ID K8W3N3_9GAMM Unreviewed; 393 AA.
AC K8W3N3;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:EKT54421.1};
GN ORFNames=OOA_17351 {ECO:0000313|EMBL:EKT54421.1};
OS Providencia burhodogranariea DSM 19968.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Providencia.
OX NCBI_TaxID=1141662 {ECO:0000313|EMBL:EKT54421.1, ECO:0000313|Proteomes:UP000009336};
RN [1] {ECO:0000313|EMBL:EKT54421.1, ECO:0000313|Proteomes:UP000009336}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19968 {ECO:0000313|EMBL:EKT54421.1,
RC ECO:0000313|Proteomes:UP000009336};
RX PubMed=23145767; DOI=10.1186/1471-2164-13-612;
RA Galac M.R., Lazzaro B.P.;
RT "Comparative genomics of bacteria in the genus Providencia isolated from
RT wild Drosophila melanogaster.";
RL BMC Genomics 13:612-612(2012).
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:EKT54421.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AKKL01000047; EKT54421.1; -; Genomic_DNA.
DR AlphaFoldDB; K8W3N3; -.
DR STRING; 1141662.OOA_17351; -.
DR PATRIC; fig|1141662.3.peg.3522; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_0_0_6; -.
DR OrthoDB; 9764638at2; -.
DR Proteomes; UP000009336; 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:SF164; ACETYL-COA 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; 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|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU003557};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:EKT54421.1}.
FT DOMAIN 5..261
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 269..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 348
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 378
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 393 AA; 40988 MW; A89A78049D5B5148 CRC64;
MNDMVIVSAV RTAIGNFGGA LANISATELG AIVAKAAFER AGINPDLVDE VILGNVLQAG
LGQNPARQVS LKAEMSDSIP ATTLNIVCGS GLKSVILAAQ TIKAGDNKIV LAGGMENMSA
APYLLDKARF GYRMGNGTLT DSVVHDGLSC AFNHYHMGIT AENVAKYYAI SREEQDEIAL
RSQQRAQAAI ENGAFKNEIV PVIVKQKKVE VVFKQDEYPR FDTSLESLSK LRPAFTNDGS
VTAGNSSGIN DGAAALLVMS SQQAADLSLK PLARIRGYAT TGVNPSVMGI GPVSSTLNAL
KKAQLTIADL DLIEANEAFA AQFIAVGKEL GLDPQKTNIN GGAIALGHPI GASGARILVS
LLHALQQQDK TFGLATLCVG GGQGVSVIVE RLS
//
