ID E8LEL0_9FIRM Unreviewed; 512 AA.
AC E8LEL0;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=Succinate CoA transferase {ECO:0000313|EMBL:EFY04735.1};
DE EC=2.8.3.- {ECO:0000313|EMBL:EFY04735.1};
GN ORFNames=HMPREF9443_01294 {ECO:0000313|EMBL:EFY04735.1};
OS Phascolarctobacterium succinatutens YIT 12067.
OC Bacteria; Bacillota; Negativicutes; Acidaminococcales; Acidaminococcaceae;
OC Phascolarctobacterium.
OX NCBI_TaxID=626939 {ECO:0000313|EMBL:EFY04735.1, ECO:0000313|Proteomes:UP000004923};
RN [1] {ECO:0000313|EMBL:EFY04735.1, ECO:0000313|Proteomes:UP000004923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIT 12067 {ECO:0000313|EMBL:EFY04735.1,
RC ECO:0000313|Proteomes:UP000004923};
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., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (JAN-2011) 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:EFY04735.1}.
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DR EMBL; AEVN01000052; EFY04735.1; -; Genomic_DNA.
DR RefSeq; WP_009145653.1; NZ_GL830888.1.
DR AlphaFoldDB; E8LEL0; -.
DR eggNOG; COG0427; Bacteria.
DR HOGENOM; CLU_019748_3_0_9; -.
DR OrthoDB; 9801795at2; -.
DR Proteomes; UP000004923; 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:UP000004923};
KW Transferase {ECO:0000313|EMBL:EFY04735.1}.
FT DOMAIN 15..225
FT /note="Acetyl-CoA hydrolase/transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02550"
FT DOMAIN 327..472
FT /note="Acetyl-CoA hydrolase/transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13336"
FT ACT_SITE 297
FT /note="5-glutamyl coenzyme A thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR617821-1"
FT BINDING 272..276
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|PIRSR:PIRSR617821-2"
FT BINDING 367
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|PIRSR:PIRSR617821-2"
FT BINDING 387
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|PIRSR:PIRSR617821-2"
FT BINDING 391
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|PIRSR:PIRSR617821-2"
FT BINDING 411
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|PIRSR:PIRSR617821-2"
SQ SEQUENCE 512 AA; 55436 MW; 1FB30317C9CC06E7 CRC64;
MIDIKDRICD VVADKVMSAE AAAEFVKDGD NLGVSGFTPS GYPKAVPLAL AEKGKKTPFK
VNVWTGASVG PEIDQAMVEA GIIDRRLPYQ TNGTMRKAIN AGKVKYADIH LSHMAQMVRY
GFMAGRPTGP DVAIVEVCKI NDLGDGKVGL IPTTSMGNSS SYVAGAKKVI VEVNTTQPVG
LEGMHDSYVP LDPPYRKAIP IEKPEDRIGT TYIPCEVDKI VAVVPCDITD KVRPLGEIDE
DAKHMGANLV NFLKNEVKEG RLPKNLLPLQ SGVGSVANAV INGLVNSDFE DLTVYTEVIQ
DGMFDLIDAG KLRVASGTAL TPPPECQKKF YENVEHYKKY LLLRPQEISN SPEVARRIGV
IAMNTAIEVD IYGNVNSTHV CGTKLMNGVG GSGDFARNGY LTVFFTNSLA KGGKISSVVP
FCSHIDHATL DVDVIVSERG VADLRGLSPK EKAPIIIDQI ANPKYQPWLY DYFKRACEAC
GNSQTPHILS EAFDCYKLFA ETGSMEGMVE GK
//
