ID A4F856_SACEN Unreviewed; 406 AA.
AC A4F856;
DT 17-APR-2007, integrated into UniProtKB/TrEMBL.
DT 17-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE SubName: Full=Acetyl-CoA C-acetyltransferase {ECO:0000313|EMBL:PFG94025.1};
DE SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:CAM00231.1};
DE EC=2.3.1.- {ECO:0000313|EMBL:CAM00231.1};
GN Name=fadA3 {ECO:0000313|EMBL:CAM00231.1};
GN OrderedLocusNames=SACE_0897 {ECO:0000313|EMBL:CAM00231.1};
GN ORFNames=A8924_1291 {ECO:0000313|EMBL:PFG94025.1};
OS Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 /
OS NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharopolyspora.
OX NCBI_TaxID=405948 {ECO:0000313|EMBL:CAM00231.1, ECO:0000313|Proteomes:UP000006728};
RN [1] {ECO:0000313|EMBL:CAM00231.1, ECO:0000313|Proteomes:UP000006728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 /
RC NRRL 2338 {ECO:0000313|Proteomes:UP000006728}, and NRRL 2338
RC {ECO:0000313|EMBL:CAM00231.1};
RX PubMed=17369815; DOI=10.1038/nbt1297;
RA Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S.,
RA Haydock S.F., Leadlay P.F.;
RT "Complete genome sequence of the erythromycin-producing bacterium
RT Saccharopolyspora erythraea NRRL23338.";
RL Nat. Biotechnol. 25:447-453(2007).
RN [2] {ECO:0000313|EMBL:PFG94025.1, ECO:0000313|Proteomes:UP000225825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40517 {ECO:0000313|EMBL:PFG94025.1,
RC ECO:0000313|Proteomes:UP000225825};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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; AM420293; CAM00231.1; -; Genomic_DNA.
DR EMBL; PDBV01000001; PFG94025.1; -; Genomic_DNA.
DR RefSeq; WP_009944150.1; NZ_PDBV01000001.1.
DR AlphaFoldDB; A4F856; -.
DR STRING; 405948.SACE_0897; -.
DR KEGG; sen:SACE_0897; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_1_1_11; -.
DR OrthoDB; 9764638at2; -.
DR Proteomes; UP000006728; Chromosome.
DR Proteomes; UP000225825; Unassembled WGS sequence.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
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:CAM00231.1};
KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW Reference proteome {ECO:0000313|Proteomes:UP000006728};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:CAM00231.1}.
FT DOMAIN 5..274
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 282..404
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; 42788 MW; 41925382D194675A CRC64;
MTEAVIVATA RSPIGRAGKG SLVDVRPDDL TAQIVRAALD KVPELDPSDI DDLMLGCGLP
GGEQGFNMAR VVSVLLGYDH LPGTTVTRYC SSSLQTTRMA LHAIKAGEGD VFISAGVEMV
SRFAKGNSDS LEDTRNPLFD DAQERTQRTA EQGADSWTDP REFDALPDVY IPMGQTAENL
ARLKGISRDE MDDFGVRSQN LAEKAIANGF WAREIVPVTT PSGKVVDADD GPRAGVTKEG
VAGLKPVFRP DGRITAANCC PLNDGAAAVV IMSDTKARQL GLTPLARIVS TGVSGLSPEI
MGLGPVEASK QALARAGLSV GDIDLVEINE AFAAQVIPSY QDLGIPLEKV NVNGGAIAVG
HPFGMTGARI TTTLLNSLQW HDKQFGLETM CVGGGQGMAM VVERLS
//
