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Database: UniProt
Entry: A0A2E7NXR3_9BURK
LinkDB: A0A2E7NXR3_9BURK
Original site: A0A2E7NXR3_9BURK 
ID   A0A2E7NXR3_9BURK        Unreviewed;       302 AA.
AC   A0A2E7NXR3;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=hydroxymethylglutaryl-CoA lyase {ECO:0000256|ARBA:ARBA00012910};
DE            EC=4.1.3.4 {ECO:0000256|ARBA:ARBA00012910};
GN   ORFNames=CME87_02155 {ECO:0000313|EMBL:MBO14266.1};
OS   Herbaspirillum sp.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Herbaspirillum.
OX   NCBI_TaxID=1890675 {ECO:0000313|EMBL:MBO14266.1, ECO:0000313|Proteomes:UP000226028};
RN   [1] {ECO:0000313|Proteomes:UP000226028}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Tully B.J., Graham E.D., Heidelberg J.F.;
RT   "The Reconstruction of 2,631 Draft Metagenome-Assembled Genomes from the
RT   Global Oceans.";
RL   Submitted (SEP-2017) 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:MBO14266.1}.
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DR   EMBL; PBPP01000020; MBO14266.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2E7NXR3; -.
DR   UniPathway; UPA00896; UER00863.
DR   Proteomes; UP000226028; 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:MBO14266.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          7..274
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
SQ   SEQUENCE   302 AA;  32038 MW;  A574510494B0886E CRC64;
     MSLPKKVKIV EVGPRDGLQN EKETISAEVK IELVNRLSAA GFPNVEAASF VSPKWVPQMA
     TSSEVMHGIT RKPGVVYSAL VPNMKGFEAA LEAGVDEVVI FGAASEAFSQ KNINCSIAES
     IERFAEVAKA AKDHRKRLRA AVSCAFGCPY QGEVPLDAVA DVVRRFRELG CDEIDIADTI
     GVATPGKVRP VMETAIREFH IEGLSGHFHD TYGQALANIY ASLQTGISIY HASVAGLGGC
     PYAKGATGNV ATEDVLYMMN GLGIETGIDL DAVAEAGQFI SQQLGRKSVS RVGNALAAKR
     VG
//
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