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Database: UniProt
Entry: A0A429ZXT7_9ENTE
LinkDB: A0A429ZXT7_9ENTE
Original site: A0A429ZXT7_9ENTE 
ID   A0A429ZXT7_9ENTE        Unreviewed;       387 AA.
AC   A0A429ZXT7;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Hydroxymethylglutaryl-CoA synthase {ECO:0000313|EMBL:RST98714.1};
GN   ORFNames=CBF37_06600 {ECO:0000313|EMBL:RST98714.1};
OS   Vagococcus vulneris.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae; Vagococcus.
OX   NCBI_TaxID=1977869 {ECO:0000313|EMBL:RST98714.1, ECO:0000313|Proteomes:UP000287857};
RN   [1] {ECO:0000313|EMBL:RST98714.1, ECO:0000313|Proteomes:UP000287857}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS1995 {ECO:0000313|EMBL:RST98714.1,
RC   ECO:0000313|Proteomes:UP000287857};
RA   Gulvik C.A.;
RT   "Vagococcus spp. assemblies.";
RL   Submitted (MAY-2017) 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:RST98714.1}.
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DR   EMBL; NGJS01000008; RST98714.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A429ZXT7; -.
DR   OrthoDB; 9769523at2; -.
DR   Proteomes; UP000287857; 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; -; 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   Reference proteome {ECO:0000313|Proteomes:UP000287857}.
FT   DOMAIN          3..164
FT                   /note="Hydroxymethylglutaryl-coenzyme A synthase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01154"
FT   DOMAIN          177..247
FT                   /note="Hydroxymethylglutaryl-coenzyme A synthase C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08540"
FT   DOMAIN          264..385
FT                   /note="Hydroxymethylglutaryl-coenzyme A synthase C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08540"
FT   ACT_SITE        78
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611554-1"
FT   ACT_SITE        110
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611554-1"
FT   ACT_SITE        232
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611554-1"
FT   BINDING         28
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611554-2"
FT   BINDING         142
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611554-2"
FT   BINDING         147
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611554-2"
FT   BINDING         241
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611554-2"
FT   BINDING         274
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611554-2"
SQ   SEQUENCE   387 AA;  43017 MW;  08A87FAC052D6B95 CRC64;
     MAGIDKISFF TPNTYVNLEK LAIHRGIDPN KFLIGIGQTN MAVPTITQDT VSMGANAALS
     ILSEEDRELI DLVIVGTESG VDQSKSCASF IHDILNIQPF AKSYEIKHAC YGATAGLMSA
     IDYVQNNPDR KALVIGSDIA RYGLNSGGEV TQGAGAVAML ISNNPRILEF DTPSISLTKN
     IFDFWRPNYS DVAFVDGKFS NEAYIEFFNT LWQEFSNKNN LLLEDIDAFC LHMPYTKMGQ
     KALSPLLAEA KTEIRDSLLS QYELSTTYSR QIGNIYTGSL YLSLISLLDQ SSTLVSGDRI
     AFFSYGSGAV AEMFSATLVK DYTDQLLAQH HQTMLNQRTS LTIEQYETIF SQELPKEDGL
     YTFEQELDTA SIYLSAITDH QRIYTKK
//
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