ID A0A2S4YZI6_9ACTN Unreviewed; 406 AA.
AC A0A2S4YZI6;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Acetyl-CoA C-acyltransferase {ECO:0000313|EMBL:POX54356.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:POX54356.1};
GN ORFNames=C3488_02620 {ECO:0000313|EMBL:POX54356.1};
OS Streptomyces sp. Ru72.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2080747 {ECO:0000313|EMBL:POX54356.1, ECO:0000313|Proteomes:UP000237426};
RN [1] {ECO:0000313|EMBL:POX54356.1, ECO:0000313|Proteomes:UP000237426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ru72 {ECO:0000313|EMBL:POX54356.1,
RC ECO:0000313|Proteomes:UP000237426};
RA Suneja G., Sharma R.;
RT "Genome sequencing of cellulose degrading bacteria.";
RL Submitted (FEB-2018) 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:POX54356.1}.
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DR EMBL; PQSR01000003; POX54356.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S4YZI6; -.
DR OrthoDB; 9764638at2; -.
DR Proteomes; UP000237426; Unassembled WGS sequence.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
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; 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:POX54356.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000237426};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:POX54356.1}.
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; 42799 MW; 2D86F1DFA1ED7D46 CRC64;
MPEAVIVSTA RSPIGRAFKG SLKDLRPDDL TATIIQAALD KVPALDPKDI DDLMLGCGLP
GGEQGHNLGR IVAVQMGMDH LPGCTVTRYC SSSLQTSRMA LHAIKAGEGD VFISAGVEMV
SRSVKGTSDG LPDTHNPLFA DAEARTAAVA ESEGAEWHDP REDGLLPDPY IAMGQTAENL
ARLKGVTREE MDEFGVRSQN LAEQAIAKGF WEREITPVTL PDGTVVSKDD GPRPGVTLEA
VAGLKPVFRP DGRVTAGNCC PLNDGAAALV IMSDTKAREL GLTPLARIVS TGVSGLSPEI
MGYGPVEASK QALKRAGLTI DDIDLVEINE AFAAQVIPSY RDLGIPLEKL NVNGGAIAVG
HPFGMTGARI TATLINSLQW HDKQFGLETM CVGGGQGMAM VIERLS
//
