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Database: UniProt
Entry: K1Z3J3_9BACT
LinkDB: K1Z3J3_9BACT
Original site: K1Z3J3_9BACT 
ID   K1Z3J3_9BACT            Unreviewed;        45 AA.
AC   K1Z3J3;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   22-FEB-2023, entry version 20.
DE   SubName: Full=Acetyl-CoA hydrolase/transferase {ECO:0000313|EMBL:EKD39173.1};
GN   ORFNames=ACD_75C00487G0001 {ECO:0000313|EMBL:EKD39173.1};
OS   uncultured bacterium.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=77133 {ECO:0000313|EMBL:EKD39173.1};
RN   [1] {ECO:0000313|EMBL:EKD39173.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23019650; DOI=10.1126/science.1224041;
RA   Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA   VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA   Long P.E., Banfield J.F.;
RT   "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT   bacterial phyla.";
RL   Science 337:1661-1665(2012).
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:EKD39173.1}.
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DR   EMBL; AMFJ01031156; EKD39173.1; -; Genomic_DNA.
DR   AlphaFoldDB; K1Z3J3; -.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.1080.20; Acetyl-CoA hydrolase/transferase C-terminal domain; 1.
DR   InterPro; IPR026888; AcetylCoA_hyd_C.
DR   InterPro; IPR038460; AcetylCoA_hyd_C_sf.
DR   InterPro; IPR037171; NagB/RpiA_transferase-like.
DR   Pfam; PF13336; AcetylCoA_hyd_C; 1.
DR   SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:EKD39173.1};
KW   Transferase {ECO:0000313|EMBL:EKD39173.1}.
FT   DOMAIN          1..38
FT                   /note="Acetyl-CoA hydrolase/transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13336"
SQ   SEQUENCE   45 AA;  5244 MW;  7D9A85D74B318B40 CRC64;
     MVTEYGLINL KGKSTWERAN ALISIAHPDF REELTEHAKR MNIQM
//
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