ID W5TSA1_9NOCA Unreviewed; 442 AA.
AC W5TSA1;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=3-ketoacyl-CoA thiolase {ECO:0000313|EMBL:AHH22167.1};
GN ORFNames=NONO_c74120 {ECO:0000313|EMBL:AHH22167.1};
OS Nocardia nova SH22a.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=1415166 {ECO:0000313|EMBL:AHH22167.1, ECO:0000313|Proteomes:UP000019150};
RN [1] {ECO:0000313|EMBL:AHH22167.1, ECO:0000313|Proteomes:UP000019150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH22a {ECO:0000313|EMBL:AHH22167.1};
RX PubMed=24747905;
RA Luo Q., Hiessl S., Poehlein A., Daniel R., Steinbuchel A.;
RT "Insights into the Microbial Degradation of Rubber and Gutta-Percha by
RT Analysis of the Complete Genome of Nocardia nova SH22a.";
RL Appl. Environ. Microbiol. 80:3895-3907(2014).
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000256|RuleBase:RU003557}.
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DR EMBL; CP006850; AHH22167.1; -; Genomic_DNA.
DR RefSeq; WP_025353437.1; NZ_CP006850.1.
DR AlphaFoldDB; W5TSA1; -.
DR STRING; 1415166.NONO_c74120; -.
DR KEGG; nno:NONO_c74120; -.
DR PATRIC; fig|1415166.3.peg.7605; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_2_0_11; -.
DR OrthoDB; 1402717at2; -.
DR Proteomes; UP000019150; Chromosome.
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:UP000019150};
KW Transferase {ECO:0000256|RuleBase:RU003557}.
FT DOMAIN 23..292
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 300..442
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 107
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 399
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 429
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 442 AA; 46689 MW; C30B9767713185D8 CRC64;
MTTKARSAKT TSASSRGKQA KPVAVLGGNR IPFARSDGRY AHASNQDMFT AALNGLVSRF
GLQGERLGMV VGGAVLKRVG EHGMVRESVL GSELSPYTPA HDLQLACGTG LQSIVTVGDG
IALGRIEAGI GGGTDTTSDA PIGVSESMRE WMLDANRARN NKDYVKLVGR LRPSMVGIEI
PRNAEPRTGL SMGDHAAITA KEFGIAREAQ DELAYLSHKN MAAAYDRGFF DDLVTPFLGL
TRDDNLRPNS TLEKLATLKP VFGNKLGDAT MTAGNSTPLT DGASAVLLGS EEWAAEHKLA
PLAYLVDSEV AAVDYVWGPD GLLMAPTYAV PRLLARNGLT LQDFDYYEIH EAFASVVLAT
LQSWESDQYC KERLGLDGAL GSIDRSKLNV NGSSLAAGHP FAATGGRIIA QTAKQLAEKG
SGRALISICA AGGQGVVAIL ER
//
