ID   CATI_PSEKB              Reviewed;         282 AA.
AC   Q8VPF3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=3-oxoadipate CoA-transferase subunit A;
DE            EC=2.8.3.6;
DE   AltName: Full=3-oxoadipate:succinyl-CoA transferase subunit A;
DE   AltName: Full=Beta-ketoadipate:succinyl-CoA transferase subunit A;
GN   Name=catI;
OS   Pseudomonas knackmussii (strain DSM 6978 / LMG 23759 / B13).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1301098;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11741863; DOI=10.1128/jb.184.1.216-223.2002;
RA   Goebel M., Kassel-Cati K., Schmidt E., Reineke W.;
RT   "Degradation of aromatics and chloroaromatics by Pseudomonas sp. strain
RT   B13: cloning, characterization, and analysis of sequences encoding 3-
RT   oxoadipate:succinyl-coenzyme A (CoA) transferase and 3-oxoadipyl-CoA
RT   thiolase.";
RL   J. Bacteriol. 184:216-223(2002).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-31, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND SUBUNIT.
RX   PubMed=11741862; DOI=10.1128/jb.184.1.207-215.2002;
RA   Kaschabek S.R., Kuhn B., Mueller D., Schmidt E., Reineke W.;
RT   "Degradation of aromatics and chloroaromatics by Pseudomonas sp. strain
RT   B13: purification and characterization of 3-oxoadipate:succinyl-coenzyme A
RT   (CoA) transferase and 3-oxoadipyl-CoA thiolase.";
RL   J. Bacteriol. 184:207-215(2002).
CC   -!- FUNCTION: Catalyzes the CoA transfer from succinate to 3-oxoadipate
CC       (beta-ketoadipate).
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         Evidence={ECO:0000269|PubMed:11741862};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.4 mM for 3-oxoadipate {ECO:0000269|PubMed:11741862};
CC         KM=0.2 mM for succinyl-CoA {ECO:0000269|PubMed:11741862};
CC       pH dependence:
CC         Optimum pH is 8.4. {ECO:0000269|PubMed:11741862};
CC   -!- PATHWAY: Aromatic compound metabolism; beta-ketoadipate pathway;
CC       acetyl-CoA and succinyl-CoA from 3-oxoadipate: step 1/2.
CC   -!- SUBUNIT: Heterotetramer composed of 2 A and 2 B subunits.
CC       {ECO:0000269|PubMed:11741862}.
CC   -!- SIMILARITY: Belongs to the 3-oxoacid CoA-transferase subunit A family.
CC       {ECO:0000305}.
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DR   EMBL; AY044272; AAL02405.1; -; Genomic_DNA.
DR   RefSeq; WP_043252822.1; NZ_HG322950.1.
DR   AlphaFoldDB; Q8VPF3; -.
DR   SMR; Q8VPF3; -.
DR   STRING; 1301098.PKB_2952; -.
DR   eggNOG; COG1788; Bacteria.
DR   OrthoDB; 9777193at2; -.
DR   BRENDA; 2.8.3.6; 5180.
DR   SABIO-RK; Q8VPF3; -.
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; 3.30.30.40; -; 1.
DR   Gene3D; 3.40.1080.10; Glutaconate Coenzyme A-transferase; 1.
DR   InterPro; IPR004165; CoA_trans_fam_I.
DR   InterPro; IPR037171; NagB/RpiA_transferase-like.
DR   Pfam; PF01144; CoA_trans; 1.
DR   SMART; SM00882; CoA_trans; 1.
DR   SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 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:11741862"
FT   CHAIN           2..282
FT                   /note="3-oxoadipate CoA-transferase subunit A"
FT                   /id="PRO_0000337673"
SQ   SEQUENCE   282 AA;  30973 MW;  EFC6A128C8F8CB34 CRC64;
     MAELLTLREA VERFVNDGDT VALEGFTHLI PTAASHEIIR QGKKDLHLVR MTPDLVYDLL
     IGAGCARKLT FSWGGNPGVG SLHRLRDAVE KGWPNALEID EHSHADLANS YVAGASGLPF
     AVLRAYAGSD LPKVNPNIKF INCPFTGEQL AAVPSVRPDV TVIHAQKADR KGNVLLWGIL
     GVQKEAALAA KRCIVTVEEI VDDLNAPMNS CVLPTWALSA VCHVPGGSHP SYAHGYYERD
     NRFYQAWDPI ARDRETFTAW IDEYIRGTKD FSEFQAKIAE GK
//