ID A0A365ZAI0_9ACTN Unreviewed; 448 AA.
AC A0A365ZAI0;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE SubName: Full=Acetyl-CoA C-acetyltransferase {ECO:0000313|EMBL:RBM16166.1};
GN ORFNames=DEH69_17400 {ECO:0000313|EMBL:RBM16166.1};
OS Streptomyces sp. PT12.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1510197 {ECO:0000313|EMBL:RBM16166.1, ECO:0000313|Proteomes:UP000252839};
RN [1] {ECO:0000313|EMBL:RBM16166.1, ECO:0000313|Proteomes:UP000252839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PT12 {ECO:0000313|EMBL:RBM16166.1,
RC ECO:0000313|Proteomes:UP000252839};
RA Devaraj K., Tan G.Y.A.;
RT "Diversity of actinobacteria isolated from Cape Rachado, Malaysia.";
RL Submitted (MAY-2018) 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:RBM16166.1}.
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DR EMBL; QEST01000149; RBM16166.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A365ZAI0; -.
DR OrthoDB; 1402717at2; -.
DR Proteomes; UP000252839; Unassembled WGS sequence.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
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 Reference proteome {ECO:0000313|Proteomes:UP000252839};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:RBM16166.1}.
FT DOMAIN 9..282
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 315..443
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 93
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 395
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 431
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 448 AA; 46824 MW; 6E1C0200AF8DAA8F CRC64;
MRASGVRRVA VLGGNRIPFA RADGPYATAS NGEMLAAALE GLVERFGLRG ELLGEFVAGA
VLKHSRDFQL ARETVLGSAL DHRTPAFDVQ QACGTGLEAV ILVANKIALG QIDSGVAGGV
DTASDVPLAL HDGLRRLLLR ARRERTTPRR LRALAGVRPR QLLPEIPRNA EPRTGLSMGE
HAARTAAAWG VTRADQDAFA AASHRRLAAA YERGFFDDLL TPFRGLQRDQ TLRPDSTPGQ
LAALRPVFGV GQGGGGEGAT MTAGNSTPLT DGAATVLLAS EEWARERRLP VLAYLTHART
AAVDFVEGDD GPDGPDGLLM APAYAVPRLL DDAGLGLADL DVLEIHEAFA AQVLATLAAW
EDPAFGAQRL GLPGAFGAVD RERVNPLGSS LATGHPFAAT GGRIVATLAK ELHERTRERG
GGPVRGLVSV CAAGGVGVTA ILESRQGS
//
