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Database: UniProt
Entry: F2LPS8_BURGS
LinkDB: F2LPS8_BURGS
Original site: F2LPS8_BURGS 
ID   F2LPS8_BURGS            Unreviewed;       504 AA.
AC   F2LPS8;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=Coenzyme A transferase {ECO:0000313|EMBL:AEA64117.1};
GN   OrderedLocusNames=bgla_2g16750 {ECO:0000313|EMBL:AEA64117.1};
OS   Burkholderia gladioli (strain BSR3).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=999541 {ECO:0000313|EMBL:AEA64117.1, ECO:0000313|Proteomes:UP000008316};
RN   [1] {ECO:0000313|EMBL:AEA64117.1, ECO:0000313|Proteomes:UP000008316}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BSR3 {ECO:0000313|EMBL:AEA64117.1,
RC   ECO:0000313|Proteomes:UP000008316};
RX   PubMed=21478339; DOI=10.1128/JB.00420-11;
RA   Seo Y.S., Lim J., Choi B.S., Kim H., Goo E., Lee B., Lim J.S., Choi I.Y.,
RA   Moon J.S., Kim J., Hwang I.;
RT   "Complete genome sequence of Burkholderia gladioli BSR3.";
RL   J. Bacteriol. 193:3149-3149(2011).
CC   -!- SIMILARITY: Belongs to the acetyl-CoA hydrolase/transferase family.
CC       {ECO:0000256|ARBA:ARBA00009632}.
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DR   EMBL; CP002600; AEA64117.1; -; Genomic_DNA.
DR   RefSeq; WP_013690444.1; NC_015376.1.
DR   AlphaFoldDB; F2LPS8; -.
DR   STRING; 999541.bgla_2g16750; -.
DR   GeneID; 66460538; -.
DR   KEGG; bgd:bgla_2g16750; -.
DR   eggNOG; COG0427; Bacteria.
DR   HOGENOM; CLU_019748_3_0_4; -.
DR   Proteomes; UP000008316; Chromosome 2.
DR   GO; GO:0008775; F:acetate CoA-transferase activity; IEA:InterPro.
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   Transferase {ECO:0000313|EMBL:AEA64117.1}.
FT   DOMAIN          14..222
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   504 AA;  54228 MW;  786446A833301979 CRC64;
     MPTSRILAES LRSLIRTADE AAALIAPNMT VAMSGFTGSG YPKAVPAALA TRISAAHARG
     EDFRINVLTG ASTAPELDGA LAKADGISMR LPYQSDPILR EKINAGELDY QDIHLSHVAQ
     YAWFGLFGDL DVAVVEVAGI REDGLLIPSA SVGNNKTWLD QAKKVILEVN TRQPLGLDGM
     HDIYYGTALP PHRKPIPLVA ADDRIGEPYL RCPAEKIIAI VETDAPDRSN AFNAPDATSK
     QIAAHLIDFL RHEIGRGRLP ANLLPLQSGV GNITNAVLAG LGEGGFTNLS AYTEVIQDGM
     LDLLANGTLS FASATALSLS PEAVKRFADD IALFRSKILL RPQEISNHPE LVRRLGCIAM
     NGMIEADIYG NVNSTHVMGT KIQNGIGGSG DFARNGYLSC FMSASTAKGG TISRIVPMAS
     HVDHTEHDVG VVVTEQGLAD LRGLSPRQRA RKIIDTCAHP DFRPMLADYF ERASRESFGK
     QTPHLLGEAL SWHERFVRTG SMKP
//
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