ID H0E1N0_9ACTN Unreviewed; 411 AA.
AC H0E1N0;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 13-SEP-2023, entry version 39.
DE RecName: Full=N-acetyltransferase domain-containing protein {ECO:0000259|PROSITE:PS51186};
GN ORFNames=PAI11_06920 {ECO:0000313|EMBL:EHN12414.1};
OS Patulibacter medicamentivorans.
OC Bacteria; Actinomycetota; Thermoleophilia; Solirubrobacterales;
OC Patulibacteraceae; Patulibacter.
OX NCBI_TaxID=1097667 {ECO:0000313|EMBL:EHN12414.1, ECO:0000313|Proteomes:UP000005143};
RN [1] {ECO:0000313|EMBL:EHN12414.1, ECO:0000313|Proteomes:UP000005143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=I11 {ECO:0000313|EMBL:EHN12414.1,
RC ECO:0000313|Proteomes:UP000005143};
RX PubMed=23212173; DOI=10.1007/s10532-012-9610-5;
RA Almeida B., Kjeldal H., Lolas I., Knudsen A.D., Carvalho G., Nielsen K.L.,
RA Barreto Crespo M.T., Stensballe A., Nielsen J.L.;
RT "Quantitative proteomic analysis of ibuprofen-degrading Patulibacter sp.
RT strain I11.";
RL Biodegradation 24:615-630(2013).
CC -!- SUBUNIT: Homohexamer; trimer of dimers. {ECO:0000256|HAMAP-
CC Rule:MF_01812}.
CC -!- SIMILARITY: Belongs to the acetyltransferase Eis family.
CC {ECO:0000256|ARBA:ARBA00009213, ECO:0000256|HAMAP-Rule:MF_01812}.
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:EHN12414.1}.
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DR EMBL; AGUD01000026; EHN12414.1; -; Genomic_DNA.
DR RefSeq; WP_007570926.1; NZ_AGUD01000026.1.
DR AlphaFoldDB; H0E1N0; -.
DR PATRIC; fig|1097667.3.peg.689; -.
DR OrthoDB; 8399956at2; -.
DR Proteomes; UP000005143; Unassembled WGS sequence.
DR GO; GO:0008080; F:N-acetyltransferase activity; IEA:UniProtKB-UniRule.
DR CDD; cd04301; NAT_SF; 1.
DR Gene3D; 3.40.630.30; -; 2.
DR Gene3D; 3.30.1050.10; SCP2 sterol-binding domain; 1.
DR HAMAP; MF_01812; Eis; 1.
DR InterPro; IPR041380; Acetyltransf_17.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR025559; Eis_dom.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR022902; NAcTrfase_Eis.
DR InterPro; IPR036527; SCP2_sterol-bd_dom_sf.
DR PANTHER; PTHR37817; N-ACETYLTRANSFERASE EIS; 1.
DR PANTHER; PTHR37817:SF1; N-ACETYLTRANSFERASE EIS; 1.
DR Pfam; PF17668; Acetyltransf_17; 1.
DR Pfam; PF13527; Acetyltransf_9; 1.
DR Pfam; PF13530; SCP2_2; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF55718; SCP-like; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW Rule:MF_01812}; Reference proteome {ECO:0000313|Proteomes:UP000005143};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01812}.
FT DOMAIN 5..152
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 411 AA; 43969 MW; 4F62C104599C0E88 CRC64;
MSDRLAVRAA TEDEFGALLD AAAIAFHGDR SDASRLRLRD RFELDRSRIA LDDGQVVGTS
SAWGWRLTVP GGELPCAAIT LVTVLPTHRR RGILRRMMKA LVADARERGE PLAALWASEG
RIYGRFGFGP ASWTRRSRID LAGGVPLRSP VADPSLRLVD LAGAAPLTAA IFDRARRQRA
GIMSRPPAWW TTRILSDAQD ERPADGAPKR LVACGEDGYA LYRVHEDVAG GPVGGIGQTT
VEVQELIAAT PEAGRALLAF LTSIDLATRV ELHERPLDDE LELAPADPRA MRTIQQGDAL
WLRILDLPAA VAGRSWAADA DLVLQVDAPG DPGLDGRWAL RIADGAGVAE RSERPADLAI
ADRDLASAYL GGVRVAALAA AGVVVEHEPG AVATLDLALR TARAPWTVDV F
//
