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4-hydroxyphenylpyruvate 3-dimethylallyltransferase (EC 2.5.1.111) (4HPP 3-dimethylallyltransferase) (Aromatic prenyltransferase CloQ) (Clorobiocin biosynthesis protein Q)

 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}.
-----------------------------------------------------------------------
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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


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