ID A0A0M4Q9F8_9PSEU Unreviewed; 406 AA.
AC A0A0M4Q9F8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:ALE80461.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:ALE80461.1};
GN ORFNames=WY02_20885 {ECO:0000313|EMBL:ALE80461.1};
OS Pseudonocardia sp. AL041005-10.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=445576 {ECO:0000313|EMBL:ALE80461.1, ECO:0000313|Proteomes:UP000067245};
RN [1] {ECO:0000313|EMBL:ALE80461.1, ECO:0000313|Proteomes:UP000067245}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AL041005-10 {ECO:0000313|EMBL:ALE80461.1,
RC ECO:0000313|Proteomes:UP000067245};
RX PubMed=26438860; DOI=10.1073/pnas.1515348112;
RA Sit C.S., Van Arnam E.B., Ramadhar T.R.;
RT "Variable genetic architectures produce virtually identical molecules in
RT bacterial symbionts of fungus-growing ants.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:13150-13154(2015).
CC -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000256|ARBA:ARBA00004792}.
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; CP011862; ALE80461.1; -; Genomic_DNA.
DR RefSeq; WP_062400346.1; NZ_CP011862.1.
DR AlphaFoldDB; A0A0M4Q9F8; -.
DR STRING; 445576.WY02_20885; -.
DR KEGG; psea:WY02_20885; -.
DR PATRIC; fig|445576.3.peg.4560; -.
DR OrthoDB; 9764638at2; -.
DR Proteomes; UP000067245; Chromosome.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
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:SF8; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 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 ECO:0000313|EMBL:ALE80461.1};
KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:ALE80461.1}.
FT DOMAIN 5..274
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 283..403
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 361
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 391
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 406 AA; 42650 MW; 7B8110ED9595B7DD CRC64;
MPEAVIVAAA RSPIGRANKG SLAGMRPDDL TVQMVRAALG QVPQLDPAEI DDLMLGCGLP
GGEQGNNLAR IVAIQLGQDS LPGTTVTRYC SSSLQTTRMA LHAIKAGEGD VFVSAGVETV
SRFSRGTSDS WPDTHNPLFA DAEARTAETA EKGAESWTDP RDQSLLPDAY ISMGQTAENL
ARYKDVSRED MDRFAVQSQN RAEKAIADGF FAREITPVTL PDGTVVDTDD GPRPGTTYDK
ISQLKPVFRP DGRITAGNAC PLNDGAAALV IMSDTKAEQL GVTPLARVVS TGVTGLSPEI
MGYGPVEASQ QALRRAGLTI DDIDLVEINE AFAAQVLPSA RDLGIDEAKL NVHGGAIALG
HPFGMTGARI TTTLMNGLRS TGGRYGLETM CVGGGQGMAL VIENLA
//
