ID A0A0S8B2H8_9PROT Unreviewed; 402 AA.
AC A0A0S8B2H8;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Beta-ketoadipyl CoA thiolase {ECO:0000313|EMBL:KPK05800.1};
GN ORFNames=AMJ64_10775 {ECO:0000313|EMBL:KPK05800.1};
OS Betaproteobacteria bacterium SG8_39.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1703390 {ECO:0000313|EMBL:KPK05800.1, ECO:0000313|Proteomes:UP000051483};
RN [1] {ECO:0000313|EMBL:KPK05800.1, ECO:0000313|Proteomes:UP000051483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_39 {ECO:0000313|EMBL:KPK05800.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPK05800.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LJTQ01000105; KPK05800.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8B2H8; -.
DR STRING; 1703390.AMJ64_10775; -.
DR PATRIC; fig|1703390.3.peg.3223; -.
DR Proteomes; UP000051483; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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; IPR020615; Thiolase_acyl_enz_int_AS.
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; PTHR43853; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 1.
DR PANTHER; PTHR43853:SF2; 3-OXOADIPYL-COA_3-OXO-5,6-DEHYDROSUBERYL-COA THIOLASE; 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; PS00098; THIOLASE_1; 1.
DR PROSITE; PS00737; THIOLASE_2; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW Transferase {ECO:0000256|RuleBase:RU003557}.
FT DOMAIN 5..267
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 278..400
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 89
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 357
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 387
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 402 AA; 42340 MW; 64C96B3A6242EF9C CRC64;
MLDAYIYDGL RSPIGRHAGK LAPVRPDDLA GEVIKEVVAR NQIAPEEISD VVLGCVTQAG
EDCRNVARFA ALLSGLPPTV PGVTVNRLCA SGLQAVTDAA RAITCAEGEL YIAGGVESMT
RAPYVMGKAD SPYSRGVKMY DTTIGSRFTN PRFAKQYGDH AMPQTGDNVA KDFGITREEA
DAFALASQQK YAKAEQEGFY KGEILPITLP AKKKDAAPES VERDEHPRRD ATMEALAKLK
PLFEGGVVTA GNASGVNDGA AALVVGSRAW GEKKSKAPLV RIRAAASAAV EPRIMGVGPA
YAIPLALERA GLALKDMDII EINEAFASQV LGCLKLLKVD FKDPRVNPNG GAIAIGHPLG
CSGARLALTV AREMQQSGAR YAAVSLCIGV GQGLAVILEK LN
//
