ID   A0A2S8WIQ7_9MICC        Unreviewed;       494 AA.
AC   A0A2S8WIQ7;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Propionyl-CoA--succinate CoA transferase {ECO:0000313|EMBL:PQZ88191.1};
GN   ORFNames=CQ018_16925 {ECO:0000313|EMBL:PQZ88191.1};
OS   Arthrobacter sp. MYb227.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1848601 {ECO:0000313|EMBL:PQZ88191.1, ECO:0000313|Proteomes:UP000239972};
RN   [1] {ECO:0000313|EMBL:PQZ88191.1, ECO:0000313|Proteomes:UP000239972}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MYb227 {ECO:0000313|EMBL:PQZ88191.1,
RC   ECO:0000313|Proteomes:UP000239972};
RA   Zimmermann J., Obeng N., Yang W., Obeng O., Kissoyan K., Pees B.,
RA   Dirksen P., Hoppner M., Franke A., Rosenstiel P., Leippe M., Dierking K.,
RA   Kaleta C., Schulenburg H.;
RT   "Genomic, metabolic, and phenotypic characteristics of bacterial isolates
RT   from the natural microbiome of the model nematode Caenorhabditis elegans.";
RL   Submitted (SEP-2017) 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:PQZ88191.1}.
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DR   EMBL; PCPT01000012; PQZ88191.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S8WIQ7; -.
DR   OrthoDB; 9801795at2; -.
DR   Proteomes; UP000239972; Unassembled WGS sequence.
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   Reference proteome {ECO:0000313|Proteomes:UP000239972};
KW   Transferase {ECO:0000313|EMBL:PQZ88191.1}.
FT   DOMAIN          2..207
FT                   /note="Acetyl-CoA hydrolase/transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02550"
FT   DOMAIN          308..454
FT                   /note="Acetyl-CoA hydrolase/transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13336"
FT   ACT_SITE        279
FT                   /note="5-glutamyl coenzyme A thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617821-1"
FT   BINDING         349
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617821-2"
FT   BINDING         369
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617821-2"
FT   BINDING         373
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617821-2"
FT   BINDING         393
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617821-2"
SQ   SEQUENCE   494 AA;  53679 MW;  AB97E54651A85B68 CRC64;
     MSAEQAASMV KPGMTVAMSG FTGAGYPKAV PGALAAMMEK EQAAGKEFKI NVLTGASTAP
     ELDGVLARAG GMDLRLPYMS DPELRRRINE GEMEYMDIHL SHVAQHAWFG FYGKIDLAVI
     EVVGITADGE LIPSSSVGNN KTWLDMADKV ILEVNTEQSA AMEGMHDIYY GTALPPHRKP
     IEMTTADQRI GQPYLRVDPE KIVAVVETNA PDRLSPFAPV DETSAQIADH LLDFLDHEIR
     AGRLTDKLLP LQSGVGNIAN AVLAGLARGG YKGLQAYTEV IQDGMLSLIK DGTIGFASAT
     SFSLSSDGID EFNEHVDFYR ERILLRPQEI SNHPELVRRL GCIALNGMIE ADIYGNVNST
     NVVGSHVMNG IGGSGDFARN GYLSVFMSPS TAKGGKISGI VPMASHVDHT EHDTMILITE
     QGLADLRGLS PKQRAQVVID KCTAPEYRPM LQDYFDRAKF GSYGKHTPHL LTESLSWHQR
     YIETGDMRTG LEIA
//