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Database: UniProt
Entry: A0A2N0VIU6_9BACT
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Original site: A0A2N0VIU6_9BACT 
ID   A0A2N0VIU6_9BACT        Unreviewed;       404 AA.
AC   A0A2N0VIU6;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=3-oxoadipyl-CoA thiolase {ECO:0000313|EMBL:PKD44112.1};
GN   Name=pcaF {ECO:0000313|EMBL:PKD44112.1};
GN   ORFNames=CWD77_01170 {ECO:0000313|EMBL:PKD44112.1};
OS   Rhodohalobacter barkolensis.
OC   Bacteria; Balneolota; Balneolia; Balneolales; Balneolaceae;
OC   Rhodohalobacter.
OX   NCBI_TaxID=2053187 {ECO:0000313|EMBL:PKD44112.1, ECO:0000313|Proteomes:UP000233398};
RN   [1] {ECO:0000313|EMBL:PKD44112.1, ECO:0000313|Proteomes:UP000233398}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=15182 {ECO:0000313|EMBL:PKD44112.1,
RC   ECO:0000313|Proteomes:UP000233398};
RA   Han S.;
RT   "Rhodohalobacter 15182 sp. nov., isolated from a salt lake.";
RL   Submitted (NOV-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}.
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:PKD44112.1}.
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DR   EMBL; PISP01000001; PKD44112.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N0VIU6; -.
DR   OrthoDB; 9764892at2; -.
DR   Proteomes; UP000233398; 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; 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; 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:UP000233398};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003557}.
FT   DOMAIN          8..270
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          279..403
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
FT   ACT_SITE        93
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        360
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        390
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ   SEQUENCE   404 AA;  43404 MW;  64EE59D503481A4B CRC64;
     MSDQEEAFIV DAIRTPIGNF RGSLSPVRTD DLAAHVIKSL MERNSDLDPV AINDVIMGCA
     NQAGEDNRNI ARMALLLAGL PFTVPGETVN RLCASSMSAA VHANRAIKAG DGDLFITGGV
     EHMTRGPWVI SKSSKPFGND SEMHDSSFGW RFINPKMEEL YGTDGMGNTA ENLVEKFNIS
     REDQDKFAAW SQQKAAKARE SGRLAEEIVP VEIPRRKQDP IIFDDDEFIR PTTTPEVLAK
     LRPAFKKDGS VTAGNSSGLN DGAAAMLVAS GKAVQDHNLK PMARIVSSGV AGVEPRIMGI
     GPVYASEIAL NKAGLTYDDM DIIELNEAFA AQSLACTREM GLEDDDSRIN PNGGAIALGH
     PLGMSGARIL QTAAIELQKQ SKKYALVTMC IGVGQGYAVI LERV
//
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