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Database: UniProt
Entry: A0A3P3W7C9_9FLAO
LinkDB: A0A3P3W7C9_9FLAO
Original site: A0A3P3W7C9_9FLAO 
ID   A0A3P3W7C9_9FLAO        Unreviewed;       504 AA.
AC   A0A3P3W7C9;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Succinate CoA transferase {ECO:0000313|EMBL:RRJ91085.1};
GN   ORFNames=EG849_09085 {ECO:0000313|EMBL:RRJ91085.1};
OS   Flavobacterium macacae.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=2488993 {ECO:0000313|EMBL:RRJ91085.1, ECO:0000313|Proteomes:UP000271937};
RN   [1] {ECO:0000313|EMBL:RRJ91085.1, ECO:0000313|Proteomes:UP000271937}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIM 102600 {ECO:0000313|EMBL:RRJ91085.1,
RC   ECO:0000313|Proteomes:UP000271937};
RA   Li G., Jiang Y.;
RT   "Flavobacterium sp. nov., YIM 102600 draft genome.";
RL   Submitted (NOV-2018) 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:RRJ91085.1}.
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DR   EMBL; RQVR01000009; RRJ91085.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3P3W7C9; -.
DR   OrthoDB; 9801795at2; -.
DR   Proteomes; UP000271937; 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:UP000271937};
KW   Transferase {ECO:0000313|EMBL:RRJ91085.1}.
FT   DOMAIN          9..215
FT                   /note="Acetyl-CoA hydrolase/transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02550"
FT   DOMAIN          329..464
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         263..267
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617821-2"
FT   BINDING         358
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617821-2"
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   504 AA;  55590 MW;  D30D3A66EEF1E1BB CRC64;
     MHSERIQFQN YEEKVISAHE ASLFFKDKMT VGTSGFTKAG DSKAVLPAFA ERAKEEEIAI
     TLITGASLGH TTDADLAQNN ALYKRMPFQV DPTLRKKIND GSILFVDQHL SETVELLENK
     HLPKMDLAVL EAAYIDENGN IIPTTSVGNS VTFAHLAEKI IIEINLSIPM NFKGIHDIYL
     PEPYPNRKPL DITASSERIG QDFISIDPQK VIGVVFTEIP DSPAQVVAPD EKTTAIAGHL
     LAFFEKEIAD GRLTKSLLPL QAGIGKVANA VMSGLGKGDF ENLEMYSEVL QDSTFELIDS
     GKMNFASASS LTVSQNCYAH ILNNFELYKD KILLRPQQIS NSAEVIRRLG IIAINTAIEF
     DIYGNVNSTH LGGTKMMNGI GGSGDFARNA YLSIFVTQSA SKEDNAISHV LPMVSHVDHT
     EHDVDILVTD QGLADLRGLA PRERAQVIIN NCVHPDYKET LQHYFERASE RGGHTPHILE
     EAFAMHTRFN QTGTMKELVL EELA
//
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