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Database: UniProt
Entry: D4E4J0_SEROD
LinkDB: D4E4J0_SEROD
Original site: D4E4J0_SEROD 
ID   D4E4J0_SEROD            Unreviewed;       401 AA.
AC   D4E4J0;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=3-oxoadipyl-CoA thiolase {ECO:0000256|ARBA:ARBA00012233};
DE            EC=2.3.1.174 {ECO:0000256|ARBA:ARBA00012233};
GN   Name=pcaF {ECO:0000313|EMBL:EFE95399.1};
GN   ORFNames=HMPREF0758_3090 {ECO:0000313|EMBL:EFE95399.1};
OS   Serratia odorifera DSM 4582.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=667129 {ECO:0000313|EMBL:EFE95399.1, ECO:0000313|Proteomes:UP000005723};
RN   [1] {ECO:0000313|EMBL:EFE95399.1, ECO:0000313|Proteomes:UP000005723}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4582 {ECO:0000313|EMBL:EFE95399.1,
RC   ECO:0000313|Proteomes:UP000005723};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA   Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA   Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA   Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA   Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA   Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA   Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (JAN-2010) 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:EFE95399.1}.
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DR   EMBL; ADBY01000048; EFE95399.1; -; Genomic_DNA.
DR   RefSeq; WP_004961225.1; NZ_GG753567.1.
DR   AlphaFoldDB; D4E4J0; -.
DR   STRING; 667129.HMPREF0758_3090; -.
DR   HOGENOM; CLU_031026_2_2_6; -.
DR   OrthoDB; 9764638at2; -.
DR   Proteomes; UP000005723; 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|ARBA:ARBA00023315,
KW   ECO:0000256|RuleBase:RU003557};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005723};
KW   Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:EFE95399.1}.
FT   DOMAIN          5..268
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          277..400
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        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   401 AA;  42073 MW;  0E03D775E4D1AD80 CRC64;
     MSQAFICDGV RTPIGRYGGA LATVRTDDLA ALPLRALMER HPQLDWARVD DVILGCANQA
     GEDNRNLARM AALLAGLPQS VSGTTVNRLC GSGLDALAMA ARSIKAGEAG LVVAGGAESM
     TRAPLVMGKA DSAFSRQAQL YDTTLGWRFV NPLMQQRFGT DSMPETAENV AAQFSISRAD
     QDAFALRSQQ RTAHAQAAGI LAQQIVPVSI SDKKGALRVF DQDQHPRADT TLAQLQALKT
     PFRQPGSVTA GNASGLNDGA AALLVASETI AMQQGLTPRA RIVATATCGV EPRLMGIGPL
     PATRRVLEIA GLSLAQMDVI ELNEAFAAQA LAVLRQLGLP DDAEQVNPNG GAIALGHPLG
     MSGARLALAA MFELERRAGR YALCTMCIGV GQGIAMIIER V
//
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