PPZP_STRAQ
ID PPZP_STRAQ Reviewed; 299 AA.
AC C4PWA1;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 31.
DE RecName: Full=5,10-dihydrophenazine-1-carboxylate 9-dimethylallyltransferase {ECO:0000305};
DE Short=Dihydro-PCA dimethylallyltransferase {ECO:0000303|PubMed:19339241};
DE EC=2.5.1.121 {ECO:0000269|PubMed:19339241};
DE AltName: Full=Dihydro-PCA prenyltransferase {ECO:0000303|PubMed:19339241};
GN Name=ppzP {ECO:0000303|PubMed:19339241};
OS Streptomyces anulatus (Streptomyces chrysomallus).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1892;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=9663;
RX PubMed=19339241; DOI=10.1074/jbc.m901312200;
RA Saleh O., Gust B., Boll B., Fiedler H.P., Heide L.;
RT "Aromatic prenylation in phenazine biosynthesis: dihydrophenazine-1-
RT carboxylate dimethylallyltransferase from Streptomyces anulatus.";
RL J. Biol. Chem. 284:14439-14447(2009).
CC -!- FUNCTION: Involved in the biosynthesis of prenylated phenazines.
CC Catalyzes the transfer of a dimethylallyl moiety to C-9 of 5,10-
CC dihydrophenazine 1-carboxylate (dihydro-PCA). Specific for both
CC dimethylallyl diphosphate and dihydro-PCA.
CC {ECO:0000269|PubMed:19339241}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,10-dihydrophenazine 1-carboxylate + dimethylallyl
CC diphosphate = 5,10-dihydro-9-dimethylallylphenazine 1-carboxylate +
CC diphosphate; Xref=Rhea:RHEA:41580, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57623, ChEBI:CHEBI:78312, ChEBI:CHEBI:78313;
CC EC=2.5.1.121; Evidence={ECO:0000269|PubMed:19339241};
CC -!- ACTIVITY REGULATION: Does not require magnesium or any other divalent
CC metal ions for activity. {ECO:0000269|PubMed:19339241}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=116 uM for dimethylallyl diphosphate
CC {ECO:0000269|PubMed:19339241};
CC Note=kcat is 0.435 sec(-1). {ECO:0000269|PubMed:19339241};
CC -!- PATHWAY: Antibiotic biosynthesis; phenazine biosynthesis.
CC {ECO:0000269|PubMed:19339241}.
CC -!- DISRUPTION PHENOTYPE: Mutant can form only nonprenylated phenazine 1-
CC carboxylic acid. {ECO:0000269|PubMed:19339241}.
CC -!- SIMILARITY: Belongs to the aromatic prenyltransferase family.
CC {ECO:0000305}.
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DR EMBL; FN178498; CAX48655.1; -; Genomic_DNA.
DR AlphaFoldDB; C4PWA1; -.
DR SMR; C4PWA1; -.
DR KEGG; ag:CAX48655; -.
DR BRENDA; 2.5.1.121; 5994.
DR UniPathway; UPA00099; -.
DR GO; GO:0004659; F:prenyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0002047; P:phenazine biosynthetic process; IEA:UniProtKB-UniPathway.
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; SSF143492; 1.
PE 1: Evidence at protein level;
KW Antibiotic biosynthesis; Prenyltransferase; Transferase.
FT CHAIN 1..299
FT /note="5,10-dihydrophenazine-1-carboxylate 9-
FT dimethylallyltransferase"
FT /id="PRO_0000430678"
SQ SEQUENCE 299 AA; 33012 MW; E92778A36C604182 CRC64;
MSESAELTEL YSAIEETTRV VGAPCRRDTV RPILTAYEDV IAQSVISFRV QTGTSDAGDL
DCRFTLLPKD MDPYATALSN GLTAKTDHPV GSLLEEVHRQ FPVDCYGIDF GAVGGFKKAW
SFFRPDSLQS ASDLAALPSM PSGVSENLGL FDRYGMTDTV SVVGFDYAKR SVNLYFTGAS
PESFEPRGIQ AILRECGLPE PSDELLRFGE EAFAIYVTLS WDSQKIERVT YSVNTPDPMA
LPVRIDTRIE QLVKDAPLGS AGHRYVYGVT ATPKGEYHKI QKYFQWQSRV EKMLTADAG