ID   Q1IGV1_PSEE4            Unreviewed;       497 AA.
AC   Q1IGV1;
DT   13-JUN-2006, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2006, sequence version 1.
DT   27-MAR-2024, entry version 85.
DE   SubName: Full=Putative acetyl-CoA hydrolase/transferase {ECO:0000313|EMBL:CAK13101.1};
DE            EC=3.1.2.1 {ECO:0000313|EMBL:CAK13101.1};
GN   OrderedLocusNames=PSEEN0113 {ECO:0000313|EMBL:CAK13101.1};
OS   Pseudomonas entomophila (strain L48).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=384676 {ECO:0000313|EMBL:CAK13101.1, ECO:0000313|Proteomes:UP000000658};
RN   [1] {ECO:0000313|EMBL:CAK13101.1, ECO:0000313|Proteomes:UP000000658}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L48 {ECO:0000313|EMBL:CAK13101.1,
RC   ECO:0000313|Proteomes:UP000000658};
RX   PubMed=16699499; DOI=10.1038/nbt1212;
RA   Vodovar N., Vallenet D., Cruveiller S., Rouy Z., Barbe V., Acosta C.,
RA   Cattolico L., Jubin C., Lajus A., Segurens B., Vacherie B., Wincker P.,
RA   Weissenbach J., Lemaitre B., Medigue C., Boccard F.;
RT   "Complete genome sequence of the entomopathogenic and metabolically
RT   versatile soil bacterium Pseudomonas entomophila.";
RL   Nat. Biotechnol. 24:673-679(2006).
CC   -!- SIMILARITY: Belongs to the acetyl-CoA hydrolase/transferase family.
CC       {ECO:0000256|ARBA:ARBA00009632}.
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DR   EMBL; CT573326; CAK13101.1; -; Genomic_DNA.
DR   RefSeq; WP_011531562.1; NC_008027.1.
DR   AlphaFoldDB; Q1IGV1; -.
DR   STRING; 384676.PSEEN0113; -.
DR   GeneID; 32803474; -.
DR   KEGG; pen:PSEEN0113; -.
DR   eggNOG; COG0427; Bacteria.
DR   HOGENOM; CLU_019748_3_0_6; -.
DR   OrthoDB; 9801795at2; -.
DR   Proteomes; UP000000658; Chromosome.
DR   GO; GO:0008775; F:acetate CoA-transferase activity; IEA:InterPro.
DR   GO; GO:0003986; F:acetyl-CoA hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006083; P:acetate metabolic process; IEA:InterPro.
DR   GO; GO:0006084; P:acetyl-CoA metabolic process; IEA:InterPro.
DR   Gene3D; 3.30.750.70; 4-hydroxybutyrate coenzyme like domains; 1.
DR   Gene3D; 3.40.1080.20; Acetyl-CoA hydrolase/transferase C-terminal domain; 1.
DR   Gene3D; 3.40.1080.10; Glutaconate Coenzyme A-transferase; 1.
DR   InterPro; IPR026888; AcetylCoA_hyd_C.
DR   InterPro; IPR038460; AcetylCoA_hyd_C_sf.
DR   InterPro; IPR046433; ActCoA_hydro.
DR   InterPro; IPR003702; ActCoA_hydro_N.
DR   InterPro; IPR037171; NagB/RpiA_transferase-like.
DR   InterPro; IPR017821; Succinate_CoA_transferase.
DR   NCBIfam; TIGR03458; YgfH_subfam; 1.
DR   PANTHER; PTHR43609; ACETYL-COA HYDROLASE; 1.
DR   PANTHER; PTHR43609:SF1; ACETYL-COA HYDROLASE; 1.
DR   Pfam; PF13336; AcetylCoA_hyd_C; 1.
DR   Pfam; PF02550; AcetylCoA_hydro; 1.
DR   SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 2.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:CAK13101.1};
KW   Transferase {ECO:0000313|EMBL:CAK13101.1}.
FT   DOMAIN          11..215
FT                   /note="Acetyl-CoA hydrolase/transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02550"
FT   DOMAIN          322..463
FT                   /note="Acetyl-CoA hydrolase/transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13336"
FT   ACT_SITE        288
FT                   /note="5-glutamyl coenzyme A thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617821-1"
FT   BINDING         378
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617821-2"
FT   BINDING         382
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617821-2"
FT   BINDING         402
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617821-2"
SQ   SEQUENCE   497 AA;  53761 MW;  87EF055611AEB5BE CRC64;
     MYRDRIRLSS LHSKVMSAAD AAGLIQDGMT VGMSGFTRAG EAKAVPHALA ERAKQSPLKI
     SLMTGASLGN DLDKQLTEAG VLARRMPFQV DSTLRKAIND GKVMFIDQHL SETVEQLRNK
     QLTLPDIAVI EAVAITEQGH IVPTTSVGNS ASFAIFAKQV IVEINLSHNA NLEGLHDIYI
     PTYRPTRTPI PLVKVDDRIG STAIPIDPAK IVGIVISDQP DSPSTVLPPD HETQGIADHL
     IAFLKGEVDA GRMSNNLGPL QAGIGSIANA VMCGLIESPF ENLTMYSEVL QDSTFDLIDA
     GKLSFASGSS ITLSSRRNAD VFGNLERYKD KLVLRPQEIS NHPEVVRRLG IIGINTALEF
     DIYGNVNSTH VCGTKMMNGI GGSGDFARNA HLAIFVTKSI AKGGAISSVV PMVSHVDHTE
     HDVDILVTEV GLADLRGLAP RERARVIIDN CVHPDYRAAL NDYFERACQR GGHTPHILRE
     ALSWHENLEE TGRMLVG
//