NOVQ_STRNV
ID NOVQ_STRNV Reviewed; 323 AA.
AC Q9L9F1; C9K4Z5;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 2.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=4-hydroxyphenylpyruvate 3-dimethylallyltransferase {ECO:0000303|Ref.3};
DE EC=2.5.1.111 {ECO:0000269|PubMed:19557032, ECO:0000269|Ref.3};
DE AltName: Full=4HPP 3-dimethylallyltransferase {ECO:0000303|Ref.3};
DE AltName: Full=Aromatic prenyltransferase NovQ {ECO:0000303|PubMed:19557032};
DE AltName: Full=Dimethylallyl diphosphate:4-hydroxyphenylpyruvate dimethylallyl transferase {ECO:0000303|Ref.3};
DE AltName: Full=Novobiocin biosynthesis protein Q {ECO:0000303|PubMed:10770754};
GN Name=novQ {ECO:0000303|PubMed:10770754};
OS Streptomyces niveus (Streptomyces spheroides).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=193462;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 23965 / DSM 40292 / JCM 4252 / NBRC 12917 / NCIMB 11891 / NRRL
RC 2449;
RX PubMed=10770754; DOI=10.1128/aac.44.5.1214-1222.2000;
RA Steffensky M., Muhlenweg A., Wang Z.X., Li S.M., Heide L.;
RT "Identification of the novobiocin biosynthetic gene cluster of Streptomyces
RT spheroides NCIB 11891.";
RL Antimicrob. Agents Chemother. 44:1214-1222(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND SUBSTRATE SPECIFICITY.
RC STRAIN=16259;
RX PubMed=19557032; DOI=10.1038/ja.2009.48;
RA Ozaki T., Mishima S., Nishiyama M., Kuzuyama T.;
RT "NovQ is a prenyltransferase capable of catalyzing the addition of a
RT dimethylallyl group to both phenylpropanoids and flavonoids.";
RL J. Antibiot. 62:385-392(2009).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, AND SUBSTRATE SPECIFICITY.
RC STRAIN=ATCC 23965 / DSM 40292 / JCM 4252 / NBRC 12917 / NCIMB 11891 / NRRL
RC 2449;
RX DOI=10.1111/j.1574-6968.1998.tb12930.x;
RA Steffensky M., Li S.-M., Vogler B., Heide L.;
RT "Novobiocin biosynthesis in Streptomyces spheroides: identification of a
RT dimethylallyl diphosphate:4-hydroxyphenylpyruvate dimethylallyl
RT transferase.";
RL FEMS Microbiol. Ecol. 161:69-74(1998).
CC -!- FUNCTION: Magnesium-independent aromatic prenyltransferase that
CC catalyzes the irreversible transfer of a dimethylallyl group to 4-
CC hydroxyphenylpyruvate to produce the ring A structure in the novobiocin
CC biosynthesis pathway. Novobiocin is an aminocoumarin family antibiotic
CC that targets bacterial DNA gyrases. It is able to prenylate many
CC different compounds, including the phenylpropanoids 4-coumarate and
CC caffeate, the plant polyketide resveratrol, the (iso)flavonoid
CC naringenin, apigenin, daidzein and genistein, and the
CC dihydroxynaphthalenes 1,6-DHN and 2,7-DHN.
CC {ECO:0000269|PubMed:19557032, ECO:0000269|Ref.3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-(4-hydroxyphenyl)pyruvate + dimethylallyl diphosphate = 3-
CC dimethylallyl-4-hydroxyphenylpyruvate + diphosphate;
CC Xref=Rhea:RHEA:37055, ChEBI:CHEBI:33019, ChEBI:CHEBI:36242,
CC ChEBI:CHEBI:57623, ChEBI:CHEBI:74408; EC=2.5.1.111;
CC Evidence={ECO:0000269|PubMed:19557032, ECO:0000269|Ref.3};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=33 uM for 4-hydroxyphenylpyruvate {ECO:0000269|PubMed:19557032};
CC KM=15.1 uM for dimethylallyl diphosphate
CC {ECO:0000269|PubMed:19557032};
CC pH dependence:
CC Optimum pH is 7. {ECO:0000269|Ref.3};
CC Temperature dependence:
CC Optimum temperature is between 30 and 40 degrees Celsius.
CC {ECO:0000269|Ref.3};
CC -!- PATHWAY: Antibiotic biosynthesis; novobiocin biosynthesis.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:19557032}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|Ref.3}.
CC -!- SIMILARITY: Belongs to the aromatic prenyltransferase family.
CC {ECO:0000305}.
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; AF170880; AAF67510.2; -; Genomic_DNA.
DR EMBL; AB496950; BAI44329.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9L9F1; -.
DR SMR; Q9L9F1; -.
DR KEGG; ag:AAF67510; -.
DR BioCyc; MetaCyc:MON-18091; -.
DR BRENDA; 2.5.1.111; 6099.
DR UniPathway; UPA01035; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004659; F:prenyltransferase activity; IDA:UniProtKB.
DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IDA:UniProtKB.
DR GO; GO:0043642; P:novobiocin biosynthetic process; IDA:UniProtKB.
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; Cytoplasm; Prenyltransferase; Transferase.
FT CHAIN 1..323
FT /note="4-hydroxyphenylpyruvate 3-dimethylallyltransferase"
FT /id="PRO_0000423991"
FT BINDING 160
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8GHB2"
FT BINDING 281
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8GHB2"
SQ SEQUENCE 323 AA; 35357 MW; 4F2EE8DF47502A4C CRC64;
MPALPMNQEF DRERFRVDLR ATAAAIGAPV TPRVTDTVLE TFRDNFAQGA TLWKTTSQPG
DQLSYRFFSR LKMDTVGRAV DAGLLDGTHP TVPIVEDWSD LYGGTPVQSA DFDAGRGMAK
TWLYFGGLRP AEDILSVPAL PAPVQARLKD FLGLGLAHVR FAAVDWRHRS ANVYFRGQGP
LDTAQFARVH ALSGGTPPAA DVVAEVLAYV PEDYCVAITL DLHTGAIDRV CFYALKVPKD
ARPRVPARIA TFLEVAPSHD PEECNVIGWS FGRSGDYVKA ERSYTGNMTE ILSGWNCFFH
GEEGRDHDLR ALQDTGSITG GAR
