ID A0A0S9RD64_9ACTN Unreviewed; 415 AA.
AC A0A0S9RD64;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:KQP80157.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:KQP80157.1};
GN ORFNames=ASF37_01140 {ECO:0000313|EMBL:KQP80157.1};
OS Aeromicrobium sp. Leaf289.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Aeromicrobium.
OX NCBI_TaxID=1736324 {ECO:0000313|EMBL:KQP80157.1, ECO:0000313|Proteomes:UP000051640};
RN [1] {ECO:0000313|Proteomes:UP000051640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf289 {ECO:0000313|Proteomes:UP000051640};
RA Garrido-Oter R., Mueller D.B.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000051640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf289 {ECO:0000313|Proteomes:UP000051640};
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:KQP80157.1}.
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DR EMBL; LMNK01000001; KQP80157.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S9RD64; -.
DR Proteomes; UP000051640; 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:KQP80157.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051640};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:KQP80157.1}.
FT DOMAIN 2..263
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 271..413
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 77
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 370
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 401
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 415 AA; 43942 MW; A7AD28CE8C9F1EA7 CRC64;
MPFARSNTVY QNVSNQDMLT AALDGLVERY DLEGEKVGEV VAGAVLKHSR DFNLARETVL
GSKLSPETPA EDIQQACGTG LQAAFQVAAK ISLGKIESGI AGGTDTTSDA PLAVGDKLRK
ILIEANNAKD NKGRLAAIAK IRPGYLAPDQ PRNAEPRTGL SMGDHQAITT HAWGITREAQ
DELAAASHQN LAASWDAGWQ DDLVTPFNGV TKDNHLRPDS TVEKLAKLKP VFGKQLGDEA
TMTAGNSTPL SDGASVALLA SEEEAQRRGW TPRAYFVDYE TAAVDYVSGA EGLLMAPAYA
VPRMLARNGL TLQDFDYYEI HEAFAGQVLS TLAAWEDPDF CKERLGLDVP LGSIDRSRLN
VKGSSLAAAH PFAATGARIV ANLAKLLHEK GPGSRGLISI CAAGGQGVVA ILEGA
//
