ID D1AB90_THECD Unreviewed; 386 AA.
AC D1AB90;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:ACY99033.1};
DE EC=2.3.1.16 {ECO:0000313|EMBL:ACY99033.1};
GN OrderedLocusNames=Tcur_3495 {ECO:0000313|EMBL:ACY99033.1};
OS Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 / KCTC
OS 9072 / NBRC 15933 / NCIMB 10081 / Henssen B9).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Thermomonospora.
OX NCBI_TaxID=471852 {ECO:0000313|EMBL:ACY99033.1, ECO:0000313|Proteomes:UP000001918};
RN [1] {ECO:0000313|EMBL:ACY99033.1, ECO:0000313|Proteomes:UP000001918}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19995 / DSM 43183 / JCM 3096 / KCTC 9072 / NBRC 15933 /
RC NCIMB 10081 / Henssen B9 {ECO:0000313|Proteomes:UP000001918};
RX PubMed=21475583; DOI=10.4056/sigs.1453580;
RA Chertkov O., Sikorski J., Nolan M., Lapidus A., Lucas S., Del Rio T.G.,
RA Tice H., Cheng J.F., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA Mavromatis K., Mikhailova N., Ovchinnikova G., Pati A., Chen A.,
RA Palaniappan K., Djao O.D., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Brettin T., Han C., Detter J.C., Rohde M., Goker M., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Thermomonospora curvata type strain (B9).";
RL Stand. Genomic Sci. 1:13-22(2011).
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000256|ARBA:ARBA00010982, ECO:0000256|RuleBase:RU003557}.
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DR EMBL; CP001738; ACY99033.1; -; Genomic_DNA.
DR RefSeq; WP_012853817.1; NC_013510.1.
DR AlphaFoldDB; D1AB90; -.
DR STRING; 471852.Tcur_3495; -.
DR KEGG; tcu:Tcur_3495; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_2_3_11; -.
DR OrthoDB; 3761315at2; -.
DR Proteomes; UP000001918; Chromosome.
DR GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IEA:UniProtKB-EC.
DR CDD; cd00751; thiolase; 1.
DR Gene3D; 3.40.47.10; -; 2.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020610; Thiolase_AS.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR43365; BLR7806 PROTEIN; 1.
DR PANTHER; PTHR43365:SF1; STEROID 3-KETOACYL-COA THIOLASE FADA6; 1.
DR Pfam; PF02803; Thiolase_C; 1.
DR Pfam; PF00108; Thiolase_N; 1.
DR PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW ECO:0000313|EMBL:ACY99033.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001918};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:ACY99033.1}.
FT DOMAIN 5..254
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 264..385
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 89
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 342
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 372
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 386 AA; 39959 MW; 47917CEA8354B54F CRC64;
MPEAVIVEAV RTPVGKRNGV LSGLHPAELL GAAQKGLLDK AGIAPEVIGQ VVGGCVTQAG
EQSNNVTRQA WLHAGLPYQT ACTTIDCACG SSQQAVHMVA GLIASGAIDA GIGCGVESMS
RVFLGQAVTP ETGNPFPDSW SLDMPDQFTA AERIAKRRGI TRQDADAFGL ASQRKAAQAW
AENRFAGQIV EVTAPVMGPE GPTGETAVVT RDQGLRETSM EALAKLKPVI PDGIHTAGNT
SQISDGAAAV LLTTPEKAAE LGLRPRARIV ASGMVGSDPY YHLDGPIDAT RHVLAKAKMT
LDDIDLVEIN EAFASVVLSW AGVLNADMDK VNVNGGAIAL GHAVGSTGAR LITQAVHELE
RADKSTALIT MCAGGAHATA TIIERI
//
