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Database: UniProt
Entry: E1IM18_ECOLX
LinkDB: E1IM18_ECOLX
Original site: E1IM18_ECOLX 
ID   E1IM18_ECOLX            Unreviewed;       492 AA.
AC   E1IM18;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   SubName: Full=Succinate CoA transferase {ECO:0000313|EMBL:EFO59662.1};
DE            EC=2.8.3.- {ECO:0000313|EMBL:EFO59662.1};
GN   ORFNames=HMPREF9348_01169 {ECO:0000313|EMBL:EFO59662.1};
OS   Escherichia coli MS 145-7.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=679204 {ECO:0000313|EMBL:EFO59662.1, ECO:0000313|Proteomes:UP000003691};
RN   [1] {ECO:0000313|EMBL:EFO59662.1, ECO:0000313|Proteomes:UP000003691}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MS 145-7 {ECO:0000313|EMBL:EFO59662.1,
RC   ECO:0000313|Proteomes:UP000003691};
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 (AUG-2010) 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:EFO59662.1}.
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DR   EMBL; ADWS01000004; EFO59662.1; -; Genomic_DNA.
DR   RefSeq; WP_000449941.1; NZ_ADWS01000004.1.
DR   AlphaFoldDB; E1IM18; -.
DR   GeneID; 75173022; -.
DR   Proteomes; UP000003691; 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:EFO59662.1}.
FT   DOMAIN          1..213
FT                   /note="Acetyl-CoA hydrolase/transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02550"
FT   DOMAIN          317..461
FT                   /note="Acetyl-CoA hydrolase/transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13336"
FT   ACT_SITE        286
FT                   /note="5-glutamyl coenzyme A thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617821-1"
FT   BINDING         376
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         400
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617821-2"
SQ   SEQUENCE   492 AA;  53855 MW;  2C252973430AB2B0 CRC64;
     METQWTRMTA DEAAEIIQHN DMVAFSGFTP AGSPKALPTA IARRANEQHE AKKPYQIRLL
     TGASISAAAD DVLSDADAVS WRAPYQTSSG LRKKINQGAV SFVDLHLSEV AQMVNYGFFG
     DIDVAVIEAS ALAPDGRVWL TSGIGNAPTW LLRAKKVIIE LNHYHDPRVA ELADIVIPGA
     PPRRNSVSIF HAMDRVGTRY VQIDPKKIVA VVETNLPDAG NMLDKQNPMC QQIADNVVTF
     LLQEMAHGRI PPEFLPLQSG VGNINNAVMA RLGENPEIPP FMMYSEVLQE SVVHLLETGK
     ISGASASSLT ISADSLRKIY DNMDYFASRI VLRPQEISNN PEIIRRLGVI ALNVGLEFDI
     YGHANSTHVA GVDLMNGIGG SGDFERNAYL SIFMAPSIAK EGKISTVVPM CSHVDHSEHS
     VKVIITEQGI ADLRGLSPLQ RARTIIDNCA HPMYRDYLHR YLENAPGGHI HHDLSHVFDL
     HRNLIATGSM LG
//
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