ID F6F1K0_SPHCR Unreviewed; 417 AA.
AC F6F1K0;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:AEG51416.1};
DE EC=2.3.1.16 {ECO:0000313|EMBL:AEG51416.1};
GN ORFNames=Sphch_3834 {ECO:0000313|EMBL:AEG51416.1};
OS Sphingobium chlorophenolicum L-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=690566 {ECO:0000313|EMBL:AEG51416.1, ECO:0000313|Proteomes:UP000007150};
RN [1] {ECO:0000313|EMBL:AEG51416.1, ECO:0000313|Proteomes:UP000007150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-1 {ECO:0000313|EMBL:AEG51416.1,
RC ECO:0000313|Proteomes:UP000007150};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Daligault H., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Pagani I., Turner P., Copley S., Woyke T.;
RT "Complete sequence of chromosome 2 of Sphingobium chlorophenolicum L-1.";
RL Submitted (MAY-2011) 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}.
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DR EMBL; CP002799; AEG51416.1; -; Genomic_DNA.
DR RefSeq; WP_013849640.1; NC_015594.1.
DR AlphaFoldDB; F6F1K0; -.
DR STRING; 690566.Sphch_3834; -.
DR KEGG; sch:Sphch_3834; -.
DR HOGENOM; CLU_031026_2_3_5; -.
DR Proteomes; UP000007150; Chromosome 2.
DR GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IEA:UniProtKB-EC.
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; IPR020613; Thiolase_CS.
DR InterPro; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR43365; BLR7806 PROTEIN; 1.
DR PANTHER; PTHR43365:SF1; STEROID 3-KETOACYL-COA THIOLASE FADA6; 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; PS00737; THIOLASE_2; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW ECO:0000313|EMBL:AEG51416.1};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:AEG51416.1}.
FT DOMAIN 4..235
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 295..416
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 92
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 373
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 403
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 417 AA; 43992 MW; F2EAC158260D081F CRC64;
MSEVYIVDAV RTPRGIGKVG KGALADMHPQ HLAAATLKAL AERNAIRTEE VDDIIWGTSA
QRGPQGGDMA RMAALDAGYD VRASGVTLDR FCGSGISTVS LAAGMIKSGL EDLIIAGGTE
MMSLTATMAR QDAARGAPPT MMDAGNLRLR ARHPQSHQGV CADAIATLEG IRRADVDALA
LDSQQKAARA MSEGRFDRSV IAVHREDGSV ALDKDEFPRP QTTAEGLAGL KPSFDALADF
ALDESGTTYR GLINAVYPDL KIEHIHHAGN SSGVVDGAAA LLLSSPDYAA RQGWKPRARI
VATANIGDSP TLMLNAPVPA AKKVLAKAGL KIEDIDLWEV NEAFAVVTEK FIRDLRLDRD
KVNVNGGAIA LGHPIGATGS ILIGTVLDEL ERRDLKRGLI TMCAAGGMAP AIIIERV
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