ID A0A387BEY2_9LACT Unreviewed; 383 AA.
AC A0A387BEY2;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Hydroxymethylglutaryl-CoA synthase {ECO:0000313|EMBL:AYG00632.1};
DE EC=2.3.3.10 {ECO:0000313|EMBL:AYG00632.1};
GN ORFNames=D7I46_05715 {ECO:0000313|EMBL:AYG00632.1};
OS Lactococcus allomyrinae.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=2419773 {ECO:0000313|EMBL:AYG00632.1, ECO:0000313|Proteomes:UP000269374};
RN [1] {ECO:0000313|EMBL:AYG00632.1, ECO:0000313|Proteomes:UP000269374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1JSPR-7 {ECO:0000313|EMBL:AYG00632.1,
RC ECO:0000313|Proteomes:UP000269374};
RA Heo J., Kim S.-J., Kwon S.-W.;
RT "Genome sequencing of strain 1JSPR-7.";
RL Submitted (SEP-2018) 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; CP032627; AYG00632.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A387BEY2; -.
DR KEGG; lact:D7I46_05715; -.
DR OrthoDB; 9769523at2; -.
DR Proteomes; UP000269374; Chromosome.
DR GO; GO:0004421; F:hydroxymethylglutaryl-CoA synthase activity; IEA:UniProtKB-EC.
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:AYG00632.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000269374};
KW Transferase {ECO:0000313|EMBL:AYG00632.1}.
FT DOMAIN 2..164
FT /note="Hydroxymethylglutaryl-coenzyme A synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF01154"
FT DOMAIN 180..244
FT /note="Hydroxymethylglutaryl-coenzyme A synthase C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08540"
FT DOMAIN 263..365
FT /note="Hydroxymethylglutaryl-coenzyme A synthase C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08540"
FT ACT_SITE 79
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR611554-1"
FT ACT_SITE 111
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR611554-1"
FT ACT_SITE 233
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR611554-1"
FT BINDING 29
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR611554-2"
FT BINDING 143
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR611554-2"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR611554-2"
FT BINDING 242
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR611554-2"
FT BINDING 275
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR611554-2"
SQ SEQUENCE 383 AA; 42335 MW; 702956142F1D9B30 CRC64;
MKVGIDKLAF FVPNTYVDMT ELALARGVDP AKFHIGIGQD EMAVNPATQD IITFATNAAA
SILTDEDKKS IDMVIVGTES SVDESKASAV VVHGLLDIQP FARSIEMKEA CYATTAGLAA
ARDHVLLHPE SKVLVIASDI AKYGLNTGGE PTQGGGAVAM LITSEPHLLT LNNDNVALSQ
DIYDFWRPFG QAYPSVDGKF SNETYINAFA KVWDEYTSRT SLTFEDFKAV AFHTPYTKMG
KKALLPKLES ESPKNADDLM KQFEYGIAYN RRVGNLYTGS LYLSLISLLE NSPDLSAGDK
IGLFSYGSGT VAEFFSGELV DGFEKYLRTK DHQALLDGRS KLTISEYETM FNEKLDLNHH
AEYHDEMPFS ISEIRDNHRL YKK
//
