ID Q9CFA9_LACLA Unreviewed; 384 AA.
AC Q9CFA9;
DT 01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2001, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE SubName: Full=Hydroxymethylglutaryl-CoA synthase {ECO:0000313|EMBL:AAK05670.1};
DE EC=2.3.3.10 {ECO:0000313|EMBL:AAK05670.1};
GN Name=hmcM {ECO:0000313|EMBL:AAK05670.1};
GN ORFNames=L13187 {ECO:0000313|EMBL:AAK05670.1};
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623 {ECO:0000313|EMBL:AAK05670.1, ECO:0000313|Proteomes:UP000002196};
RN [1] {ECO:0000313|EMBL:AAK05670.1, ECO:0000313|Proteomes:UP000002196}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403 {ECO:0000313|EMBL:AAK05670.1,
RC ECO:0000313|Proteomes:UP000002196};
RX PubMed=11337471; DOI=10.1101/gr.GR-1697R;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. HMG-CoA synthase
CC family. {ECO:0000256|ARBA:ARBA00007061}.
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DR EMBL; AE005176; AAK05670.1; -; Genomic_DNA.
DR PIR; D86821; D86821.
DR RefSeq; NP_267728.1; NC_002662.1.
DR RefSeq; WP_010906037.1; NC_002662.1.
DR AlphaFoldDB; Q9CFA9; -.
DR PaxDb; 272623-L13187; -.
DR EnsemblBacteria; AAK05670; AAK05670; L13187.
DR KEGG; lla:L13187; -.
DR PATRIC; fig|272623.7.peg.1690; -.
DR eggNOG; COG3425; Bacteria.
DR HOGENOM; CLU_008065_3_2_9; -.
DR OrthoDB; 9803760at2; -.
DR Proteomes; UP000002196; 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:AAK05670.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002196};
KW Transferase {ECO:0000313|EMBL:AAK05670.1}.
FT DOMAIN 2..165
FT /note="Hydroxymethylglutaryl-coenzyme A synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF01154"
FT DOMAIN 180..257
FT /note="Hydroxymethylglutaryl-coenzyme A synthase C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08540"
FT DOMAIN 258..368
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 384 AA; 42714 MW; CABCE1B178C87E52 CRC64;
MKVGIDKLGF FVPNTFVDMR DLANARNVDP AKFQIGIGQD EMAVNPATQD IITFAANAAA
SILTEEDKKA IDMIIVGTES SLDESKASAV VVHDLLGIQP FARSIEMKEA CYATTAGLTL
ARDHVLLNPD TKVLVIASDI AKYGLNTGGE PTQGAGSVAM LITADPKILA LNNDNVALTQ
DIYDFWRPFG QAYPSVDGKF SNETYIDAFA KIWKEYSHRT NLKFEDFAAI AFHTPYTKMG
KKALLPMLES EKPANAEELM EQFEHGIVYN RRVGNLYTGS LYLSLISLLE NSDKLSAGQR
IGLFSYGSGT VAEFFSGELV EGYENHLLKI EHQSMLDART RLSIPEYENM FNQYLDLNHN
ISFNDETDYS VSEVVDNHRK YKKR
//
