ID A4XT23_PSEMY Unreviewed; 394 AA.
AC A4XT23;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:ABP84489.1};
DE EC=2.3.1.16 {ECO:0000313|EMBL:ABP84489.1};
GN OrderedLocusNames=Pmen_1725 {ECO:0000313|EMBL:ABP84489.1};
OS Pseudomonas mendocina (strain ymp).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=399739 {ECO:0000313|EMBL:ABP84489.1};
RN [1] {ECO:0000313|EMBL:ABP84489.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ymp {ECO:0000313|EMBL:ABP84489.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C., Bruce D., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Hersman L., Dubois J., Maurice P., Richardson P.;
RT "Complete sequence of Pseudomonas mendocina ymp.";
RL Submitted (APR-2007) 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; CP000680; ABP84489.1; -; Genomic_DNA.
DR AlphaFoldDB; A4XT23; -.
DR STRING; 399739.Pmen_1725; -.
DR KEGG; pmy:Pmen_1725; -.
DR PATRIC; fig|399739.8.peg.1749; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_1_1_6; -.
DR OrthoDB; 8951704at2; -.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IEA:UniProtKB-EC.
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|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU003557};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:ABP84489.1}.
FT DOMAIN 5..262
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 273..392
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 90
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 350
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 380
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 394 AA; 41027 MW; 065F60572B45111F CRC64;
MQDAVIVSTA RTPIAKAFRG AFNDLKAPSM SAIAIQAAVQ RAGIEPAEIE DVVMGTAMQG
GTASTNLARL SLLAAGLPLS VSGQTIDRQC ASGLMAISIA AKQIMVDGMA VTIGAGQEQI
SLVQNHHMQW AGADADAQVI RQAEHAYLPM LQTAELVARR YGISREAQDA YALESQRRTA
AAQDAGLFAE EIVAVSARKK RVDKETGALS FEDVTLRLDE GNRPQTALAD LQALRPVIEG
GCITAGNASQ LSDGASACVL MSGALAAQRG IAPLGLYRGI AVAGLAPEEM GIGPVFAVPK
LLRQHGLTVD DIGLWELNEA FACQVLYSAE KLGIDPTRLN VNGGAIAIGH PYGMSGARMV
GHALLEGKRR GVKYVVVTMC VGGGMGAAGL FEVL
//
