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Database: UniProt
Entry: A0A0R0AU73_9GAMM
LinkDB: A0A0R0AU73_9GAMM
Original site: A0A0R0AU73_9GAMM 
ID   A0A0R0AU73_9GAMM        Unreviewed;       505 AA.
AC   A0A0R0AU73;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Acetyl-CoA hydrolase {ECO:0000313|EMBL:KRG44184.1};
GN   ORFNames=ARC20_08570 {ECO:0000313|EMBL:KRG44184.1};
OS   Stenotrophomonas panacihumi.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas.
OX   NCBI_TaxID=676599 {ECO:0000313|EMBL:KRG44184.1, ECO:0000313|Proteomes:UP000051802};
RN   [1] {ECO:0000313|EMBL:KRG44184.1, ECO:0000313|Proteomes:UP000051802}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 16536 {ECO:0000313|EMBL:KRG44184.1,
RC   ECO:0000313|Proteomes:UP000051802};
RA   Patil P.P., Midha S., Patil P.B.;
RT   "Genome sequencing and analysis of members of genus Stenotrophomonas.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the acetyl-CoA hydrolase/transferase family.
CC       {ECO:0000256|ARBA:ARBA00009632}.
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:KRG44184.1}.
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DR   EMBL; LLXU01000069; KRG44184.1; -; Genomic_DNA.
DR   RefSeq; WP_057646181.1; NZ_PZOY01000001.1.
DR   AlphaFoldDB; A0A0R0AU73; -.
DR   STRING; 676599.ARC20_08570; -.
DR   OrthoDB; 9801795at2; -.
DR   Proteomes; UP000051802; Unassembled WGS sequence.
DR   GO; GO:0008775; F:acetate CoA-transferase activity; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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:KRG44184.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051802}.
FT   DOMAIN          15..221
FT                   /note="Acetyl-CoA hydrolase/transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02550"
FT   DOMAIN          335..469
FT                   /note="Acetyl-CoA hydrolase/transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13336"
FT   ACT_SITE        294
FT                   /note="5-glutamyl coenzyme A thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617821-1"
FT   BINDING         364
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617821-2"
FT   BINDING         384
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617821-2"
FT   BINDING         388
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617821-2"
FT   BINDING         408
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617821-2"
SQ   SEQUENCE   505 AA;  55148 MW;  4DE7C20D8D6D6F5B CRC64;
     MTAERILHPR LRDRVVSAEA AAAWIAPGET VAMSGFTGSG YPKAVPIALA QQIETAHQAG
     QPFQIKLMTG ASTAPELDGA LAKADGIALR MPFQTDPDAR ARINAGKLDY IDIHLSHVAQ
     HVWFGFYGEI DTAVIEVTAI REDGSLVPST SVGNNKTWLD LAKKIIIEVN EWQPADIDGM
     HDIYYGTALP PHRKPIPLVH GDDRIGQTTL NCDLDKVVAV VRTNGPDRNS PFTPADETSE
     RIAGHLIEFL KHEVARGRLP ANLLPLQSGV GNIPNAVLAG LANSGFRDLE AFTEVIQDGM
     LDLLKSGVLR YASCTGFALS PAANEEFKRN IAFYRERIVM RTQEISNHPE LVRRLGCIGM
     NGMIEADLYG NVNSTHVMGS RIMNGIGGSG DFARNGFLSA FLSPSTAKNG TISSIVPMVS
     HVDHTEHDVA VVVTEQGLAD LRGLTPKQRA RVVIDHCVHP DYRAQLEDYF DRACRDAYGK
     HTPHLLPEAL SWHQRWLDTG TMREG
//
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