GENTAUR Molecular Products.

 CLOQ_STRRC              Reviewed;         324 AA.
 Q8GHB2;
 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
 01-MAR-2003, sequence version 1.
 25-OCT-2017, entry version 33.
 RecName: Full=4-hydroxyphenylpyruvate 3-dimethylallyltransferase {ECO:0000303|PubMed:12618544};
          EC=2.5.1.111 {ECO:0000269|PubMed:12618544};
 AltName: Full=4HPP 3-dimethylallyltransferase {ECO:0000303|PubMed:12618544};
 AltName: Full=Aromatic prenyltransferase CloQ {ECO:0000303|PubMed:12618544};
 AltName: Full=Clorobiocin biosynthesis protein Q {ECO:0000303|PubMed:12480894};
 Name=cloQ {ECO:0000303|PubMed:12480894};
 Streptomyces roseochromogenus subsp. oscitans.
 Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
 Streptomyces.
 NCBI_TaxID=149682;
 [1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
 STRAIN=DS 12.976;
 PubMed=12480894;
 Pojer F., Li S.M., Heide L.;
 "Molecular cloning and sequence analysis of the clorobiocin
 biosynthetic gene cluster: new insights into the biosynthesis of
 aminocoumarin antibiotics.";
 Microbiology 148:3901-3911(2002).
 [2]
 FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY,
 AND SUBUNIT.
 STRAIN=DS 12.976;
 PubMed=12618544; DOI=10.1073/pnas.0337708100;
 Pojer F., Wemakor E., Kammerer B., Chen H., Walsh C.T., Li S.M.,
 Heide L.;
 "CloQ, a prenyltransferase involved in clorobiocin biosynthesis.";
 Proc. Natl. Acad. Sci. U.S.A. 100:2316-2321(2003).
 [3]
 DISRUPTION PHENOTYPE.
 STRAIN=DS 12.976;
 PubMed=15152806; DOI=10.7164/antibiotics.57.205;
 Freitag A., Galm U., Li S.M., Heide L.;
 "New aminocoumarin antibiotics from a cloQ-defective mutant of the
 clorobiocin producer Streptomyces roseochromogenes DS12.976.";
 J. Antibiot. 57:205-209(2004).
 [4]
 PRELIMINARY CRYSTALLIZATION, AND SUBUNIT.
 PubMed=17077503; DOI=10.1107/S1744309106042527;
 Keller S., Pojer F., Heide L., Lawson D.M.;
 "Crystallization and preliminary X-ray analysis of the aromatic
 prenyltransferase CloQ from the clorobiocin biosynthetic cluster of
 Streptomyces roseochromogenes.";
 Acta Crystallogr. F 62:1153-1155(2006).
 [5]
 X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH
 4-HYDROXYPHENYLPYRUVATE, AND MUTAGENESIS OF LYS-54; ARG-66; PHE-68;
 ARG-160; CYS-215 AND GLU-281.
 STRAIN=DS 12.976;
 PubMed=20946900; DOI=10.1016/j.jmb.2010.09.067;
 Metzger U., Keller S., Stevenson C.E., Heide L., Lawson D.M.;
 "Structure and mechanism of the magnesium-independent aromatic
 prenyltransferase CloQ from the clorobiocin biosynthetic pathway.";
 J. Mol. Biol. 404:611-626(2010).
 -!- FUNCTION: Magnesium-independent aromatic prenyltransferase that
     catalyzes the irreversible transfer of a dimethylallyl group to 4-
     hydroxyphenylpyruvate to produce the ring A structure in the
     clorobiocin biosynthesis pathway. Clorobiocin is an aminocoumarin
     family antibiotic. {ECO:0000269|PubMed:12618544}.
 -!- CATALYTIC ACTIVITY: Dimethylallyl diphosphate + 4-
     hydroxyphenylpyruvate = diphosphate + 3-dimethylallyl-4-
     hydroxyphenylpyruvate. {ECO:0000269|PubMed:12618544}.
 -!- BIOPHYSICOCHEMICAL PROPERTIES:
     Kinetic parameters:
       KM=25 uM for 4-hydroxyphenylpyruvate
       {ECO:0000269|PubMed:12618544};
       KM=35 uM for dimethylallyl diphosphate
       {ECO:0000269|PubMed:12618544};
 -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000269|PubMed:12618544}.
 -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12618544,
     ECO:0000269|PubMed:17077503, ECO:0000269|PubMed:20946900}.
 -!- DISRUPTION PHENOTYPE: Cells lacking this gene produce antibiotic
     compounds (vanillobiocin, isovanillobiocin and declovanillobiocin)
     with a methoxy instead of the dimethylallyl group at the position
     3 of the 4-hydroxybenzoic acid moiety of clorobiocin.
     {ECO:0000269|PubMed:15152806}.
 -!- SIMILARITY: Belongs to the aromatic prenyltransferase family.
     {ECO:0000305}.
 -----------------------------------------------------------------------
 Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
 Distributed under the Creative Commons Attribution (CC BY 4.0) License
 -----------------------------------------------------------------------
 EMBL; AF329398; AAN65239.1; -; Genomic_DNA.
 PDB; 2XLQ; X-ray; 2.22 A; A=1-324.
 PDB; 2XLY; X-ray; 3.10 A; A=1-324.
 PDB; 2XM5; X-ray; 1.85 A; A=1-324.
 PDB; 2XM7; X-ray; 2.22 A; A=1-324.
 PDBsum; 2XLQ; -.
 PDBsum; 2XLY; -.
 PDBsum; 2XM5; -.
 PDBsum; 2XM7; -.
 SMR; Q8GHB2; -.
 KEGG; ag:AAN65239; -.
 KO; K12707; -.
 BRENDA; 2.5.1.111; 13262.
 EvolutionaryTrace; Q8GHB2; -.
 GO; GO:0004659; F:prenyltransferase activity; IDA:UniProtKB.
 GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IDA:UniProtKB.
 GO; GO:0017000; P:antibiotic biosynthetic process; IDA:UniProtKB.
 CDD; cd13931; PT-CloQ_NphB; 1.
 InterPro; IPR020965; Prenyltransferase_CloQ.
 InterPro; IPR036239; PrenylTrfase-like_sf.
 Pfam; PF11468; PTase_Orf2; 1.
 SFLD; SFLDG01163; II; 1.
 SUPFAM; SSF143492; SSF143492; 1.
 1: Evidence at protein level;
 3D-structure; Antibiotic biosynthesis; Prenyltransferase; Transferase.
 CHAIN         1    324       4-hydroxyphenylpyruvate 3-
                              dimethylallyltransferase.
                              /FTId=PRO_0000423992.
 BINDING     160    160       Substrate.
 BINDING     281    281       Substrate.
 MUTAGEN      54     54       K->S: Abolishes prenyltransferase
                              activity. {ECO:0000269|PubMed:20946900}.
 MUTAGEN      66     66       R->S: Abolishes prenyltransferase
                              activity. {ECO:0000269|PubMed:20946900}.
 MUTAGEN      68     68       F->S: Almost abolishes prenyltransferase
                              activity. {ECO:0000269|PubMed:20946900}.
 MUTAGEN     160    160       R->A,Q: Impaired prenyltransferase
                              activity. {ECO:0000269|PubMed:20946900}.
 MUTAGEN     215    215       C->A,S: Does not affect prenyltransferase
                              activity. {ECO:0000269|PubMed:20946900}.
 MUTAGEN     281    281       E->G: Abolishes prenyltransferase
                              activity. {ECO:0000269|PubMed:20946900}.
 STRAND        7      9       {ECO:0000244|PDB:2XM5}.
 HELIX        12     26       {ECO:0000244|PDB:2XM5}.
 HELIX        32     48       {ECO:0000244|PDB:2XM5}.
 STRAND       49     58       {ECO:0000244|PDB:2XM5}.
 STRAND       64     68       {ECO:0000244|PDB:2XM5}.
 HELIX        75     81       {ECO:0000244|PDB:2XM5}.
 HELIX        92    104       {ECO:0000244|PDB:2XM5}.
 STRAND      107    113       {ECO:0000244|PDB:2XM5}.
 TURN        114    116       {ECO:0000244|PDB:2XM5}.
 STRAND      117    130       {ECO:0000244|PDB:2XM5}.
 HELIX       131    135       {ECO:0000244|PDB:2XM5}.
 HELIX       142    145       {ECO:0000244|PDB:2XM5}.
 HELIX       148    153       {ECO:0000244|PDB:2XM5}.
 STRAND      158    165       {ECO:0000244|PDB:2XM5}.
 TURN        166    169       {ECO:0000244|PDB:2XM5}.
 STRAND      170    176       {ECO:0000244|PDB:2XM5}.
 HELIX       183    191       {ECO:0000244|PDB:2XM5}.
 TURN        192    194       {ECO:0000244|PDB:2XM5}.
 HELIX       200    208       {ECO:0000244|PDB:2XM5}.
 STRAND      215    221       {ECO:0000244|PDB:2XM5}.
 TURN        222    224       {ECO:0000244|PDB:2XM5}.
 STRAND      227    236       {ECO:0000244|PDB:2XM5}.
 HELIX       239    241       {ECO:0000244|PDB:2XM5}.
 HELIX       247    255       {ECO:0000244|PDB:2XM5}.
 STRAND      260    262       {ECO:0000244|PDB:2XM7}.
 STRAND      265    272       {ECO:0000244|PDB:2XM5}.
 STRAND      277    286       {ECO:0000244|PDB:2XM5}.
 HELIX       288    294       {ECO:0000244|PDB:2XM5}.
 HELIX       307    314       {ECO:0000244|PDB:2XM5}.
 SEQUENCE   324 AA;  35626 MW;  D522DC79173052DA CRC64;
 MPALPIDQEF DCERFRADIR ATAAAIGAPI AHRLTDTVLE AFRDNFAQGA TLWKTTSQPG
 DQLSYRFFSR LKMDTVSRAI DAGLLDAAHP TLAVVDAWSS LYGGAPVQSG DFDAGRGMAK
 TWLYFGGLRP AEDILTVPAL PASVQARLKD FLALGLAHVR FAAVDWRHHS ANVYFRGKGP
 LDTVQFARIH ALSGSTPPAA HVVEEVLAYM PEDYCVAITL DLHSGDIERV CFYALKVPKN
 ALPRIPTRIA RFLEVAPSHD VEECNVIGWS FGRSGDYVKA ERSYTGNMAE ILAGWNCFFH
 GEEGRDHDLR ALHQHTESTM GGAR

Related products :