ID A0A1B3Z772_9SPHN Unreviewed; 413 AA.
AC A0A1B3Z772;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:AOH83284.1};
GN ORFNames=AWL63_04155 {ECO:0000313|EMBL:AOH83284.1};
OS Sphingomonas panacis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1560345 {ECO:0000313|EMBL:AOH83284.1, ECO:0000313|Proteomes:UP000094256};
RN [1] {ECO:0000313|EMBL:AOH83284.1, ECO:0000313|Proteomes:UP000094256}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DCY99 {ECO:0000313|EMBL:AOH83284.1,
RC ECO:0000313|Proteomes:UP000094256};
RA Kim Y.J., Yang D.C., Sing P.;
RT "Complete genome and mega plasmid sequence of Sphingomonas panacis DCY99
RT elicits systemic resistance in rice to Xanthomonas oryzae.";
RL Submitted (JAN-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; CP014168; AOH83284.1; -; Genomic_DNA.
DR RefSeq; WP_069203862.1; NZ_CP014168.1.
DR AlphaFoldDB; A0A1B3Z772; -.
DR STRING; 1560345.AWL63_04155; -.
DR KEGG; span:AWL63_04155; -.
DR OrthoDB; 9764638at2; -.
DR Proteomes; UP000094256; 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; 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 Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:AOH83284.1}.
FT DOMAIN 5..231
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 290..412
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 369
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 399
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 413 AA; 43736 MW; A27A69343471EB6D CRC64;
MGDALIIDVC RTPRGIGRVG KGALASFHPQ HLAATVLRAV VERNDLRSED IDDVIWGVST
QQGKQGRDLA RMAALFAGFD ERVSGVTLDR FCGSGITAVS FGAGQIMSGM EDLIVAGGTE
MMSHVAELRA SDPSSGMLDA GNLALRRMRP QSNQGICADA IATLDGIPRE ALDDLAYQSQ
QRAEVAIREG RFDRSLVPVL DEHGAIALDR EEYPRPQTTR EGLAALKPSF AELADLPIDA
DGTTFGGMIR RAFPDLKFNH VHHAGNSSGV VDGAAAVLLA SPAYAARNGL KPRARIRAMA
NVGADPTLML NGPGPAARKA LAKAGLTLDD IDLWEVNEAF AIVPEKFIRD LGVDREKVNV
NGGAIALGHP IGCTGAILIG TILDELERRD LKRGLVTMCA AGGMAPAIVI ERV
//
