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Database: UniProt
Entry: R2Q161_9ENTE
LinkDB: R2Q161_9ENTE
Original site: R2Q161_9ENTE 
ID   R2Q161_9ENTE            Unreviewed;       817 AA.
AC   R2Q161;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=Acetyl-CoA acetyltransferase {ECO:0000256|ARBA:ARBA00044137};
DE            EC=2.3.1.9 {ECO:0000256|ARBA:ARBA00012705};
DE   AltName: Full=Acetoacetyl-CoA thiolase {ECO:0000256|ARBA:ARBA00030755};
GN   ORFNames=UAS_00622 {ECO:0000313|EMBL:EOH89083.1};
OS   Enterococcus asini ATCC 700915.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=1158606 {ECO:0000313|EMBL:EOH89083.1, ECO:0000313|Proteomes:UP000013777};
RN   [1] {ECO:0000313|EMBL:EOH89083.1, ECO:0000313|Proteomes:UP000013777}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700915 {ECO:0000313|EMBL:EOH89083.1,
RC   ECO:0000313|Proteomes:UP000013777};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A.M., Gilmore M.S., Lebreton F., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
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 Enterococcus asini ATCC_700915.";
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the HMG-CoA reductase family.
CC       {ECO:0000256|ARBA:ARBA00007661}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC       {ECO:0000256|ARBA:ARBA00010982}.
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:EOH89083.1}.
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DR   EMBL; AJAP01000007; EOH89083.1; -; Genomic_DNA.
DR   AlphaFoldDB; R2Q161; -.
DR   STRING; 57732.RU94_GL001632; -.
DR   PATRIC; fig|1158606.3.peg.581; -.
DR   eggNOG; COG0183; Bacteria.
DR   eggNOG; COG1257; Bacteria.
DR   HOGENOM; CLU_017993_1_0_9; -.
DR   Proteomes; UP000013777; Unassembled WGS sequence.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   GO; GO:0004420; F:hydroxymethylglutaryl-CoA reductase (NADPH) activity; IEA:InterPro.
DR   GO; GO:0015936; P:coenzyme A metabolic process; IEA:InterPro.
DR   CDD; cd00644; HMG-CoA_reductase_classII; 1.
DR   CDD; cd00751; thiolase; 1.
DR   Gene3D; 1.10.8.660; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 3.30.70.420; Hydroxymethylglutaryl-CoA reductase, class I/II, NAD/NADP-binding domain; 1.
DR   InterPro; IPR002202; HMG_CoA_Rdtase.
DR   InterPro; IPR004553; HMG_CoA_Rdtase_bac-typ.
DR   InterPro; IPR023074; HMG_CoA_Rdtase_cat_sf.
DR   InterPro; IPR023076; HMG_CoA_Rdtase_CS.
DR   InterPro; IPR009023; HMG_CoA_Rdtase_NAD(P)-bd_sf.
DR   InterPro; IPR009029; HMG_CoA_Rdtase_sub-bd_dom_sf.
DR   InterPro; IPR002155; Thiolase.
DR   InterPro; IPR016039; Thiolase-like.
DR   InterPro; IPR020615; Thiolase_acyl_enz_int_AS.
DR   InterPro; IPR020610; Thiolase_AS.
DR   InterPro; IPR020617; Thiolase_C.
DR   InterPro; IPR020616; Thiolase_N.
DR   NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR   NCBIfam; TIGR00532; HMG_CoA_R_NAD; 1.
DR   PANTHER; PTHR18919; ACETYL-COA C-ACYLTRANSFERASE; 1.
DR   PANTHER; PTHR18919:SF153; TRIFUNCTIONAL ENZYME SUBUNIT BETA, MITOCHONDRIAL; 1.
DR   Pfam; PF00368; HMG-CoA_red; 1.
DR   Pfam; PF02803; Thiolase_C; 1.
DR   Pfam; PF00108; Thiolase_N; 1.
DR   PRINTS; PR00071; HMGCOARDTASE.
DR   SUPFAM; SSF55035; NAD-binding domain of HMG-CoA reductase; 1.
DR   SUPFAM; SSF56542; Substrate-binding domain of HMG-CoA reductase; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 2.
DR   PROSITE; PS00318; HMG_COA_REDUCTASE_2; 1.
DR   PROSITE; PS50065; HMG_COA_REDUCTASE_4; 1.
DR   PROSITE; PS00098; THIOLASE_1; 1.
DR   PROSITE; PS00099; THIOLASE_3; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013777};
KW   Transferase {ECO:0000313|EMBL:EOH89083.1}.
FT   DOMAIN          20..271
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          281..401
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
SQ   SEQUENCE   817 AA;  86699 MW;  EDFE28B267D4BE9E CRC64;
     MFFISIMVYC KMEVANLKEV VIIDGLRTPI GKYKGMLKDL SAVELGSAVT KALLTKYPEA
     KADVTQVIFG NVLQAGTGQN PARQIALKSG LDYAVTAATI NEVCGSGMKA VLMARQAIQL
     GEAEVVLAGG IESMTRAPGV ATFDYDTKTY GAPLASMIID GLTDAQSGEH MGLTAENVAE
     RYQVSRKEQD AFALASQQKA AQARSQGLFK NEILPLQVGE HLLTEDEGIR GNSTLEKLAT
     LRPAFKEGGT VTAGNASTIN DGAAALLLAS KDYAEAHSIP YLAIVKETAE VGIDPAIMGI
     SPITAIRQLV EKSGVSLDDI DLYEINEAFA ASSIVVEQEL GLPKEKVNIY GGGISLGHAI
     GATGARLLTT LSHQLQDKDK RYGIASLCIG GGLGMAVLLE RPQPTKAKRF YELTAEERLQ
     KLVADGAITP EVYATFKDTA LDSEISSHLI ENAISEVEIP LGVAQHLEVN GRKYLVPVAT
     EEPSVIAALS NGAKIAGNFT SRILSRLMRG QIVFYDVPNQ EALIDWLKAQ EAHFFAVAKE
     AHPSIYRRGG GLREIHTRKV GEDFVSCDFL VDVQEAMGAN IVNTILEAVA SEIRSLRVEP
     ILFAILSNLT TESLVTTSCR IPVTRLGAKN GSEIAAKIAQ AATYAQLDPY RAATHNKGIM
     NGIDGILLAT GNDTRAQAAA IHAYAASQGQ YQGLSQWQVV GDELVGELTL PLAVGTVGGG
     TRVLPKAQAA MALLNVSGAA ELAQVIVSAG LAQNLAALKA LVGEGIQRGH MALQARSLAM
     TVGAKGAEIP ELSRQLKKAP HMNEETAKEL LAKMRQS
//
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