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Database: UniProt
Entry: A0A101HDA6_9FIRM
LinkDB: A0A101HDA6_9FIRM
Original site: A0A101HDA6_9FIRM 
ID   A0A101HDA6_9FIRM        Unreviewed;       491 AA.
AC   A0A101HDA6;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Succinate CoA transferase {ECO:0000313|EMBL:KUK74115.1};
GN   ORFNames=XD91_0163 {ECO:0000313|EMBL:KUK74115.1};
OS   Clostridiales bacterium 38_11.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales.
OX   NCBI_TaxID=1641393 {ECO:0000313|EMBL:KUK74115.1, ECO:0000313|Proteomes:UP000053314};
RN   [1] {ECO:0000313|Proteomes:UP000053314}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA   Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA   Andersen G.L., Banfield J.F.;
RT   "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT   Other Microbial Community Members in Biogeochemical Transformations in Oil
RT   Reservoirs.";
RL   MBio 7:e01669-15(2015).
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:KUK74115.1}.
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DR   EMBL; LGGM01000004; KUK74115.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A101HDA6; -.
DR   PATRIC; fig|1641393.3.peg.1584; -.
DR   Proteomes; UP000053314; 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:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KUK74115.1}.
FT   DOMAIN          9..216
FT                   /note="Acetyl-CoA hydrolase/transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02550"
FT   DOMAIN          321..464
FT                   /note="Acetyl-CoA hydrolase/transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13336"
FT   ACT_SITE        289
FT                   /note="5-glutamyl coenzyme A thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617821-1"
FT   BINDING         264..268
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617821-2"
FT   BINDING         359
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617821-2"
FT   BINDING         379
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617821-2"
FT   BINDING         383
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"
SQ   SEQUENCE   491 AA;  54032 MW;  B533485FCE51769F CRC64;
     MLDGRIRCKT LNQKIMTAEK AAELIKDGMT VGASGFTPAG YPKAVPLALA QRAGDGEDIK
     ITLITGASVG DELDGALTRS GVIARRYPYQ TNASMRDAIN NGSIKYSDMH LSHVPQWIKY
     GFFGKIDVVI VEAIGITENG GIIPSTSIGN SNVLVEMADM VIVELNTSQP VTLEGIHDIY
     SLDNPPNRKA IPIFKPDDRI GTTYIPCNPE KIKAIVYTDI IDKTRDVTLI DDDSRKISNH
     IIKFLYDEKT AGRIPEKLLP LQSGVGSVAN AILGGLCECD FKNLTIYSEV LQDSVLDLID
     AGKVDFASAT SLTISPSRLD DFYRNFGKYR DKIILRPQEI SNNPEVIRRL GVIAMNTAIE
     FDIYGNVNST NIGGTRMMNG IGGSGDFTRN GYISIFTTVS TAKDGKISSI VPFVRHVDHT
     EHDVQVVVTE QGLADLRGLN PSERADLIIE NCVHPDFKNQ LREYVERAIR TSKFVHTPHD
     FETVFLEFSD D
//
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