ID A0A2U1C4G7_9BURK Unreviewed; 392 AA.
AC A0A2U1C4G7;
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:PVY55813.1};
GN ORFNames=C8D04_1027 {ECO:0000313|EMBL:PVY55813.1};
OS Simplicispira sp. 125.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Simplicispira.
OX NCBI_TaxID=2135643 {ECO:0000313|EMBL:PVY55813.1, ECO:0000313|Proteomes:UP000245599};
RN [1] {ECO:0000313|EMBL:PVY55813.1, ECO:0000313|Proteomes:UP000245599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=125 {ECO:0000313|EMBL:PVY55813.1,
RC ECO:0000313|Proteomes:UP000245599};
RA Chistoserdova L.;
RT "Synthetic bacterial communities of pure cultures isolated from sediment of
RT Lake Washington, USA.";
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:PVY55813.1}.
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DR EMBL; QEKM01000001; PVY55813.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U1C4G7; -.
DR OrthoDB; 6139495at2; -.
DR Proteomes; UP000245599; 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:UP000245599};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:PVY55813.1}.
FT DOMAIN 4..262
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 270..391
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 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 392 AA; 40156 MW; DC446F575D04FABC CRC64;
MEDIVIVSAA RTAVGKFGGA LAKTPATELG SIVIREAMAR AGLQADQIGE VIMGQVLAAG
VGQNPARQAM MKAGVAKETP ALTINAVCGS GLKAVMLAAQ AVATGDSEIV VAGGQENMSL
SPHVLNGSRD GQRMGDWKLT DTMIVDGLWD VYNQYHMGIT AENVAKQYGI TREMQDALAL
ASQQKAAAAQ DAGRFADEIV GVSIPQRKGD PVVFNADEYL NRKTNAEALA GLRAAFDKAG
SVTAGNASGI NDGAAAVVVM SAKKAAALGL KPLARIAAFG TSGLDPAIMG MGPVSASRKA
LQRAGWNAAD VDLFELNEAF AAQACAVNKE LAIDPAKVNV NGGAIAIGHP IGASGCRILV
TLLHEMQRRD AKKGLAALCI GGGMGVSLAL ER
//
