ID   PCAJ_PSEPU              Reviewed;         213 AA.
AC   P0A102; Q01104;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 67.
DE   RecName: Full=3-oxoadipate CoA-transferase subunit B;
DE            EC=2.8.3.6;
DE   AltName: Full=Beta-ketoadipate:succinyl-CoA transferase subunit B;
GN   Name=pcaJ;
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=PRS2000;
RX   PubMed=1624453; DOI=10.1128/jb.174.14.4657-4666.1992;
RA   Parales R.E., Harwood C.S.;
RT   "Characterization of the genes encoding beta-ketoadipate: succinyl-coenzyme
RT   A transferase in Pseudomonas putida.";
RL   J. Bacteriol. 174:4657-4666(1992).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-7.
RX   PubMed=6780551; DOI=10.1016/s0021-9258(19)69841-8;
RA   Yeh W.-K., Ornston L.N.;
RT   "Evolutionarily homologous alpha 2 beta 2 oligomeric structures in beta-
RT   ketoadipate succinyl-CoA transferases from Acinetobacter calcoaceticus and
RT   Pseudomonas putida.";
RL   J. Biol. Chem. 256:1565-1569(1981).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-oxoadipate + succinyl-CoA = 3-oxoadipyl-CoA + succinate;
CC         Xref=Rhea:RHEA:12048, ChEBI:CHEBI:15775, ChEBI:CHEBI:30031,
CC         ChEBI:CHEBI:57292, ChEBI:CHEBI:57348; EC=2.8.3.6;
CC   -!- PATHWAY: Aromatic compound metabolism; beta-ketoadipate pathway;
CC       acetyl-CoA and succinyl-CoA from 3-oxoadipate: step 1/2.
CC   -!- SUBUNIT: Heterodimer.
CC   -!- SIMILARITY: Belongs to the 3-oxoacid CoA-transferase subunit B family.
CC       {ECO:0000305}.
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DR   EMBL; M88763; AAA25923.1; -; Genomic_DNA.
DR   PIR; B42985; B42985.
DR   RefSeq; WP_003251131.1; NZ_WOWR01000003.1.
DR   AlphaFoldDB; P0A102; -.
DR   SMR; P0A102; -.
DR   GeneID; 83679430; -.
DR   OMA; ANWHTGE; -.
DR   BioCyc; MetaCyc:MONOMER-3191; -.
DR   BRENDA; 2.8.3.6; 5092.
DR   UniPathway; UPA00157; UER00262.
DR   GO; GO:0047569; F:3-oxoadipate CoA-transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042952; P:beta-ketoadipate pathway; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.1080.10; Glutaconate Coenzyme A-transferase; 1.
DR   InterPro; IPR012791; 3-oxoacid_CoA-transf_B.
DR   InterPro; IPR004165; CoA_trans_fam_I.
DR   InterPro; IPR004164; CoA_transf_AS.
DR   InterPro; IPR037171; NagB/RpiA_transferase-like.
DR   NCBIfam; TIGR02428; pcaJ_scoB_fam; 1.
DR   PANTHER; PTHR13707; KETOACID-COENZYME A TRANSFERASE; 1.
DR   PANTHER; PTHR13707:SF59; SUCCINYL-COA:3-KETOACID COENZYME A TRANSFERASE SUBUNIT B-RELATED; 1.
DR   Pfam; PF01144; CoA_trans; 1.
DR   SMART; SM00882; CoA_trans; 1.
DR   SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 1.
DR   PROSITE; PS01274; COA_TRANSF_2; 1.
PE   1: Evidence at protein level;
KW   Aromatic hydrocarbons catabolism; Direct protein sequencing; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:6780551"
FT   CHAIN           2..213
FT                   /note="3-oxoadipate CoA-transferase subunit B"
FT                   /id="PRO_0000157919"
FT   ACT_SITE        50
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10034"
SQ   SEQUENCE   213 AA;  22552 MW;  5071B33173AD8B7B CRC64;
     MTITKKLSRT EMAQRVAADI QEGAYVNLGI GAPTLVANYL GDKEVFLHSE NGLLGMGPSP
     APGEEDDDLI NAGKQHVTLL TGGAFFHHAD SFSMMRGGHL DIAVLGAFQV SVKGDLANWH
     TGAEGSIPAV GGAMDLATGA RQVFVMMDHL TKTGESKLVP ECTYPLTGIA CVSRIYTDLA
     VLEVTPEGLK VVEICADIDF DELQKLSGVP LIK
//