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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//