ID   A4TZG8_9PROT            Unreviewed;       297 AA.
AC   A4TZG8;
DT   15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   15-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=hydroxymethylglutaryl-CoA lyase {ECO:0000256|ARBA:ARBA00012910};
DE            EC=4.1.3.4 {ECO:0000256|ARBA:ARBA00012910};
GN   ORFNames=MGR_1491 {ECO:0000313|EMBL:CAM76025.1};
OS   Magnetospirillum gryphiswaldense.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Magnetospirillum.
OX   NCBI_TaxID=55518 {ECO:0000313|EMBL:CAM76025.1};
RN   [1] {ECO:0000313|EMBL:CAM76025.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=MSR-1 {ECO:0000313|EMBL:CAM76025.1};
RX   PubMed=17449609; DOI=10.1128/JB.00119-07;
RA   Richter M., Kube M., Bazylinski D.A., Lombardot T., Gloeckner F.O.,
RA   Reinhardt R., Schueler D.;
RT   "Comparative genome analysis of four magnetotactic bacteria reveals a
RT   complex set of group-specific genes implicated in magnetosome
RT   biomineralization and function.";
RL   J. Bacteriol. 189:4899-4910(2007).
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; CU459003; CAM76025.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4TZG8; -.
DR   UniPathway; UPA00896; UER00863.
DR   GO; GO:0004419; F:hydroxymethylglutaryl-CoA lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; 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   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Pyruvate {ECO:0000313|EMBL:CAM76025.1};
KW   Transferase {ECO:0000313|EMBL:CAM76025.1}.
FT   DOMAIN          7..274
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
SQ   SEQUENCE   297 AA;  30494 MW;  B21CFE8E5B9C998B CRC64;
     MTIPAYVKIV EVGPRDGLQN EASPVSVQTK IGLIDRLSAA GLPVIESGSF VSPKWVPQMA
     ASAEVLTGIS QKPGVVYPVL TPNMQGLEAA LAAGAREVAV FGAASESFSQ KNINCSIGDS
     LDRFAPVVTR ARDQGVKVRG YVSCVLGCPY EGDINPAAVA DVARRLAEMG CYEISLGDTV
     GVGTPLKAQA MIDAVTAHLP VAMLAAHFHD TYGQALANIL GVLERGVAVV DSSVAGLGGC
     PYAKGAAGNV ASEDVVYMLH GMGIQTGIDL TKLIEAGSFI CDAIGRPTGS KVARALG
//