ID A0A0S9CQN4_9MICC Unreviewed; 438 AA.
AC A0A0S9CQN4;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:KQN95949.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:KQN95949.1};
GN ORFNames=ASF21_15510 {ECO:0000313|EMBL:KQN95949.1};
OS Arthrobacter sp. Leaf234.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1736303 {ECO:0000313|EMBL:KQN95949.1, ECO:0000313|Proteomes:UP000053418};
RN [1] {ECO:0000313|Proteomes:UP000053418}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf234 {ECO:0000313|Proteomes:UP000053418};
RA Garrido-Oter R., Mueller D.B.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000053418}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf234 {ECO:0000313|Proteomes:UP000053418};
RA Vorholt J.;
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|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:KQN95949.1}.
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DR EMBL; LMLU01000011; KQN95949.1; -; Genomic_DNA.
DR RefSeq; WP_055773445.1; NZ_LMLU01000011.1.
DR AlphaFoldDB; A0A0S9CQN4; -.
DR STRING; 1736303.ASF21_15510; -.
DR Proteomes; UP000053418; 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; -; 1.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR42689; ACETYL-COA ACYLTRANSFERASE FADA2 (3-KETOACYL-COA THIOLASE) (BETA-KETOTHIOLASE)-RELATED; 1.
DR PANTHER; PTHR42689:SF1; ACETYL-COA ACYLTRANSFERASE FADA2 (3-KETOACYL-COA THIOLASE) (BETA-KETOTHIOLASE)-RELATED; 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.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW ECO:0000313|EMBL:KQN95949.1};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:KQN95949.1}.
FT DOMAIN 18..287
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 296..435
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 101
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 394
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 423
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 438 AA; 45779 MW; 8455C3E2B11A9F7B CRC64;
MADQAGAQNA AQSPRTAVVI GGNRIPFARA GGAYAYSSNR DMLIAALDGL VARFGLQGER
IGEVAAGAVL KHSRDFNLTR EAVLGSALSP ETPAYDLQQA CATGLETVVG LSNKIKLGQI
ESGIAGGVDS ASDAPIAVSE GLRRVLLDLS RARTTQQKIR ILSTLRPKDL SPNAPGTGEP
RTGLSMGEHQ AITTAAWQIT REAQDELAYR SHQNLAAAYD RGFFADLLTP YRGLMRDANL
RADTSPEKLA TLKPVFGKGL DSPATMTAGN STPLTDGAAV VLLGSEDYAR ANNLPMLANV
VDAEAAAVDF VQGDEGLLMA PVHALPRLLK RNGLTFADFD FFEIHEAFAG TVLSSLAAWE
DEEYCRRVLG LDGALGSIDR SKLNVNGSSL AAGHPFAATG GRIVASLAKT LSEQGGRGLI
SVCAAGGQGV VAILEARN
//
