ID   HMGCL_PSEMV             Reviewed;         301 AA.
AC   P13703;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Hydroxymethylglutaryl-CoA lyase;
DE            Short=HL;
DE            Short=HMG-CoA lyase;
DE            EC=4.1.3.4;
DE   AltName: Full=3-hydroxy-3-methylglutarate-CoA lyase;
GN   Name=mvaB;
OS   Pseudomonas mevalonii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales.
OX   NCBI_TaxID=32044;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2687236; DOI=10.1128/jb.171.12.6468-6472.1989;
RA   Anderson D.H., Rodwell V.W.;
RT   "Nucleotide sequence and expression in Escherichia coli of the 3-hydroxy-3-
RT   methylglutaryl coenzyme A lyase gene of Pseudomonas mevalonii.";
RL   J. Bacteriol. 171:6468-6472(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2656635; DOI=10.1128/jb.171.6.2994-3001.1989;
RA   Beach M.J., Rodwell V.W.;
RT   "Cloning, sequencing, and overexpression of mvaA, which encodes Pseudomonas
RT   mevalonii 3-hydroxy-3-methylglutaryl coenzyme A reductase.";
RL   J. Bacteriol. 171:2994-3001(1989).
RN   [3]
RP   ACTIVE SITE.
RX   PubMed=1637819; DOI=10.1021/bi00144a026;
RA   Hruz P.W., Narasimhan C., Miziorko H.M.;
RT   "3-hydroxy-3-methylglutaryl coenzyme A lyase: affinity labeling of the
RT   Pseudomonas mevalonii enzyme and assignment of cysteine-237 to the active
RT   site.";
RL   Biochemistry 31:6842-6847(1992).
CC   -!- FUNCTION: Involved in the catabolism of branched amino acids such as
CC       leucine. {ECO:0000305}.
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; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10115};
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.
CC   -!- SIMILARITY: Belongs to the HMG-CoA lyase family. {ECO:0000305}.
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DR   EMBL; M24016; AAA25896.1; -; Genomic_DNA.
DR   EMBL; M31807; AAA25895.1; -; Genomic_DNA.
DR   AlphaFoldDB; P13703; -.
DR   SMR; P13703; -.
DR   BioCyc; MetaCyc:MON-11828; -.
DR   UniPathway; UPA00896; UER00863.
DR   GO; GO:0004419; F:hydroxymethylglutaryl-CoA lyase activity; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; ISS:UniProtKB.
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   3: Inferred from homology;
KW   Lyase; Metal-binding.
FT   CHAIN           1..301
FT                   /note="Hydroxymethylglutaryl-CoA lyase"
FT                   /id="PRO_0000151521"
FT   DOMAIN          4..271
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
FT   ACT_SITE        237
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10115,
FT                   ECO:0000269|PubMed:1637819"
FT   BINDING         12
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         13
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         204
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         206
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         246
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   301 AA;  31609 MW;  C796EE24C9BC830A CRC64;
     MQAVKVFEVG PRDGLQNERQ PLSVAARVGL IGELAGTGLR HIEAGAFVSP RWVPQMAGSD
     EVLRQLPSND GVSYTALVPN RQGFEAAQRA GCREVAVFAA ASEAFSRNNI NCSIDESFER
     FTPVLRAANE ASIRVRGYVS CVLGCPFSGA VAPEAVAKVA RRLYELGCYE ISLGDTIGAG
     RPDETAQLFE LCARQLPVAA LAGHFHDTWG MAIANVHAAL AQGVRTFDSS VAGLGGCPYS
     PGASGNVATE DLLYLLHGLG YSTGVDLEAV AQVGVRISAQ LGTANRSRAG LALAARSARE
     H