ID A0A1B3Z795_9SPHN Unreviewed; 390 AA.
AC A0A1B3Z795;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:AOH83293.1};
GN ORFNames=AWL63_04215 {ECO:0000313|EMBL:AOH83293.1};
OS Sphingomonas panacis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1560345 {ECO:0000313|EMBL:AOH83293.1, ECO:0000313|Proteomes:UP000094256};
RN [1] {ECO:0000313|EMBL:AOH83293.1, ECO:0000313|Proteomes:UP000094256}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DCY99 {ECO:0000313|EMBL:AOH83293.1,
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; AOH83293.1; -; Genomic_DNA.
DR RefSeq; WP_069203871.1; NZ_CP014168.1.
DR AlphaFoldDB; A0A1B3Z795; -.
DR STRING; 1560345.AWL63_04215; -.
DR KEGG; span:AWL63_04215; -.
DR OrthoDB; 7181944at2; -.
DR Proteomes; UP000094256; Chromosome.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
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; -; 1.
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; PTHR43853; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 1.
DR PANTHER; PTHR43853:SF22; ACETYL-COA ACETYLTRANSFERASE; 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 Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:AOH83293.1}.
FT DOMAIN 5..259
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 269..388
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 346
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 376
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 390 AA; 40693 MW; 0F175BA5855034EB CRC64;
MREAVIVSTA RTPIGRAYKG AFNATPSPTL AAHAIRAAVE RSGVAPRDID DVIMGSALPQ
GFQHTIGRTA ALRAGLPNGV SGQTIDRQCA SGLMAIATAA KQVIVDRMNI VVAGGVESIS
MVQTPALRVD EDADLAAMAP DIYMPMLQTA EIVAKRYGIS RERQDAYALR SQRLTGEAQA
AGAFDAEIVP VTTIMAVTDI QTRTTNHVAV TLDEDQGNRP QTTLEGLAAL RPVIEGGQIS
AGNASQLSDG ASACVVMDAQ YAADCGIAPL GRYVGMAMAG TDPDEMGIGP ALAVPKLLDR
FGLTVDDIGL WELNEAFAVQ VLYCQDVLGI PDDRLNVSGG AISIGHPYGM SGARMTGHAL
IEGRRRNARY VVVTMCVGGG MGAAALFETA
//
