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Database: UniProt
Entry: A0A3N1AQA0_9ACTN
LinkDB: A0A3N1AQA0_9ACTN
Original site: A0A3N1AQA0_9ACTN 
ID   A0A3N1AQA0_9ACTN        Unreviewed;       401 AA.
AC   A0A3N1AQA0;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=3-oxoadipyl-CoA thiolase {ECO:0000256|ARBA:ARBA00012233};
DE            EC=2.3.1.174 {ECO:0000256|ARBA:ARBA00012233};
GN   ORFNames=EDC02_0546 {ECO:0000313|EMBL:ROO58778.1};
OS   Micromonospora sp. Llam0.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=2485143 {ECO:0000313|EMBL:ROO58778.1, ECO:0000313|Proteomes:UP000275308};
RN   [1] {ECO:0000313|EMBL:ROO58778.1, ECO:0000313|Proteomes:UP000275308}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Llam0 {ECO:0000313|EMBL:ROO58778.1,
RC   ECO:0000313|Proteomes:UP000275308};
RA   D'Agostino P.;
RT   "Genome mining of underrepresented organisms for secondary metabolites.";
RL   Submitted (NOV-2018) 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}.
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:ROO58778.1}.
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DR   EMBL; RJJY01000001; ROO58778.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N1AQA0; -.
DR   OrthoDB; 5167532at2; -.
DR   Proteomes; UP000275308; Unassembled WGS sequence.
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:ROO58778.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000275308};
KW   Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:ROO58778.1}.
FT   DOMAIN          5..266
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;  41050 MW;  C90B8334E2F3B3EE CRC64;
     MPVAYLVAGV RTPFGRYAGA LAPVRPDDLA AHVIRELVAR HPSVDWDAVD DVVLGCANQA
     GEDNRNVARM AALLAGLPTG TSGTTVNRLC GSGLDAVAIA ARSVVAGEAD LVVAGGVESM
     SRAPFVLPKA ATAYGRTAEI HDTTIGWRLV NPLMRAGWGT DSMPETAENV AAEYGVERAA
     QDTFALRSQQ RAAQAQGSGR LAAEIVPIEV PQGRKGTVTV SVDEHPRQTS LEKLAALPTP
     FRADGTVTAG NSSGVNDGAV ALLVASDAAV RRYGLTPLAR VAGAATAGVE PRVMGIGPVP
     ATRRLLGRLG VELSEVDVVE LNEAFAAQAV AVLRELGLPA EAEHVNPNGG AIALGHPLGA
     SGARLALTAA LELGVRDADR ALCTMCIGVG QGISLLLESA S
//
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