ID E5KWG9_STRVG Unreviewed; 302 AA. AC E5KWG9; DT 08-FEB-2011, integrated into UniProtKB/TrEMBL. DT 08-FEB-2011, sequence version 1. DT 28-JUN-2023, entry version 47. DE SubName: Full=Prenyltransferase {ECO:0000313|EMBL:ADQ43372.1}; GN Name=epzP {ECO:0000313|EMBL:ADQ43372.1}; OS Streptomyces virginiae (Streptomyces cinnamonensis). OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; Streptomyces. OX NCBI_TaxID=1961 {ECO:0000313|EMBL:ADQ43372.1}; RN [1] {ECO:0000313|EMBL:ADQ43372.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 1042 {ECO:0000313|EMBL:ADQ43372.1}; RX PubMed=21342470; RA Seeger K., Flinspach K., Haug-Schifferdecker E., Kulik A., Gust B., RA Fiedler H.P., Heide L.; RT "The biosynthetic genes for prenylated phenazines are located at two RT different chromosomal loci of Streptomyces cinnamonensis DSM 1042."; RL Microb. Biotechnol. 4:252-262(2011). RN [2] {ECO:0007829|PDB:4EE6, ECO:0007829|PDB:4EE7} RP X-RAY CRYSTALLOGRAPHY (1.33 ANGSTROMS). RX PubMed=23119011; DOI=10.1371/journal.pone.0048427; RA Zocher G., Saleh O., Heim J.B., Herbst D.A., Heide L., Stehle T.; RT "Structure-based engineering increased the catalytic turnover rate of a RT novel phenazine prenyltransferase."; RL PLoS ONE 7:e48427-e48427(2012). CC -!- SIMILARITY: Belongs to the aromatic prenyltransferase family. CC {ECO:0000256|ARBA:ARBA00005368}. 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; HQ228364; ADQ43372.1; -; Genomic_DNA. DR PDB; 4EE6; X-ray; 1.33 A; A/B=1-302. DR PDB; 4EE7; X-ray; 1.67 A; A/B=1-302. DR PDB; 4EE8; X-ray; 1.93 A; A=1-302. DR PDBsum; 4EE6; -. DR PDBsum; 4EE7; -. DR PDBsum; 4EE8; -. DR AlphaFoldDB; E5KWG9; -. DR SMR; E5KWG9; -. DR GO; GO:0004659; F:prenyltransferase activity; IEA:UniProtKB-KW. DR GO; GO:0008152; P:metabolic process; IEA:UniProt. DR CDD; cd13931; PT-CloQ_NphB; 1. DR InterPro; IPR033964; Aro_prenylTrfase. DR InterPro; IPR020965; Prenyltransferase_CloQ. DR InterPro; IPR036239; PrenylTrfase-like_sf. DR Pfam; PF11468; PTase_Orf2; 1. DR SFLD; SFLDS00036; Aromatic_Prenyltransferase; 1. DR SFLD; SFLDG01163; II; 1. DR SUPFAM; SSF143492; Prenyltransferase-like; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:4EE6, ECO:0007829|PDB:4EE7}; KW Prenyltransferase {ECO:0000256|ARBA:ARBA00022602}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ADQ43372.1}. SQ SEQUENCE 302 AA; 33233 MW; A82CC764E418CE1D CRC64; MSESADLTEL YSIIEKTAQV VDVTASHDKV WPILNAFQDV IADSVISFRA STGSSADDLD CRFTMLPKGL DPYARALEHG LTPKTDHPVG SLLKEVHENL PITSCGVDFG VAGGFTKTWS FPSAEKLGKV SELVKLPSIP DAVAANRDFF EKWGIADMVS TVGIDYSKRT MNLYFGGGVG DRVPAGVFEE KGVRAILGEL GLAAPSEELL KFCERSFVIY VTLSWDSPKI NRFTYSVMTP EPLGLPVDLA PTFERLIKSA PYDTEGRNYV YGIASTPKGE YHKIASYYQW QKRVEKLLRS DG //