ID PUAC_STRAD Reviewed; 199 AA. AC P13249; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 2. DT 13-SEP-2023, entry version 89. DE RecName: Full=Puromycin N-acetyltransferase; DE EC=2.3.-.-; GN Name=pac; OS Streptomyces alboniger. OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; Streptomyces; Streptomyces aurantiacus group. OX NCBI_TaxID=132473; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 12461 / DSM 40043 / JCM 4309 / NBRC 12738 / NCIMB 13007 / RC NRRL B-2403; RX PubMed=2676728; DOI=10.1016/0378-1119(89)90220-5; RA Lacalle R.A., Pulido D., Vara J., Zalacain M., Jimenez A.; RT "Molecular analysis of the pac gene encoding a puromycin N-acetyl RT transferase from Streptomyces alboniger."; RL Gene 79:375-380(1989). CC -!- FUNCTION: Detoxification of puromycin. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M25346; AAA64928.1; -; Genomic_DNA. DR PIR; JU0052; JU0052. DR RefSeq; WP_055528321.1; NZ_LIQN01000059.1. DR PDB; 7K09; X-ray; 2.31 A; A/B/C/D/E/F=2-199. DR PDB; 7K0A; X-ray; 2.00 A; A/B=2-199. DR PDBsum; 7K09; -. DR PDBsum; 7K0A; -. DR AlphaFoldDB; P13249; -. DR SMR; P13249; -. DR KEGG; ag:AAA64928; -. DR OrthoDB; 7057833at2; -. DR BioCyc; MetaCyc:MONOMER-13983; -. DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro. DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW. DR CDD; cd04301; NAT_SF; 1. DR Gene3D; 3.40.630.30; -; 1. DR InterPro; IPR016181; Acyl_CoA_acyltransferase. DR InterPro; IPR000182; GNAT_dom. DR PANTHER; PTHR42791; GNAT FAMILY ACETYLTRANSFERASE; 1. DR PANTHER; PTHR42791:SF1; N-ACETYLTRANSFERASE DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF00583; Acetyltransf_1; 1. DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1. DR PROSITE; PS51186; GNAT; 1. PE 1: Evidence at protein level; KW 3D-structure; Acyltransferase; Antibiotic resistance; Transferase. FT CHAIN 1..199 FT /note="Puromycin N-acetyltransferase" FT /id="PRO_0000068578" FT DOMAIN 6..198 FT /note="N-acetyltransferase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532" FT STRAND 8..10 FT /evidence="ECO:0007829|PDB:7K0A" FT HELIX 13..15 FT /evidence="ECO:0007829|PDB:7K0A" FT HELIX 16..26 FT /evidence="ECO:0007829|PDB:7K0A" FT TURN 27..29 FT /evidence="ECO:0007829|PDB:7K0A" FT HELIX 31..36 FT /evidence="ECO:0007829|PDB:7K0A" FT HELIX 42..56 FT /evidence="ECO:0007829|PDB:7K0A" FT HELIX 58..61 FT /evidence="ECO:0007829|PDB:7K0A" FT STRAND 62..67 FT /evidence="ECO:0007829|PDB:7K0A" FT HELIX 68..70 FT /evidence="ECO:0007829|PDB:7K0A" FT STRAND 72..77 FT /evidence="ECO:0007829|PDB:7K0A" FT HELIX 84..99 FT /evidence="ECO:0007829|PDB:7K0A" FT HELIX 100..102 FT /evidence="ECO:0007829|PDB:7K0A" FT HELIX 103..113 FT /evidence="ECO:0007829|PDB:7K0A" FT HELIX 114..116 FT /evidence="ECO:0007829|PDB:7K0A" FT STRAND 123..130 FT /evidence="ECO:0007829|PDB:7K0A" FT HELIX 132..134 FT /evidence="ECO:0007829|PDB:7K0A" FT HELIX 139..154 FT /evidence="ECO:0007829|PDB:7K0A" FT STRAND 158..163 FT /evidence="ECO:0007829|PDB:7K0A" FT HELIX 165..167 FT /evidence="ECO:0007829|PDB:7K0A" FT HELIX 168..173 FT /evidence="ECO:0007829|PDB:7K0A" FT STRAND 177..182 FT /evidence="ECO:0007829|PDB:7K0A" FT STRAND 190..195 FT /evidence="ECO:0007829|PDB:7K0A" SQ SEQUENCE 199 AA; 21496 MW; BEDA36E20304DA35 CRC64; MTEYKPTVRL ATRDDVPRAV RTLAAAFADY PATRHTVDPD RHIERVTELQ ELFLTRVGLD IGKVWVADDG AAVAVWTTPE SVEAGAVFAE IGPRMAELSG SRLAAQQQME GLLAPHRPKE PAWFLATVGV SPDHQGKGLG SAVVLPGVEA AERAGVPAFL ETSAPRNLPF YERLGFTVTA DVEVPEGPRT WCMTRKPGA //