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Database: UniProt
Entry: A0A0N1LMP3_9PROT
LinkDB: A0A0N1LMP3_9PROT
Original site: A0A0N1LMP3_9PROT 
ID   A0A0N1LMP3_9PROT        Unreviewed;       312 AA.
AC   A0A0N1LMP3;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=3-hydroxy-3-methylglutaryl-CoA lyase {ECO:0000313|EMBL:KPF87342.1};
GN   ORFNames=IP70_03975 {ECO:0000313|EMBL:KPF87342.1};
OS   alpha proteobacterium AAP38.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria.
OX   NCBI_TaxID=1523418 {ECO:0000313|EMBL:KPF87342.1, ECO:0000313|Proteomes:UP000037884};
RN   [1] {ECO:0000313|EMBL:KPF87342.1, ECO:0000313|Proteomes:UP000037884}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AAP38 {ECO:0000313|EMBL:KPF87342.1,
RC   ECO:0000313|Proteomes:UP000037884};
RA   Zeng Y., Feng F., Liu Y., Koblizek M.;
RT   "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT   Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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:KPF87342.1}.
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DR   EMBL; LJHR01000005; KPF87342.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N1LMP3; -.
DR   STRING; 1523418.IP70_03975; -.
DR   PATRIC; fig|1523418.3.peg.3873; -.
DR   OrthoDB; 9784013at2; -.
DR   Proteomes; UP000037884; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016833; F:oxo-acid-lyase activity; IEA:InterPro.
DR   CDD; cd07938; DRE_TIM_HMGL; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
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; PS50991; PYR_CT; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:KPF87342.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          6..278
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
SQ   SEQUENCE   312 AA;  32163 MW;  F06FAF1A3D4DC3E6 CRC64;
     MTGTFIEISE VGPRDGLQSI SPIMPTEAKK AWIAAEAAAG VREIEVGSFV PAKILPQLAD
     TAELVSFART IPGLTVAVLV PNLKGAEAAV AAGAHKITIP LSVSETHSLR NVRRTHAQML
     EETAAIAALI KAQPQGGRPK FEGGLSTAFG CTLEGVVPEA KVLEIAEALM KAGCDEVGLS
     DTTGYANPAQ VKRLIRAVRG VVGHHACSGV HLHNTRGLGL ANALAALDEG ITTLDASLGG
     IGGCPFAPGA SGNIVTEDLA FMLAAMGYET GVDLERLLAV RDIVKSALPD TEMYGFTPDA
     GLPKGFQGAW GV
//
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