ID A0A239SRW1_9STRE Unreviewed; 382 AA.
AC A0A239SRW1;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=3-hydroxy-3-methylglutaryl CoA synthase {ECO:0000313|EMBL:SNU88096.1};
DE EC=2.3.3.- {ECO:0000313|EMBL:SNU88096.1};
GN Name=pksG {ECO:0000313|EMBL:SNU88096.1};
GN ORFNames=SAMEA4412692_00894 {ECO:0000313|EMBL:SNU88096.1};
OS Streptococcus merionis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=400065 {ECO:0000313|EMBL:SNU88096.1, ECO:0000313|Proteomes:UP000215185};
RN [1] {ECO:0000313|EMBL:SNU88096.1, ECO:0000313|Proteomes:UP000215185}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC13788 {ECO:0000313|EMBL:SNU88096.1,
RC ECO:0000313|Proteomes:UP000215185};
RG Pathogen Informatics;
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. HMG-CoA synthase
CC family. {ECO:0000256|ARBA:ARBA00007061}.
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DR EMBL; LT906439; SNU88096.1; -; Genomic_DNA.
DR RefSeq; WP_018372797.1; NZ_LT906439.1.
DR AlphaFoldDB; A0A239SRW1; -.
DR STRING; 1123308.GCA_000380085_00235; -.
DR KEGG; smen:SAMEA4412692_0894; -.
DR eggNOG; COG3425; Bacteria.
DR OrthoDB; 9769523at2; -.
DR Proteomes; UP000215185; Chromosome 1.
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; -; 2.
DR InterPro; IPR013746; HMG_CoA_synt_C_dom.
DR InterPro; IPR013528; HMG_CoA_synth_N.
DR InterPro; IPR011554; HMG_CoA_synthase_prok.
DR InterPro; IPR016039; Thiolase-like.
DR NCBIfam; TIGR01835; HMG-CoA-S_prok; 1.
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:SNU88096.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000215185};
KW Transferase {ECO:0000313|EMBL:SNU88096.1}.
FT DOMAIN 3..165
FT /note="Hydroxymethylglutaryl-coenzyme A synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF01154"
FT DOMAIN 182..247
FT /note="Hydroxymethylglutaryl-coenzyme A synthase C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08540"
FT DOMAIN 253..343
FT /note="Hydroxymethylglutaryl-coenzyme A synthase C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08540"
FT ACT_SITE 80
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR611554-1"
FT ACT_SITE 112
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR611554-1"
FT ACT_SITE 234
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR611554-1"
FT BINDING 30
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR611554-2"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR611554-2"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR611554-2"
FT BINDING 243
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR611554-2"
FT BINDING 270
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR611554-2"
SQ SEQUENCE 382 AA; 42615 MW; 90A7EEBB59317247 CRC64;
MTKIGIDKIG LALPNYVLDL KDLAAARGID PNKYTIGLMQ EAMAITPVTQ DIVTLGAQAA
AQILTEEDKA TIDMVIVGTE TGIDQSKATA VYIHGLLGIQ PFARAIELKE ACYSAAAGLE
FARNHIANRP EAKVLVIASD IAKYGLNSGG EPTQGAGAVA MLVSANPRIL ELNWDNVYQT
RDVMDFWRPN YSPYPKVDGR FSTEQYTDCL QTTFEHYRLQ SGKELDDFAA VCLHIPFAKQ
GLKGLRALQP SPKHEERFFE AIRYNQQVGN IYTGSLFLSL LSLLEQSKAL KAGDDILLYS
YGSGAVCELF SARLVSGYRD QLMTDRFEQM SKRQRLSMEQ YEELFFETIP IDEMGNSPEL
PEDNSPFVLT KIENHQRIYH KH
//
