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Database: UniProt
Entry: A0A2U1CH73_9BURK
LinkDB: A0A2U1CH73_9BURK
Original site: A0A2U1CH73_9BURK 
ID   A0A2U1CH73_9BURK        Unreviewed;       393 AA.
AC   A0A2U1CH73;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Acetyl-CoA C-acetyltransferase {ECO:0000313|EMBL:PVY60177.1};
GN   ORFNames=C7440_3952 {ECO:0000313|EMBL:PVY60177.1};
OS   Pusillimonas noertemannii.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Pusillimonas.
OX   NCBI_TaxID=305977 {ECO:0000313|EMBL:PVY60177.1, ECO:0000313|Proteomes:UP000246145};
RN   [1] {ECO:0000313|EMBL:PVY60177.1, ECO:0000313|Proteomes:UP000246145}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10065 {ECO:0000313|EMBL:PVY60177.1,
RC   ECO:0000313|Proteomes:UP000246145};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (APR-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:PVY60177.1}.
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DR   EMBL; QEKO01000013; PVY60177.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U1CH73; -.
DR   STRING; 1231391.GCA_000308195_01965; -.
DR   OrthoDB; 9764638at2; -.
DR   Proteomes; UP000246145; 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; IPR020610; Thiolase_AS.
DR   InterPro; IPR020617; Thiolase_C.
DR   InterPro; IPR020616; Thiolase_N.
DR   NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR   PANTHER; PTHR18919:SF138; ACETYL-COA C-ACETYLTRANSFERASE; 1.
DR   PANTHER; PTHR18919; ACETYL-COA C-ACYLTRANSFERASE; 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   Reference proteome {ECO:0000313|Proteomes:UP000246145};
KW   Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:PVY60177.1}.
FT   DOMAIN          5..263
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          271..391
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        349
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        379
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ   SEQUENCE   393 AA;  40616 MW;  23FC8604E1716772 CRC64;
     MSDPIVLVSI ARTPMGGMMG SLSGLAAHEL GAIAIKAAVE RAGISPDAVS EVIMGNVLQA
     GQGQAPARQA ALGAGLPQAV GCTTIHKVCG SGLKAAMFAH DLLKAESADV IVAGGQESMS
     NAPYLLLRGR QGYRYGHSTV YDHMALDGLE DAYQRGTAMG VFAESCAGKY SFSREQQDAF
     ALESLRRARA ATEDGSFKWE IAPVTVAGRK GDTVIDTDEG PAKAMPEKIP TLKPAFKKDG
     TVTAANASSI SDGAAAMVLM RESTAKKLGV APIARIVAQA QHSQEPEWFT TAPVGAMQKL
     LEKAGWKTSD VDLYEINEAF AVVTMAAMND LKLDHAKVNI HGGATALGHP IGASGARLLA
     TLVGALRTTG GKKGVASLCI GGGEAVAMAI EML
//
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