ID F2LF53_BURGS Unreviewed; 308 AA.
AC F2LF53;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=hydroxymethylglutaryl-CoA lyase {ECO:0000256|ARBA:ARBA00012910};
DE EC=4.1.3.4 {ECO:0000256|ARBA:ARBA00012910};
GN OrderedLocusNames=bgla_1g36490 {ECO:0000313|EMBL:AEA62252.1};
OS Burkholderia gladioli (strain BSR3).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=999541 {ECO:0000313|EMBL:AEA62252.1, ECO:0000313|Proteomes:UP000008316};
RN [1] {ECO:0000313|EMBL:AEA62252.1, ECO:0000313|Proteomes:UP000008316}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BSR3 {ECO:0000313|EMBL:AEA62252.1,
RC ECO:0000313|Proteomes:UP000008316};
RX PubMed=21478339; DOI=10.1128/JB.00420-11;
RA Seo Y.S., Lim J., Choi B.S., Kim H., Goo E., Lee B., Lim J.S., Choi I.Y.,
RA Moon J.S., Kim J., Hwang I.;
RT "Complete genome sequence of Burkholderia gladioli BSR3.";
RL J. Bacteriol. 193:3149-3149(2011).
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; CP002599; AEA62252.1; -; Genomic_DNA.
DR RefSeq; WP_013699567.1; NC_015381.1.
DR AlphaFoldDB; F2LF53; -.
DR STRING; 999541.bgla_1g36490; -.
DR KEGG; bgd:bgla_1g36490; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_022138_3_2_4; -.
DR UniPathway; UPA00896; UER00863.
DR Proteomes; UP000008316; Chromosome 1.
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:AEA62252.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 7..274
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 308 AA; 32336 MW; DEB9732C7A0B1B7F CRC64;
MTYPAAVKIV EVGPRDGLQN EKSFVPTETK IALVDRLSKA GLRNVEAASF VSPKWVPQMA
DGAELMAGIA RRPGTIYSVL TPNLKGLENA LAARADEVVI FGAASEAFSQ KNINCSIAES
IARFEPVARA AKDAGVRLRG SISCSLGCPY QGEVPVAAVI DVVERFAALG CDEIDIADTI
GVGTAARTRA LMAEVARVFP RERLSGHFHD TYGQALANIH AALLEGIEIF HASVAGLGGC
PYAKGATGNV ATEDVLYLMQ GLGIETGIDL GEVVEAGDFI SRAIGRENAS RAGRALLVKR
RDAQAACA
//
