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Database: UniProt
Entry: A0A0P7EB48_9GAMM
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Original site: A0A0P7EB48_9GAMM 
ID   A0A0P7EB48_9GAMM        Unreviewed;       308 AA.
AC   A0A0P7EB48;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=hydroxymethylglutaryl-CoA lyase {ECO:0000256|ARBA:ARBA00012910};
DE            EC=4.1.3.4 {ECO:0000256|ARBA:ARBA00012910};
GN   ORFNames=AOG28_04785 {ECO:0000313|EMBL:KPM80909.1};
OS   Cobetia sp. UCD-24C.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Cobetia.
OX   NCBI_TaxID=1716176 {ECO:0000313|EMBL:KPM80909.1, ECO:0000313|Proteomes:UP000050261};
RN   [1] {ECO:0000313|EMBL:KPM80909.1, ECO:0000313|Proteomes:UP000050261}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCD-24C {ECO:0000313|EMBL:KPM80909.1,
RC   ECO:0000313|Proteomes:UP000050261};
RA   Krusor M., Coil D.A., Lang J.M., Eisen J.A., Alexiev A.;
RT   "Draft Genome of Cobetia sp. UCD-24C.";
RL   Submitted (SEP-2015) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KPM80909.1}.
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DR   EMBL; LJTD01000003; KPM80909.1; -; Genomic_DNA.
DR   RefSeq; WP_054555516.1; NZ_LJTD01000003.1.
DR   AlphaFoldDB; A0A0P7EB48; -.
DR   STRING; 1716176.AOG28_04785; -.
DR   PATRIC; fig|1716176.3.peg.1631; -.
DR   UniPathway; UPA00896; UER00863.
DR   Proteomes; UP000050261; Unassembled WGS sequence.
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:KPM80909.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050261}.
FT   DOMAIN          7..282
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
SQ   SEQUENCE   308 AA;  32537 MW;  FF464EFEC475AC32 CRC64;
     MHFPRKVRIV EVGARDGLQN ESVPVATATK LELIRRLSDS GLAHVEAASF VSPRWVPQMA
     DHREIMLALR DGHANSTTAK SATTYSALTP NMKGLEAALE CGVREVAVFG SASESFSQRN
     INCSIAESLA RFAPVVEHSL KAGVRVRGYV SCVLGCPYEG QIAPAEVAAV ARELKAMGCY
     EVSLGDTIGV GTPLKAKHML EQVSREVPIT QLAAHFHDTY GQALANLYAV LEEGIAVIDS
     SVAGLGGCPY AKGASGNVAS EDVLYLLEGM GIETGVDLAA LARTGDWISR ELGRPNGSRV
     GQALMASC
//
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