ID   A0A1N7EYM1_9ACTN        Unreviewed;       401 AA.
AC   A0A1N7EYM1;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=3-oxoadipyl-CoA thiolase {ECO:0000256|ARBA:ARBA00012233};
DE            EC=2.3.1.174 {ECO:0000256|ARBA:ARBA00012233};
GN   ORFNames=SAMN05444858_12859 {ECO:0000313|EMBL:SIR93189.1};
OS   Micromonospora avicenniae.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=1198245 {ECO:0000313|EMBL:SIR93189.1, ECO:0000313|Proteomes:UP000186004};
RN   [1] {ECO:0000313|EMBL:SIR93189.1, ECO:0000313|Proteomes:UP000186004}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45758 {ECO:0000313|EMBL:SIR93189.1,
RC   ECO:0000313|Proteomes:UP000186004};
RA   Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + succinyl-CoA = 3-oxoadipyl-CoA + CoA;
CC         Xref=Rhea:RHEA:19481, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:57292, ChEBI:CHEBI:57348; EC=2.3.1.174;
CC         Evidence={ECO:0000256|ARBA:ARBA00000708};
CC   -!- PATHWAY: Aromatic compound metabolism. {ECO:0000256|ARBA:ARBA00005211}.
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; FTNF01000028; SIR93189.1; -; Genomic_DNA.
DR   RefSeq; WP_076473712.1; NZ_FTNF01000028.1.
DR   AlphaFoldDB; A0A1N7EYM1; -.
DR   STRING; 1198245.SAMN05444858_12859; -.
DR   OrthoDB; 5167532at2; -.
DR   Proteomes; UP000186004; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0033812; F:3-oxoadipyl-CoA thiolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019619; P:3,4-dihydroxybenzoate catabolic process; IEA:InterPro.
DR   CDD; cd00751; thiolase; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   InterPro; IPR012793; PcaF.
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   NCBIfam; TIGR02430; pcaF; 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   ECO:0000313|EMBL:SIR93189.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186004};
KW   Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:SIR93189.1}.
FT   DOMAIN          5..267
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          275..398
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        356
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        386
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ   SEQUENCE   401 AA;  41630 MW;  1A8BF1040CDA9F5B CRC64;
     MTVAYLVAGV RTPIGRYGGV LAGVRPDDLA AHVIRELVDR HRTVDWERVD DVILGCANQA
     GEDNRNVARM AALLGGLPEQ VPGSTVNRLC GSGLDALATA ARAIVAGEAE LIVAGGVESM
     SRAPFVMPKA GTAYSRAAEI YDTTIGWRLV NPLMKKQWGI DSMPETAENV AAEFGVDRAA
     QDGFALRSQQ RAAKAQADGR LAEEIVPVTV PAGKRETKQV DTDEHPRETS LEKLAALPTP
     FREGGTVTAG NSSGVNDGAV ALLVASEAAV DRYALTPLAR VTGAAAAGVP PRIMGVGPVP
     ATRKLLDRLG LGLGDVDVIE LNEAFAAQSV AVLRELGLPE DAEHVNPNGG AIALGHPLGA
     SGARLALTAA LELRRRGGRR ALATMCIGVG QGISLMMESA A
//