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Database: UniProt
Entry: O51626_BORBU
LinkDB: O51626_BORBU
Original site: O51626_BORBU 
ID   O51626_BORBU            Unreviewed;       407 AA.
AC   O51626;
DT   01-JUN-1998, integrated into UniProtKB/TrEMBL.
DT   01-JUN-1998, sequence version 1.
DT   08-NOV-2023, entry version 119.
DE   SubName: Full=Hydroxymethylglutaryl-CoA synthase {ECO:0000313|EMBL:AAC67034.1};
DE            EC=2.3.3.10 {ECO:0000313|EMBL:AAC67034.1};
GN   OrderedLocusNames=BB_0683 {ECO:0000313|EMBL:AAC67034.1};
OS   Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS   (Borrelia burgdorferi).
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Borreliaceae;
OC   Borreliella.
OX   NCBI_TaxID=224326 {ECO:0000313|EMBL:AAC67034.1, ECO:0000313|Proteomes:UP000001807};
RN   [1] {ECO:0000313|EMBL:AAC67034.1, ECO:0000313|Proteomes:UP000001807}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35210 / B31 / CIP 102532 / DSM 4680
RC   {ECO:0000313|Proteomes:UP000001807};
RX   PubMed=9403685; DOI=10.1038/37551;
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R., Lathigra R.,
RA   White O., Ketchum K.A., Dodson R., Hickey E.K., Gwinn M., Dougherty B.,
RA   Tomb J.F., Fleischmann R.D., Richardson D., Peterson J., Kerlavage A.R.,
RA   Quackenbush J., Salzberg S., Hanson M., van Vugt R., Palmer N., Adams M.D.,
RA   Gocayne J., Weidman J., Utterback T., Watthey L., McDonald L., Artiach P.,
RA   Bowman C., Garland S., Fuji C., Cotton M.D., Horst K., Roberts K.,
RA   Hatch B., Smith H.O., Venter J.C.;
RT   "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL   Nature 390:580-586(1997).
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. HMG-CoA synthase
CC       family. {ECO:0000256|ARBA:ARBA00007061}.
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DR   EMBL; AE000783; AAC67034.1; -; Genomic_DNA.
DR   PIR; B70185; B70185.
DR   RefSeq; NP_212817.1; NC_001318.1.
DR   RefSeq; WP_010889798.1; NC_001318.1.
DR   AlphaFoldDB; O51626; -.
DR   STRING; 224326.BB_0683; -.
DR   PaxDb; 224326-BB_0683; -.
DR   EnsemblBacteria; AAC67034; AAC67034; BB_0683.
DR   KEGG; bbu:BB_0683; -.
DR   PATRIC; fig|224326.49.peg.1074; -.
DR   HOGENOM; CLU_008065_3_0_12; -.
DR   OMA; DDAYNWI; -.
DR   OrthoDB; 9769523at2; -.
DR   BRENDA; 2.3.3.10; 902.
DR   Proteomes; UP000001807; 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; -; 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; 3-HYDROXY-3-METHYLGLUTARYL COENZYME A SYNTHASE; 1.
DR   Pfam; PF08540; HMG_CoA_synt_C; 1.
DR   Pfam; PF01154; HMG_CoA_synt_N; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 2.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000313|EMBL:AAC67034.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001807};
KW   Transferase {ECO:0000313|EMBL:AAC67034.1}.
FT   DOMAIN          3..180
FT                   /note="Hydroxymethylglutaryl-coenzyme A synthase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01154"
FT   DOMAIN          295..379
FT                   /note="Hydroxymethylglutaryl-coenzyme A synthase C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08540"
FT   ACT_SITE        89
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611554-1"
FT   ACT_SITE        126
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611554-1"
FT   ACT_SITE        253
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611554-1"
FT   BINDING         159
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611554-2"
FT   BINDING         300
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611554-2"
SQ   SEQUENCE   407 AA;  46029 MW;  71ED5F0C0BB5D860 CRC64;
     MRIGISDIRI FLPLNYLDFS VLLENPLYFS NEVFFKKINR AIDATLQKGF RFTSPNEDSV
     TMASSAVKLI FDNNNLDLSK IRILLGGTET GVDHSKAISS YVFGALKQSG ICLGNNFLTF
     QVQHACAGAA MSLHTVASVL SHSNNSEYGI VFSSDIAHYS NLTTAEITQG AGATAILIEK
     NPKLLSINLS EFGVYTDDVD DFFRPFGSVE AKVRGQYSVE CYNNANENAL RDFAFKKQLS
     MKDLFSNYRF VLHVPFAKMP IDSMHYILKK YYSDDESVRN AYLESIDFYD GVEAAMEVGN
     LYTGSIFLSL AFYLKRVFSK KDITGEKILF CSYGSGNIMI IYELTIEKSA FDVIKLWDLE
     GLIKNRNNAN FEEYKDFFQN KIIPGESRGF YLKELRNDGY RVYGYRA
//
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