ID N0E5N3_9MICO Unreviewed; 407 AA.
AC N0E5N3;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Putative 3-ketoacyl-CoA thiolase (Beta-ketothiolase) or Acetoacetyl-CoA thiolase {ECO:0000313|EMBL:CCH71405.1};
DE EC=2.3.1.16 {ECO:0000313|EMBL:CCH71405.1};
DE EC=2.3.1.9 {ECO:0000313|EMBL:CCH71405.1};
GN ORFNames=BN10_920035 {ECO:0000313|EMBL:CCH71405.1};
OS Phycicoccus elongatus Lp2.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Phycicoccus.
OX NCBI_TaxID=1193181 {ECO:0000313|EMBL:CCH71405.1, ECO:0000313|Proteomes:UP000013167};
RN [1] {ECO:0000313|EMBL:CCH71405.1, ECO:0000313|Proteomes:UP000013167}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lp2 {ECO:0000313|EMBL:CCH71405.1,
RC ECO:0000313|Proteomes:UP000013167};
RX PubMed=23178666; DOI=10.1038/ismej.2012.136;
RA Kristiansen R., Nguyen H.T.T., Saunders A.M., Nielsen J.L., Wimmer R.,
RA Le V.Q., McIlroy S.J., Petrovski S., Seviour R.J., Calteau A.,
RA Nielsen K.L., Nielsen P.H.;
RT "A metabolic model for members of the genus Tetrasphaera involved in
RT enhanced biological phosphorus removal.";
RL ISME J. 7:543-554(2013).
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:CCH71405.1}.
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DR EMBL; CAIZ01000166; CCH71405.1; -; Genomic_DNA.
DR RefSeq; WP_010851232.1; NZ_HF570956.1.
DR AlphaFoldDB; N0E5N3; -.
DR STRING; 1193181.BN10_920035; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_0_0_11; -.
DR OrthoDB; 9764638at2; -.
DR Proteomes; UP000013167; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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:CCH71405.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000013167};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:CCH71405.1}.
FT DOMAIN 5..275
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 283..405
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 362
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 392
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 407 AA; 42614 MW; C55D4DA3B3BF8947 CRC64;
MPEAVIVATA RTPIGRAFKG SLKDIRPDDI STQVVQGLLA KLPELDPTTI DDLYWGCADP
SGKAGNNMAR VIAVMAGLDG LPAATINRFC ASSTQTMRMA FHAIKAGEGE IFVSGGVECV
SQNAAFRGAG ESDPDALNPI FADAQARSAE MARTNATWTD PREQGLLPDV YLAMGQTAEN
VATSRGISRL RQDEWGVTSQ NRAEAAIKAG FFEREILPVT LADGPVVSTD DGPRAGVTLE
AVQALNPVFR ENGTVTAGNC CPLNDGASGV VIMSDTKAKE LGLTPLARII STGVSGLSPE
IMGMGPVEAC RQALARAGMS IKDIDLYEIN EAFASQVLGS ADDLGMDFDR LNVHGGAIAL
GHPFGSTGTR IMATLINGLQ TKDKQFGLES MCVGGGQGMA ILIERLS
//
