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Database: UniProt
Entry: A0A2V2PLJ8_9ACTN
LinkDB: A0A2V2PLJ8_9ACTN
Original site: A0A2V2PLJ8_9ACTN 
ID   A0A2V2PLJ8_9ACTN        Unreviewed;       317 AA.
AC   A0A2V2PLJ8;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Hydroxymethylglutaryl-CoA lyase {ECO:0000313|EMBL:PWS40289.1};
GN   ORFNames=DKT74_33710 {ECO:0000313|EMBL:PWS40289.1};
OS   Streptomyces sp. ZEA17I.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2202516 {ECO:0000313|EMBL:PWS40289.1, ECO:0000313|Proteomes:UP000245984};
RN   [1] {ECO:0000313|EMBL:PWS40289.1, ECO:0000313|Proteomes:UP000245984}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZEA17I {ECO:0000313|EMBL:PWS40289.1,
RC   ECO:0000313|Proteomes:UP000245984};
RA   Chen X., Qin K., Li H., Cortesi P., Saracchi M., Sang W., Yang M.;
RT   "Genome sequencing and identification of chitinase family genes of
RT   Streptomyces sp. ZEA17I, a biocontrol agent against plant pathogens.";
RL   Submitted (MAY-2018) 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:PWS40289.1}.
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DR   EMBL; QGMS01001706; PWS40289.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V2PLJ8; -.
DR   Proteomes; UP000245984; 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:PWS40289.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          12..283
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
FT   REGION          296..317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   317 AA;  33228 MW;  2C8D98E3B3FDD786 CRC64;
     MKVPAPGLPA RVRIHEVGAR DGLQNEKETV PTEVKAEFIH RLAAAGLSTI EATSFVHPKW
     VPQLADAEAL FPLLGDIAEA REVALPVLVP NERGLERALA LGARSIAVFG SATETFAARN
     LNRTVDESLA MFEPVVARAK ADQVHVRGYL SMCFGDPWEG AVPVARVVKV AKALMDLGCD
     ELSLGDTIGV ATPGHVRELL TALNDSAVPT SSIGVHFHDT YGQALSNTLA ALQHGVTTVD
     ASAGGLGGCP YAKSATGNLA TEDLVWMLNG LGIETGVDLA SLTATSAWLA EHLGRPSPSR
     TVRALTPPPS SSPTRSE
//
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