ID   A0A1H0QIC2_9BACL        Unreviewed;       400 AA.
AC   A0A1H0QIC2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=3-oxo-5,6-didehydrosuberyl-CoA/3-oxoadipyl-CoA thiolase {ECO:0000313|EMBL:SDP16795.1};
GN   ORFNames=SAMN04487897_14210 {ECO:0000313|EMBL:SDP16795.1};
OS   Paenibacillus sp. yr247.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1761880 {ECO:0000313|EMBL:SDP16795.1, ECO:0000313|Proteomes:UP000198936};
RN   [1] {ECO:0000313|EMBL:SDP16795.1, ECO:0000313|Proteomes:UP000198936}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YR247 {ECO:0000313|EMBL:SDP16795.1,
RC   ECO:0000313|Proteomes:UP000198936};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FNIF01000042; SDP16795.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H0QIC2; -.
DR   STRING; 1761880.SAMN04487897_14210; -.
DR   OrthoDB; 9764892at2; -.
DR   Proteomes; UP000198936; 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   Reference proteome {ECO:0000313|Proteomes:UP000198936};
KW   Transferase {ECO:0000256|RuleBase:RU003557}.
FT   DOMAIN          5..267
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          275..397
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        354
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        384
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ   SEQUENCE   400 AA;  42544 MW;  E46BD8B227BF58D5 CRC64;
     MTQNVWIVDY IRTPIGRLNG GLKLVRPDDL AAHVIGKAVE RAGIDPSIID EVFMGCANQA
     GEDNRNVARM GLLLAGLPVD VPGVTVNRLC ASGLEAVNQA ARAISLGEID VAIAGGVESM
     TRSPNVMLKP EMEFGRGNQT LYDTTLGWRM VNPNFPYSME SMGETAENVA FQYEVSRQAQ
     DEFALASQQK AARAQAEGIF KEEIVPITVR DRKGKEFVVD TDEFLRPDTS LEALSKLKPA
     FKKEGSVTAG NASGLNDGAA ALLLVSERKG RELGLKPLAR YVVSASSGVD PSVMGIGPIG
     ATRKALQLAN LTVDQLDWVE LNEAFASQSI ACIQELGLDD QKVNPNGGAI AIGHPLGCSG
     ARLVGTLARQ LQRSGGRYGL ATLCIGVGQG LATIIERVDE
//