP1            Unreviewed;       311 AA.
AC   Q3JWU6;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   RecName: Full=hydroxymethylglutaryl-CoA lyase {ECO:0000256|ARBA:ARBA00012910};
DE            EC=4.1.3.4 {ECO:0000256|ARBA:ARBA00012910};
GN   OrderedLocusNames=BURPS1710b_0543 {ECO:0000313|EMBL:ABA47965.1};
OS   Burkholderia pseudomallei (strain 1710b).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=320372 {ECO:0000313|EMBL:ABA47965.1, ECO:0000313|Proteomes:UP000002700};
RN   [1] {ECO:0000313|EMBL:ABA47965.1, ECO:0000313|Proteomes:UP000002700}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1710b {ECO:0000313|EMBL:ABA47965.1,
RC   ECO:0000313|Proteomes:UP000002700};
RA   Woods D.E., Nierman W.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001651};
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:0000256|ARBA:ARBA00005143}.
CC   -!- SIMILARITY: Belongs to the HMG-CoA lyase family.
CC       {ECO:0000256|ARBA:ARBA00009405}.
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DR   EMBL; CP000124; ABA47965.1; -; Genomic_DNA.
DR   RefSeq; WP_004522997.1; NC_007434.1.
DR   AlphaFoldDB; Q3JWU6; -.
DR   EnsemblBacteria; ABA47965; ABA47965; BURPS1710b_0543.
DR   GeneID; 56527423; -.
DR   KEGG; bpm:BURPS1710b_0543; -.
DR   HOGENOM; CLU_022138_3_2_4; -.
DR   UniPathway; UPA00896; UER00863.
DR   Proteomes; UP000002700; Chromosome I.
DR   GO; GO:0004419; F:hydroxymethylglutaryl-CoA lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd07938; DRE_TIM_HMGL; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 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; HYDROXYMETHYLGLUTARYL-COA LYASE; 1.
DR   PANTHER; PTHR42738:SF7; HYDROXYMETHYLGLUTARYL-COA LYASE; 1.
DR   Pfam; PF00682; HMGL-like; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   PROSITE; PS01062; HMG_COA_LYASE; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:ABA47965.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          7..274
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
SQ   SEQUENCE   311 AA;  32434 MW;  AEBF65508A100A60 CRC64;
     MTLPQSVKIV EVGPRDGLQN EQTFVPTGVK IELVNRLSQA GFRNVEAASF VSPKWVPQMA
     DGADVMAGIA RRAGTIYSAL TPNLKGVENA LAARADEVVI FGAASEAFSR RNINCSIAES
     IARFEPVARA AKDAGVRLRA SVSCALGCPY QGDVPLEAVV DVVERLAALG CDEIDIADTI
     GVGTPGRTRA VLDAVAKAFP RERLSGHFHD TYGQALANIY AALLEGIAIF HASVAGLGGC
     PYAKGATGNV ATEDVLYMMR GLNIETGVDL DQVVAAGDFI SNAIGRANIS RAGRALLAKQ
     RAAAEPPSAC A
//
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