ID   A0A265Q814_9FIRM        Unreviewed;       499 AA.
AC   A0A265Q814;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Acetyl-CoA hydrolase {ECO:0000313|EMBL:OZV12426.1};
GN   ORFNames=CIW83_10090 {ECO:0000313|EMBL:OZV12426.1};
OS   Tissierella sp. P1.
OC   Bacteria; Bacillota; Tissierellia; Tissierellales; Tissierellaceae;
OC   Tissierella.
OX   NCBI_TaxID=1280483 {ECO:0000313|EMBL:OZV12426.1, ECO:0000313|Proteomes:UP000216906};
RN   [1] {ECO:0000313|EMBL:OZV12426.1, ECO:0000313|Proteomes:UP000216906}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P1 {ECO:0000313|EMBL:OZV12426.1,
RC   ECO:0000313|Proteomes:UP000216906};
RA   Bukhtiyarova P.A., Antsiferov D.V., Avakyan M.R., Frank Y.A., Ikkert O.P.,
RA   Pimenov N.V., Brasseur G., Tuovinen O.H., Karnachuk O.V.;
RT   "Isolation and Characterization of an Anaerobic Sulfidogenic Tissierella
RT   from Cu-bearing Coins.";
RL   Submitted (AUG-2017) 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:OZV12426.1}.
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DR   EMBL; NPMN01000011; OZV12426.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A265Q814; -.
DR   OrthoDB; 9801795at2; -.
DR   Proteomes; UP000216906; Unassembled WGS sequence.
DR   GO; GO:0008775; F:acetate CoA-transferase activity; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006083; P:acetate metabolic process; IEA:InterPro.
DR   GO; GO:0006084; P:acetyl-CoA metabolic process; IEA:InterPro.
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   Hydrolase {ECO:0000313|EMBL:OZV12426.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000216906}.
FT   DOMAIN          11..217
FT                   /note="Acetyl-CoA hydrolase/transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02550"
FT   DOMAIN          319..465
FT                   /note="Acetyl-CoA hydrolase/transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13336"
FT   ACT_SITE        290
FT                   /note="5-glutamyl coenzyme A thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617821-1"
FT   BINDING         265..269
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617821-2"
FT   BINDING         360
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         384
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617821-2"
FT   BINDING         404
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617821-2"
SQ   SEQUENCE   499 AA;  55878 MW;  AE96A9BE01E7C2B3 CRC64;
     MIKDRIKGNY LRKKIISSEE ASLLIKDGMI IGTSGFTPSG YPKEIPLALV KRLDESKERI
     SITLITGASV GDEIDGEFAK RGIISKRIPY QTNDCCRNSI NNGEISFVDI HLSHLSQYIN
     YGFLGKIDLG IIEAVEISEE GYIIPSTSVG ITPTIIEKAE KLIIEINTSQ PRELRGIHDI
     YQTKNPPYRE PIPIVKASDR IGENFIPIDL NKVAAIVITD KRDDVRPFTS INQNNIKMSG
     YLIDFLEEEI KRGRIPKELL PFQSGVGSVA NAVLGGFKNS NLKSLNFYTE VIQDSMLELI
     DYDKVNIVSG TAITPSPEGL EKFYKNLDKY RKKIVLRPQE ISNNPEIIRR LGVIALNTAI
     EADIYGNVNS THILGRKMMN GIGGSGDFAR NSYISIFFTE STAKNGNVSS IVPCVSHVDH
     TEHDVDIIIT EEGVADLRGL SPKERALTII KNCSNKHYKP MLMDYYKTIT KINASHTPKI
     LKEVFSWHER FEKNGTMRI
//