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Database: UniProt
Entry: A0A365HCY3_9ACTN
LinkDB: A0A365HCY3_9ACTN
Original site: A0A365HCY3_9ACTN 
ID   A0A365HCY3_9ACTN        Unreviewed;       389 AA.
AC   A0A365HCY3;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Probable acetyl-CoA acetyltransferase {ECO:0000256|ARBA:ARBA00040529};
DE            EC=2.3.1.9 {ECO:0000256|ARBA:ARBA00012705};
GN   ORFNames=DPM19_02180 {ECO:0000313|EMBL:RAY16994.1};
OS   Actinomadura craniellae.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Thermomonosporaceae; Actinomadura.
OX   NCBI_TaxID=2231787 {ECO:0000313|EMBL:RAY16994.1, ECO:0000313|Proteomes:UP000251891};
RN   [1] {ECO:0000313|EMBL:RAY16994.1, ECO:0000313|Proteomes:UP000251891}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LHW63021 {ECO:0000313|EMBL:RAY16994.1,
RC   ECO:0000313|Proteomes:UP000251891};
RA   Li L., Xu Q.H., Lin H.W., Lu Y.H.;
RT   "Actinomadura craniellae sp. nov. isolated from marine sponge Craniella
RT   sp.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC       {ECO:0000256|ARBA:ARBA00010982, ECO:0000256|RuleBase:RU003557}.
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:RAY16994.1}.
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DR   EMBL; QLYX01000001; RAY16994.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A365HCY3; -.
DR   OrthoDB; 9764638at2; -.
DR   Proteomes; UP000251891; Unassembled WGS sequence.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   CDD; cd00751; thiolase; 1.
DR   Gene3D; 3.40.47.10; -; 2.
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   PANTHER; PTHR18919; ACETYL-COA C-ACYLTRANSFERASE; 1.
DR   PANTHER; PTHR18919:SF153; TRIFUNCTIONAL ENZYME SUBUNIT BETA, MITOCHONDRIAL; 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; PS00098; THIOLASE_1; 1.
DR   PROSITE; PS00099; THIOLASE_3; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW   ECO:0000313|EMBL:RAY16994.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000251891};
KW   Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:RAY16994.1}.
FT   DOMAIN          5..257
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          267..387
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
FT   ACT_SITE        86
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        345
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        375
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ   SEQUENCE   389 AA;  40354 MW;  A388AABF6726F1BF CRC64;
     MPEAVIVSAV RTPIGTARKG TLTETPAEDL ATHVLREAVR RSGIAPERFD DVIFGESMYG
     GGDLARHAAV AAGMTRVPGV SMNRHCASSL TAVGTAAANI RAGMDRAIVA GGVQSSSLMP
     ALDWRIPLGD ATERRIAPTF PYTDDATDET AMTVGWNVAQ KYGLTREQMD AWALRSHQRA
     VAATEAGVFA DEIVPIKVTR RDGSVVEFAA DEHPRATTSA EKMAALPPLR PDIEGFSITA
     GNASGSNDGA AALAVVADDL ARAEGLRTLA TVRAWAAVGV EPKFTGVGAI DAATKVLERA
     GLTTADIDLW EINEAFASVP VATCQVLKLD EDRVNVHGSG CSLGHPIAAT GARMLTTLAH
     ELRRRGGGIG LATMCAGGGQ GGAVVIEVA
//
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