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Database: UniProt
Entry: E3PV16_ACESD
LinkDB: E3PV16_ACESD
Original site: E3PV16_ACESD 
ID   E3PV16_ACESD            Unreviewed;       215 AA.
AC   E3PV16;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Putative O-acetyltransferase {ECO:0000313|EMBL:CBH20496.1};
GN   Name=epsM {ECO:0000313|EMBL:CBH20496.1};
GN   OrderedLocusNames=CLOST_0366 {ECO:0000313|EMBL:CBH20496.1};
OS   Acetoanaerobium sticklandii (strain ATCC 12662 / DSM 519 / JCM 1433 / CCUG
OS   9281 / NCIMB 10654 / HF) (Clostridium sticklandii).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Acetoanaerobium.
OX   NCBI_TaxID=499177 {ECO:0000313|EMBL:CBH20496.1, ECO:0000313|Proteomes:UP000007041};
RN   [1] {ECO:0000313|Proteomes:UP000007041}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF
RC   {ECO:0000313|Proteomes:UP000007041};
RX   PubMed=20937090; DOI=10.1186/1471-2164-11-555;
RA   Fonknechten N., Chaussonnerie S., Tricot S., Lajus A., Andreesen J.R.,
RA   Perchat N., Pelletier E., Gouyvenoux M., Barbe V., Salanoubat M.,
RA   Le Paslier D., Weissenbach J., Cohen G.N., Kreimeyer A.;
RT   "Clostridium sticklandii, a specialist in amino acid degradation:revisiting
RT   its metabolism through its genome sequence.";
RL   BMC Genomics 11:555-555(2010).
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DR   EMBL; FP565809; CBH20496.1; -; Genomic_DNA.
DR   AlphaFoldDB; E3PV16; -.
DR   STRING; 1511.CLOST_0366; -.
DR   KEGG; cst:CLOST_0366; -.
DR   eggNOG; COG1044; Bacteria.
DR   HOGENOM; CLU_081811_2_3_9; -.
DR   Proteomes; UP000007041; Chromosome.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   CDD; cd03360; LbH_AT_putative; 1.
DR   Gene3D; 3.40.50.20; -; 1.
DR   Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR   InterPro; IPR020019; AcTrfase_PglD-like.
DR   InterPro; IPR001451; Hexapep.
DR   InterPro; IPR018357; Hexapep_transf_CS.
DR   InterPro; IPR041561; PglD_N.
DR   InterPro; IPR011004; Trimer_LpxA-like_sf.
DR   NCBIfam; TIGR03570; NeuD_NnaD; 1.
DR   PANTHER; PTHR43300; ACETYLTRANSFERASE; 1.
DR   PANTHER; PTHR43300:SF7; UDP-N-ACETYLBACILLOSAMINE N-ACETYLTRANSFERASE; 1.
DR   Pfam; PF00132; Hexapep; 1.
DR   Pfam; PF14602; Hexapep_2; 1.
DR   Pfam; PF17836; PglD_N; 1.
DR   SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
DR   PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000007041};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CBH20496.1}.
FT   DOMAIN          4..86
FT                   /note="PglD N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17836"
FT   ACT_SITE        141
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR620019-1"
FT   BINDING         74
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR620019-2"
FT   BINDING         150
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR620019-2"
FT   SITE            142
FT                   /note="Increases basicity of active site His"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR620019-1"
SQ   SEQUENCE   215 AA;  22747 MW;  7EF373BA06251453 CRC64;
     MNKKILLIGG GGHCKSVLDT LLLLNEYNEI AIVDLFENIG NSIIGIPIIG ADTDLAHLFK
     DGYEFAFITM GSIGNPRLRI KLYDEISSIG FNIPNIIDIS ANVSNFTKLG KGIFIGKKSI
     VNAGAIIGNG AIINTGSIIE HDCKIGEFVH IAPGAILGGA VEIGKNSHVG SGAIIKQQIK
     IGDNSVIGMG SIVTKIIGNN KKAYGNPCRE VNDYE
//
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