ID K1LMW7_9LACT Unreviewed; 405 AA.
AC K1LMW7;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Hydroxymethylglutaryl-CoA synthase {ECO:0000313|EMBL:EKB56081.1};
GN ORFNames=HMPREF9706_00064 {ECO:0000313|EMBL:EKB56081.1};
OS Facklamia hominis CCUG 36813.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Facklamia.
OX NCBI_TaxID=883111 {ECO:0000313|EMBL:EKB56081.1, ECO:0000313|Proteomes:UP000004465};
RN [1] {ECO:0000313|EMBL:EKB56081.1, ECO:0000313|Proteomes:UP000004465}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 36813 {ECO:0000313|EMBL:EKB56081.1,
RC ECO:0000313|Proteomes:UP000004465};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Facklamia hominis CCUG 36813.";
RL Submitted (JUL-2012) 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:EKB56081.1}.
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DR EMBL; AGZD01000001; EKB56081.1; -; Genomic_DNA.
DR RefSeq; WP_006907363.1; NZ_JH932292.1.
DR AlphaFoldDB; K1LMW7; -.
DR STRING; 883111.HMPREF9706_00064; -.
DR PATRIC; fig|883111.3.peg.65; -.
DR HOGENOM; CLU_008065_3_2_9; -.
DR OrthoDB; 9769523at2; -.
DR Proteomes; UP000004465; 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; 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:UP000004465}.
FT DOMAIN 4..166
FT /note="Hydroxymethylglutaryl-coenzyme A synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF01154"
FT DOMAIN 181..261
FT /note="Hydroxymethylglutaryl-coenzyme A synthase C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08540"
FT DOMAIN 278..398
FT /note="Hydroxymethylglutaryl-coenzyme A synthase C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08540"
FT ACT_SITE 81
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR611554-1"
FT ACT_SITE 113
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR611554-1"
FT ACT_SITE 235
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR611554-1"
FT BINDING 31
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR611554-2"
FT BINDING 145
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR611554-2"
FT BINDING 150
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR611554-2"
FT BINDING 244
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR611554-2"
FT BINDING 287
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR611554-2"
SQ SEQUENCE 405 AA; 45301 MW; 9CD14C6320ABB596 CRC64;
MKTKVGIDRI HFYLPPKYVD MGLLAEARGV DPNKYLIGIG QEKMAVTDAT IDIVSMGLNA
AYPIIQEEDK DLIDQVIFAT ESAFDYSKAA ATYLHESLGI HAFAKSYEIK EACYGATAAL
QIACDYVRLR PERKVLVVAS DIARYGLATG GEPTQGAGAI AMLISKNPSV LALEEDSISL
TDNQYDFWRP DYLDYPLVEG KFSTQLYNQC FIKIMEEAAN KHLDLFDTLK GLCFHLPFSK
MGKKALQAYQ DYLNSKEGSL DPKVVLAFNR WLEVYPDLIQ IGKQVGNIYT GSLYLGLISL
LVNGTALNAG DKLGLFSYGS GAVAELLVGQ LQVDYRKALK LEDLNKRLAQ RQELSIEEYE
MIFSEKLPND GKTHLLEPSV LPGDFYLTKI DGHRRYYQQY KTQTD
//
