ID A0A1X9YAN8_9SPHN Unreviewed; 383 AA.
AC A0A1X9YAN8;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:ARS25882.1};
GN ORFNames=KC8_01045 {ECO:0000313|EMBL:ARS25882.1};
OS Sphingomonas sp. KC8.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1030157 {ECO:0000313|EMBL:ARS25882.1, ECO:0000313|Proteomes:UP000194475};
RN [1] {ECO:0000313|EMBL:ARS25882.1, ECO:0000313|Proteomes:UP000194475}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KC8 {ECO:0000313|EMBL:ARS25882.1};
RA Chen Y.-L., Yu C.-P., Hu A., Lee T.-H., Yang F.-C., Ismail W., Wang P.-H.,
RA Wang C.-H., Goh K.-S., Shih C.-J., Chiang Y.-R.;
RT "Bacteria use an extradiol dioxygenase-mediated pathway to degrade natural
RT estrogens in aquatic ecosystems.";
RL Submitted (JUN-2016) 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; CP016306; ARS25882.1; -; Genomic_DNA.
DR RefSeq; WP_010125401.1; NZ_CP016306.1.
DR AlphaFoldDB; A0A1X9YAN8; -.
DR STRING; 1030157.GCA_000214335_02297; -.
DR KEGG; spkc:KC8_01045; -.
DR eggNOG; COG0183; Bacteria.
DR OrthoDB; 9764638at2; -.
DR Proteomes; UP000194475; Chromosome.
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; 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.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW Reference proteome {ECO:0000313|Proteomes:UP000194475};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:ARS25882.1}.
FT DOMAIN 5..252
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 260..382
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 339
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 369
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 383 AA; 40315 MW; E100CEA794D7D0EA CRC64;
MPEAYIVDAI RTPTGKKKGS LAAMHPADLG AIPIKAIVDR TGINPDAVDD VVWGCLDAIG
PQAGNMGRTA WLAAGYTEAV PGVTIDRQCG SSQQAIHFAA QGVMSGTQDL VIAGGCQNMN
AIPISAAMYA GQTYGFETPF SGSPAWAARY GDEEVNQIYA AEKIANTWGI SRRDMEVFAA
ESNARAERAI DEGRFDSQIV PVGDFKMDET VRRGTTLEGL ANLKTVREGG LITAGVSSQI
SDGAAAVLIA SERAVKEHGL KPRARIHHLT VRGDSPIFML TAPIPATRHA LAKAGMKLSD
IDLVEINEAF ASVALAWAKD LDADLSKVNV NGGAIALGHP LGATGAKLMT TLLYELERTG
GRYGLQTMCE GGGLANVTII ERL
//
