ID A0A0J5GG19_9NEIS Unreviewed; 297 AA.
AC A0A0J5GG19;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=hydroxymethylglutaryl-CoA lyase {ECO:0000256|ARBA:ARBA00012910};
DE EC=4.1.3.4 {ECO:0000256|ARBA:ARBA00012910};
GN ORFNames=ACG97_09065 {ECO:0000313|EMBL:KMJ53267.1};
OS Vogesella sp. EB.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Chromobacteriaceae; Vogesella.
OX NCBI_TaxID=1526735 {ECO:0000313|EMBL:KMJ53267.1, ECO:0000313|Proteomes:UP000054352};
RN [1] {ECO:0000313|EMBL:KMJ53267.1, ECO:0000313|Proteomes:UP000054352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EB {ECO:0000313|EMBL:KMJ53267.1,
RC ECO:0000313|Proteomes:UP000054352};
RA Arrua Day P., Revale S., Alvarez H.M.;
RT "Genome wide analysis of metabolism in the polyhydroxybutyrate-producing
RT Vogesella sp. strain EB.";
RL Submitted (JUN-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:KMJ53267.1}.
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DR EMBL; LFDT01000012; KMJ53267.1; -; Genomic_DNA.
DR RefSeq; WP_047967034.1; NZ_LFDT01000012.1.
DR AlphaFoldDB; A0A0J5GG19; -.
DR STRING; 1526735.ACG97_09065; -.
DR PATRIC; fig|1526735.3.peg.1944; -.
DR OrthoDB; 9784013at2; -.
DR UniPathway; UPA00896; UER00863.
DR Proteomes; UP000054352; 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:KMJ53267.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000054352}.
FT DOMAIN 4..271
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 297 AA; 31467 MW; 8D613491D23A39FF CRC64;
MTHVKIVEVG PRDGLQNEKH SISLATKLEL IERLAAAGLR TIEAGAFVSP KWVPQMADSL
QVLQALNLNA GIDYPVLVPN DKGLDAALEA GVREIAVFGA ASEAFSHKNI NASIAESLLR
FESVMKRAQA ANIKVRGYVS CVLGCPYEGD IAPYKVAEVA RALYNMGCYE ISLGDTIGVG
TPNKVTAMLD AVTEVVPVTK LAGHFHDTYG MAIANIHTAL QAGVRTFDSS VAGLGGCPYA
KGASGNVATE DVVYLLHGLG YHTGVDLEQL ADTAWFIAEA LVREPGSKYA KARGLRS
//