ID   C9LNB4_9FIRM            Unreviewed;       521 AA.
AC   C9LNB4;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   SubName: Full=Succinate CoA transferase {ECO:0000313|EMBL:EEW97050.1};
DE            EC=2.8.3.- {ECO:0000313|EMBL:EEW97050.1};
GN   ORFNames=GCWU000321_01034 {ECO:0000313|EMBL:EEW97050.1};
OS   Dialister invisus DSM 15470.
OC   Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC   Dialister.
OX   NCBI_TaxID=592028 {ECO:0000313|EMBL:EEW97050.1, ECO:0000313|Proteomes:UP000004736};
RN   [1] {ECO:0000313|EMBL:EEW97050.1, ECO:0000313|Proteomes:UP000004736}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15470 {ECO:0000313|EMBL:EEW97050.1,
RC   ECO:0000313|Proteomes:UP000004736};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (SEP-2009) 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:EEW97050.1}.
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DR   EMBL; ACIM02000001; EEW97050.1; -; Genomic_DNA.
DR   AlphaFoldDB; C9LNB4; -.
DR   STRING; 592028.GCWU000321_01034; -.
DR   eggNOG; COG0427; Bacteria.
DR   HOGENOM; CLU_019748_3_0_9; -.
DR   Proteomes; UP000004736; 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   Transferase {ECO:0000313|EMBL:EEW97050.1}.
FT   DOMAIN          20..237
FT                   /note="Acetyl-CoA hydrolase/transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02550"
FT   DOMAIN          338..484
FT                   /note="Acetyl-CoA hydrolase/transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13336"
FT   ACT_SITE        309
FT                   /note="5-glutamyl coenzyme A thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617821-1"
FT   BINDING         284..288
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617821-2"
FT   BINDING         399
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617821-2"
FT   BINDING         403
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617821-2"
FT   BINDING         423
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617821-2"
SQ   SEQUENCE   521 AA;  56617 MW;  7105547A3E4CD707 CRC64;
     MIVMIDINDS EFLSRIEPKE LLDKVCDGKT AAAMIQPGDI LGISGFTPCG YPKITMHELA
     ERMKQTPFQV DVWTGASTGS QIDTELVAVN GIRNRMPYQT NANLRKAINA GQINYFDLHL
     SHVAQQIREG FFTNVKGEHV TGPDFAVIEA CKIVNRDGEI GIVPTTAIGN SPVFVSQGKK
     VIIEVNTTQP VALDGMADIY EVANPPHRVP IPIVKAGDRI GKTYIPVDSA KIVAIVPCDL
     PDVTRALAPL DDDAEKMGNN LVDFLKNEVK HGRLPENLLP LQSGVGNVAN AVINGLVHSD
     FKNLSVYTEV IQDGMFDLID EGKIDMISGT SLSPSPDGLK RFHANIEKYS KKIILRPQEI
     SNNGEVARRI GVVAMNTALE MDIYGHVNST HVTGTKLMNG IGGSGDFARN GALSCFFCHS
     VAKGGAISAV VPMCSHVDHT EHDTHVFISE QGVADVRGLS PKERAKVIIN NVAHPTFRDQ
     LMDYFERACA LNGNSQTPHI LSEAFKFHTS LAETGSMLFK K
//