ID L1MXC8_9FIRM Unreviewed; 498 AA.
AC L1MXC8;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=Succinate CoA transferase {ECO:0000313|EMBL:EKX95943.1};
GN ORFNames=HMPREF9163_01931 {ECO:0000313|EMBL:EKX95943.1};
OS Selenomonas sp. oral taxon 138 str. F0429.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Selenomonas.
OX NCBI_TaxID=1127695 {ECO:0000313|EMBL:EKX95943.1, ECO:0000313|Proteomes:UP000010434};
RN [1] {ECO:0000313|EMBL:EKX95943.1, ECO:0000313|Proteomes:UP000010434}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0429 {ECO:0000313|EMBL:EKX95943.1,
RC ECO:0000313|Proteomes:UP000010434};
RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., Warren W., Mitreva M.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (MAY-2012) 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:EKX95943.1}.
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DR EMBL; AMEO01000102; EKX95943.1; -; Genomic_DNA.
DR RefSeq; WP_009441358.1; NZ_KB290947.1.
DR AlphaFoldDB; L1MXC8; -.
DR STRING; 1127695.HMPREF9163_01931; -.
DR PATRIC; fig|1127695.3.peg.1742; -.
DR eggNOG; COG0427; Bacteria.
DR HOGENOM; CLU_019748_3_0_9; -.
DR OrthoDB; 9801795at2; -.
DR Proteomes; UP000010434; 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:EKX95943.1}.
FT DOMAIN 16..202
FT /note="Acetyl-CoA hydrolase/transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02550"
FT DOMAIN 317..463
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 498 AA; 54050 MW; E84DD15B73B9874E CRC64;
MIDISDRIPK SLMDRIVSAE TAAEYFADGM TIGASGFTPS GYPKAVTLAI AERMKKNPFK
VNIWTGASTG PELDGALAEA GGIKQRLPYQ TNTPLRNAIN SGLVNYIDMH LSEVAQQSRE
GFLGKIDVAL VEAVAITEEG IIPSTSVGNT PSFIQSADVV IVEVNTSQPM ELVGMHDIYI
PLDPPNRLPI PITKAGDRIG TTFMPCPLEK IKYIVPCDIT DKTRPLAPLD DAARKMGAFT
VELLKKEIAE GRMPKGLLPL QSGVGNVANA VIAGFVNSDF TDLEVYTEVI QDGMFDLADA
GKLKFASGTA FSPSPDGLQR FYKDIDKYKK IMMLRPQEIS NNPEVVRRLG VIAMNTAIEV
DIYGNVNSTH VTGSKMMNGI GGSGDFARNA YLTIFYTQSE AKGGKISSIV PFCSHIDHGA
HDVDIIITEQ GVADLRGKSP RERALEIINN CAHPDFRPIL LDYYERALAA TKGAQTPHLL
DEALSFHQRF LATGSMQK
//
