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Database: UniProt
Entry: A0A0W0Y539_9GAMM
LinkDB: A0A0W0Y539_9GAMM
Original site: A0A0W0Y539_9GAMM 
ID   A0A0W0Y539_9GAMM        Unreviewed;       365 AA.
AC   A0A0W0Y539;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Polyketide biosynthesis 3-hydroxy-3-methylglutaryl-ACP synthase PksG {ECO:0000313|EMBL:KTD51619.1};
DE            EC=2.3.3.- {ECO:0000313|EMBL:KTD51619.1};
GN   Name=pksG {ECO:0000313|EMBL:KTD51619.1};
GN   ORFNames=Lqui_0463 {ECO:0000313|EMBL:KTD51619.1};
OS   Legionella quinlivanii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=45073 {ECO:0000313|EMBL:KTD51619.1, ECO:0000313|Proteomes:UP000054618};
RN   [1] {ECO:0000313|EMBL:KTD51619.1, ECO:0000313|Proteomes:UP000054618}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC#1442-AUS-E {ECO:0000313|EMBL:KTD51619.1,
RC   ECO:0000313|Proteomes:UP000054618};
RA   Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA   Pupko T., Shuman H.A., Segal G.;
RT   "Genomic analysis of 38 Legionella species identifies large and diverse
RT   effector repertoires.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. HMG-CoA synthase
CC       family. {ECO:0000256|ARBA:ARBA00007061}.
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:KTD51619.1}.
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DR   EMBL; LNYS01000006; KTD51619.1; -; Genomic_DNA.
DR   RefSeq; WP_058506586.1; NZ_UGOX01000001.1.
DR   AlphaFoldDB; A0A0W0Y539; -.
DR   STRING; 45073.Lqui_0463; -.
DR   PATRIC; fig|45073.5.peg.492; -.
DR   OrthoDB; 9769523at2; -.
DR   Proteomes; UP000054618; Unassembled WGS sequence.
DR   GO; GO:0004421; F:hydroxymethylglutaryl-CoA synthase activity; IEA:InterPro.
DR   GO; GO:0006084; P:acetyl-CoA metabolic process; IEA:InterPro.
DR   GO; GO:0010142; P:farnesyl diphosphate biosynthetic process, mevalonate pathway; IEA:InterPro.
DR   CDD; cd00827; init_cond_enzymes; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   InterPro; IPR013746; HMG_CoA_synt_C_dom.
DR   InterPro; IPR013528; HMG_CoA_synth_N.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR43323; 3-HYDROXY-3-METHYLGLUTARYL COENZYME A SYNTHASE; 1.
DR   PANTHER; PTHR43323:SF2; HYDROXYMETHYLGLUTARYL-COA SYNTHASE; 1.
DR   Pfam; PF08540; HMG_CoA_synt_C; 2.
DR   Pfam; PF01154; HMG_CoA_synt_N; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 2.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000313|EMBL:KTD51619.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054618};
KW   Transferase {ECO:0000313|EMBL:KTD51619.1}.
FT   DOMAIN          4..171
FT                   /note="Hydroxymethylglutaryl-coenzyme A synthase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01154"
FT   DOMAIN          183..253
FT                   /note="Hydroxymethylglutaryl-coenzyme A synthase C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08540"
FT   DOMAIN          267..358
FT                   /note="Hydroxymethylglutaryl-coenzyme A synthase C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08540"
SQ   SEQUENCE   365 AA;  40355 MW;  F0E66F933A93B561 CRC64;
     MSSSVGITSI GISFPPFYMH LNELARLRGV EAEKYTKGLG LNEMALCGNQ YTVIDLAIQA
     AQDAIKRWGG SVEDIGLIAV GTETPVDYSR PLSAWVASEL KIQGYVRSYE VKHACYGGTL
     ALLQAAEWYQ ANPDKQKVAL VIAVDEALYA QNDPGEPTQG AGAVAFIVGP ANLATINVGH
     TIAYSEPVFD FWKPLDKHYP EVNGQFSLEC YKQAAVSCYK KMVKDENPVD FLNRYSALCF
     HVPFPKMVYK AFNAVGESLG FDAAQINELY EQRVNPFMTW NQRCGNAYTA SLWIMFAYAL
     AHTPPDSRLL LFSYGSGMGS ELIECVNNSD DGYREWAAKV EEQLNQRQAL AAKDYAAIRE
     TKPAE
//
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