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Database: UniProt
Entry: A0A2S5JGI0_9RHOB
LinkDB: A0A2S5JGI0_9RHOB
Original site: A0A2S5JGI0_9RHOB 
ID   A0A2S5JGI0_9RHOB        Unreviewed;       391 AA.
AC   A0A2S5JGI0;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Acetyl-CoA C-acetyltransferase {ECO:0000313|EMBL:PPB80529.1};
GN   ORFNames=LV82_01878 {ECO:0000313|EMBL:PPB80529.1};
OS   Albidovulum inexpectatum.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Albidovulum.
OX   NCBI_TaxID=196587 {ECO:0000313|EMBL:PPB80529.1, ECO:0000313|Proteomes:UP000239736};
RN   [1] {ECO:0000313|EMBL:PPB80529.1, ECO:0000313|Proteomes:UP000239736}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12048 {ECO:0000313|EMBL:PPB80529.1,
RC   ECO:0000313|Proteomes:UP000239736};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (JAN-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:PPB80529.1}.
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DR   EMBL; PRDS01000005; PPB80529.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S5JGI0; -.
DR   OrthoDB; 9764638at2; -.
DR   Proteomes; UP000239736; 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; IPR020613; Thiolase_CS.
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; PS00737; THIOLASE_2; 1.
DR   PROSITE; PS00099; THIOLASE_3; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW   Reference proteome {ECO:0000313|Proteomes:UP000239736};
KW   Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:PPB80529.1}.
FT   DOMAIN          4..261
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          268..390
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
FT   ACT_SITE        88
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        347
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        377
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ   SEQUENCE   391 AA;  40704 MW;  23ED24CA17D2C041 CRC64;
     MTNVVIVSAA RTPVGSFNGS FANTPAHDLG AAVLEAVVAR AGIDKAEVSE TILGQVLTAG
     QGQNPARQAH IKAGLPMESA AWSINQVCGS GLRSVALAAQ HVQLGDAAIV CAGGQENMSL
     APHVAHLRAG HKMGDVQFID SMIKDGLWDA FNGYHMGNTA ENVAQKWQIS REMQDEFALS
     SQQKAAAAQA AGKFKDEIIP ITIKTRKGDI VVDADEYIRP NTTLEALQKL RPAFQKDGTV
     TAGNASGIND GAAAVLVMSE EEAARRGLKP LARIASYATA GLDPAIMGVG PIHASRKALE
     KAGWKVEDLD LIEANEAFAA QACAVNKDMG WDPAKVNVNG GAIAIGHPIG ASGARILNTL
     LFEMQRSGAK KGLATLCIGG GMGVAMCLER A
//
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