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Database: UniProt
Entry: G7VAF2_THELD
LinkDB: G7VAF2_THELD
Original site: G7VAF2_THELD 
ID   G7VAF2_THELD            Unreviewed;       503 AA.
AC   G7VAF2;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=Succinate CoA transferase {ECO:0000313|EMBL:AER67602.1};
DE            EC=3.1.2.1 {ECO:0000313|EMBL:AER67602.1};
GN   OrderedLocusNames=Tlie_1893 {ECO:0000313|EMBL:AER67602.1};
OS   Thermovirga lienii (strain ATCC BAA-1197 / DSM 17291 / Cas60314).
OG   Plasmid pTLIE01 {ECO:0000313|EMBL:AER67602.1,
OG   ECO:0000313|Proteomes:UP000005868}.
OC   Bacteria; Synergistota; Synergistia; Synergistales; Thermovirgaceae;
OC   Thermovirga.
OX   NCBI_TaxID=580340 {ECO:0000313|EMBL:AER67602.1, ECO:0000313|Proteomes:UP000005868};
RN   [1] {ECO:0000313|EMBL:AER67602.1, ECO:0000313|Proteomes:UP000005868}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1197 / DSM 17291 / Cas60314
RC   {ECO:0000313|Proteomes:UP000005868};
RC   PLASMID=Plasmid pTLIE01 {ECO:0000313|Proteomes:UP000005868};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Saunders E.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Last F.I., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA   Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M., Brambilla E.-M.,
RA   Klenk H.-P., Eisen J.A.;
RT   "The complete genome of plasmid of Thermovirga lienii DSM 17291.";
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the acetyl-CoA hydrolase/transferase family.
CC       {ECO:0000256|ARBA:ARBA00009632}.
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DR   EMBL; CP003097; AER67602.1; -; Genomic_DNA.
DR   RefSeq; WP_014164005.1; NC_016149.1.
DR   AlphaFoldDB; G7VAF2; -.
DR   KEGG; tli:Tlie_1893; -.
DR   eggNOG; COG0427; Bacteria.
DR   HOGENOM; CLU_019748_3_0_0; -.
DR   OrthoDB; 9801795at2; -.
DR   Proteomes; UP000005868; Plasmid pTLIE01.
DR   GO; GO:0008775; F:acetate CoA-transferase activity; IEA:InterPro.
DR   GO; GO:0003986; F:acetyl-CoA hydrolase activity; IEA:UniProtKB-EC.
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:AER67602.1};
KW   Plasmid {ECO:0000313|EMBL:AER67602.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005868};
KW   Transferase {ECO:0000313|EMBL:AER67602.1}.
FT   DOMAIN          12..217
FT                   /note="Acetyl-CoA hydrolase/transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02550"
FT   DOMAIN          322..465
FT                   /note="Acetyl-CoA hydrolase/transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13336"
FT   ACT_SITE        290
FT                   /note="5-glutamyl coenzyme A thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617821-1"
FT   BINDING         265..269
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617821-2"
FT   BINDING         360
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617821-2"
FT   BINDING         380
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         404
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617821-2"
SQ   SEQUENCE   503 AA;  55853 MW;  33F6D02C32942951 CRC64;
     MELHERIRSK VLREKVVSKE EAAKFIKDGM TVACSGFTPA GYPKVVPEMI AQRAQKGENI
     RLNIITGAST GDELDGVLAR SGVIKKRYPY QTNTDCRNGI NSGQIDFCDI HLSHLPQFIK
     LGYLGNIDIA LVEAVAITED GGIVPSTSVG ATNTFVQKAD KVIVEINFAQ PLDLEGLHDI
     YDPGDPPLRS PIPLCRVSDR IGIPYIPCPK EKIVAIVISN RKDSTNPVAE IDRDSRLIAG
     HIIDFLEFEI KKGRFPKNLL PLQSGVGSVA NAVLTNFKES RFENLEIYSE VLQDAVLELI
     DTGKVSFASG TAFTISPSKL DHFYKNLKFY KNYTILRPQE ISNNPEVIRR LGVIAMNTAI
     EIDIYGNVNS THIGGCAMMN GIGGSGDFTR NAALSIFTTK SVAKDGNISS IVPMVSHHDH
     TEHDVHVVVT EQGLADLRGL SPKERVKQII GKCAHPDFRK ELWDYYRKAL FYAKYKHTPH
     MLNRVFDLHN YMVKYGTMKP KVC
//
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