ID A0A2S5SSI4_9BURK Unreviewed; 306 AA.
AC A0A2S5SSI4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=hydroxymethylglutaryl-CoA lyase {ECO:0000256|ARBA:ARBA00012910};
DE EC=4.1.3.4 {ECO:0000256|ARBA:ARBA00012910};
GN ORFNames=C1704_12260 {ECO:0000313|EMBL:PPE65691.1};
OS Caldimonas caldifontis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Caldimonas.
OX NCBI_TaxID=1452508 {ECO:0000313|EMBL:PPE65691.1, ECO:0000313|Proteomes:UP000238605};
RN [1] {ECO:0000313|EMBL:PPE65691.1, ECO:0000313|Proteomes:UP000238605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCRC 80649 {ECO:0000313|EMBL:PPE65691.1,
RC ECO:0000313|Proteomes:UP000238605};
RA Tang B.;
RT "Reclassifiation of [Polyangium] brachysporum DSM 7029 as Guopingzhaonella
RT breviflexa gen. nov., sp. nov., a member of the family Comamonadaceae.";
RL Submitted (FEB-2018) 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:PPE65691.1}.
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DR EMBL; PSNX01000011; PPE65691.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S5SSI4; -.
DR OrthoDB; 9784013at2; -.
DR UniPathway; UPA00896; UER00863.
DR Proteomes; UP000238605; 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:PPE65691.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000238605}.
FT DOMAIN 6..273
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 306 AA; 32823 MW; AEBEF1C79801067C CRC64;
MFPDQVTLVD VGPRDGLQNE KQPVSAAHKI ELVHRLQAAG LREIEVTSFV SPKWVPQMAD
NAEVMVGLKR KPGVRYSVLV PNMKGLEAAL PTRPDEIVVF GAASEAFSQR NINCSIEESI
ERFRPVAAAA REQGLKVRGA ISCAVGCPYQ GEVSADEVER VVRLMKDIGV QHVGVADTIG
VGTPLKVRAA MERALRHYPL HEVSGHFHDT YGQAVGNIYA CLEMGIHHFD TSVAGLGGCP
YAKGATGNVA TEDVVFLLQG LGIDCGVDLD ALVDAGDFIS RVLGRKPVSR AANALLAKRV
REEAPA
//
