ID W5TDL7_9NOCA Unreviewed; 395 AA.
AC W5TDL7;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Putative 3-ketoacyl-CoA thiolase {ECO:0000313|EMBL:AHH15331.1};
GN ORFNames=NONO_c05180 {ECO:0000313|EMBL:AHH15331.1};
OS Nocardia nova SH22a.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=1415166 {ECO:0000313|EMBL:AHH15331.1, ECO:0000313|Proteomes:UP000019150};
RN [1] {ECO:0000313|EMBL:AHH15331.1, ECO:0000313|Proteomes:UP000019150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH22a {ECO:0000313|EMBL:AHH15331.1};
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|ARBA:ARBA00010982, ECO:0000256|RuleBase:RU003557}.
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DR EMBL; CP006850; AHH15331.1; -; Genomic_DNA.
DR AlphaFoldDB; W5TDL7; -.
DR STRING; 1415166.NONO_c05180; -.
DR KEGG; nno:NONO_c05180; -.
DR PATRIC; fig|1415166.3.peg.527; -.
DR eggNOG; COG0183; Bacteria.
DR HOGENOM; CLU_031026_2_3_11; -.
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; IPR020610; Thiolase_AS.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020613; Thiolase_CS.
DR InterPro; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR43365; BLR7806 PROTEIN; 1.
DR PANTHER; PTHR43365:SF1; STEROID 3-KETOACYL-COA THIOLASE FADA6; 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.
DR PROSITE; PS00099; THIOLASE_3; 1.
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 17..262
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 271..393
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 101
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 350
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 380
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 395 AA; 41776 MW; F1F6F300BC6D54CC CRC64;
MSTSSDRRQY APVREAYVID AVRTPIGKRG GALAGVHPAD LGAAALRGLL SRNDIDPGKV
DDVIFGCVDA IGPQAGNIAR TAWLAAGYPE EVPGTTVDRQ CGSSQQAINF GAQAIMSGTA
EVIVAGGVQN MSAIPISAAM LAGKEYGFDS PFVGSTGWDH RYGTGEVSQF NGAQMIAEKW
DISREDMERW ALRSHERARK AIAEGSFDRE IVPVGDFWID EGPRETSLEK MAGLKPLTEG
SRLTAAVASQ ISDGASATLL ASDWAVAEYG LKPRARIHHV SARGADPIYM LTAPIPATKW
ALEKTGLTID DMDVIEINEA FAPVVLAWLK ETGANPDKVN VHGGAIALGH PLGATGAKLF
ATLLNELERV NGRYGLLTIC EGGGTANATI IERIA
//
