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Database: UniProt
Entry: A0A0N0KAU4_9PROT
LinkDB: A0A0N0KAU4_9PROT
Original site: A0A0N0KAU4_9PROT 
ID   A0A0N0KAU4_9PROT        Unreviewed;       303 AA.
AC   A0A0N0KAU4;
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:KPF87308.1};
GN   ORFNames=IP70_03725 {ECO:0000313|EMBL:KPF87308.1};
OS   alpha proteobacterium AAP38.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria.
OX   NCBI_TaxID=1523418 {ECO:0000313|EMBL:KPF87308.1, ECO:0000313|Proteomes:UP000037884};
RN   [1] {ECO:0000313|EMBL:KPF87308.1, ECO:0000313|Proteomes:UP000037884}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AAP38 {ECO:0000313|EMBL:KPF87308.1,
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:KPF87308.1}.
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DR   EMBL; LJHR01000005; KPF87308.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N0KAU4; -.
DR   STRING; 1523418.IP70_03725; -.
DR   PATRIC; fig|1523418.3.peg.3822; -.
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:KPF87308.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          5..272
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
SQ   SEQUENCE   303 AA;  31339 MW;  2A11672D3F54C640 CRC64;
     MPSQVEIVEV SPRDGLQNEA TPVSTDQKVE LINRAIAAGA KRIEVTSFVN PKRVPQMADA
     EAVLAALPRG NGVSYIGLAM NGRGFDRALA AGVTEVNYVL VASDTFSQRN NGAPTMQTLT
     GWAEVAAAAK AAKLPTSITI GASFGCPFEG EVPVERVVEV AKRAADHGVD EIALADTIGV
     ASPADVVERF AAVSAALPGI RLRAHFHNTR NTGIANAYAA VMAGVGVLDS SLGGIGGCPF
     APAATGNIPT EDLVYMLNRM KIGTGIDLAA AIEAASWLEG IIGRRNQAML GRAGIFPPPA
     KTQ
//
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