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Database: UniProt
Entry: A0A0Q7PWR2_9ACTN
LinkDB: A0A0Q7PWR2_9ACTN
Original site: A0A0Q7PWR2_9ACTN 
ID   A0A0Q7PWR2_9ACTN        Unreviewed;       403 AA.
AC   A0A0Q7PWR2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:KQY55990.1};
DE            EC=2.3.1.9 {ECO:0000313|EMBL:KQY55990.1};
GN   ORFNames=ASD11_16045 {ECO:0000313|EMBL:KQY55990.1};
OS   Aeromicrobium sp. Root495.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Aeromicrobium.
OX   NCBI_TaxID=1736550 {ECO:0000313|EMBL:KQY55990.1, ECO:0000313|Proteomes:UP000051970};
RN   [1] {ECO:0000313|EMBL:KQY55990.1, ECO:0000313|Proteomes:UP000051970}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root495 {ECO:0000313|EMBL:KQY55990.1,
RC   ECO:0000313|Proteomes:UP000051970};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQY55990.1, ECO:0000313|Proteomes:UP000051970}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root495 {ECO:0000313|EMBL:KQY55990.1,
RC   ECO:0000313|Proteomes:UP000051970};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQY55990.1}.
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DR   EMBL; LMFJ01000002; KQY55990.1; -; Genomic_DNA.
DR   RefSeq; WP_056289887.1; NZ_LMFJ01000002.1.
DR   AlphaFoldDB; A0A0Q7PWR2; -.
DR   STRING; 1736550.ASD11_16045; -.
DR   OrthoDB; 4440515at2; -.
DR   Proteomes; UP000051970; Unassembled WGS sequence.
DR   GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IEA:UniProtKB-EC.
DR   CDD; cd00751; thiolase; 1.
DR   Gene3D; 3.40.47.10; -; 2.
DR   InterPro; IPR002155; Thiolase.
DR   InterPro; IPR016039; Thiolase-like.
DR   InterPro; IPR020615; Thiolase_acyl_enz_int_AS.
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; PS00098; THIOLASE_1; 1.
DR   PROSITE; PS00737; THIOLASE_2; 1.
DR   PROSITE; PS00099; THIOLASE_3; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW   ECO:0000313|EMBL:KQY55990.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051970};
KW   Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:KQY55990.1}.
FT   DOMAIN          6..227
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          280..402
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        359
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        389
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ   SEQUENCE   403 AA;  42151 MW;  C65D11D14E583482 CRC64;
     MTEAFVYDAI RTPRGRGKKT GSLHEVKPIS LLTGLLDELK TRNPDLAPNE IDDVILGVVS
     PVGDQGADIA RTAVLAAGFG EQVAGVQLNR FCGSGLESIN QASARVKSGW EDLIVAGGVE
     SMSRVPMASD GGAWAMDPKT ALETDFVPQG IGADLIATLE GFSRTDVDTF AAESQARAAK
     AIANGYFDKS VIPVKDINGL PVLDHDEFVR EGTTVESLSS LGASFAGLGD FGFDAVALEK
     YITVEKINHV HHAGNSSGIV DGASLVLIGN EKAGERHGLT PRARIVSTAV IGSEPTIMLT
     GPGPAARKAL AKAGLQPDDI DLIEINEAFA AVAMKLMRDL DDYPHEQTNV NGGAIAMGHP
     LGATGGMILG TLVDELERRE KRYGLATLCI GGGMGIATIV ERI
//
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