CLOQ_STRRC
ID CLOQ_STRRC Reviewed; 324 AA.
AC Q8GHB2;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=4-hydroxyphenylpyruvate 3-dimethylallyltransferase {ECO:0000303|PubMed:12618544};
DE EC=2.5.1.111 {ECO:0000269|PubMed:12618544};
DE AltName: Full=4HPP 3-dimethylallyltransferase {ECO:0000303|PubMed:12618544};
DE AltName: Full=Aromatic prenyltransferase CloQ {ECO:0000303|PubMed:12618544};
DE AltName: Full=Clorobiocin biosynthesis protein Q {ECO:0000303|PubMed:12480894};
GN Name=cloQ {ECO:0000303|PubMed:12480894};
OS Streptomyces roseochromogenus subsp. oscitans.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=149682;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DS 12.976;
RX PubMed=12480894; DOI=10.1099/00221287-148-12-3901;
RA Pojer F., Li S.M., Heide L.;
RT "Molecular cloning and sequence analysis of the clorobiocin biosynthetic
RT gene cluster: new insights into the biosynthesis of aminocoumarin
RT antibiotics.";
RL Microbiology 148:3901-3911(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND
RP SUBUNIT.
RC STRAIN=DS 12.976;
RX PubMed=12618544; DOI=10.1073/pnas.0337708100;
RA Pojer F., Wemakor E., Kammerer B., Chen H., Walsh C.T., Li S.M., Heide L.;
RT "CloQ, a prenyltransferase involved in clorobiocin biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:2316-2321(2003).
RN [3]
RP DISRUPTION PHENOTYPE.
RC STRAIN=DS 12.976;
RX PubMed=15152806; DOI=10.7164/antibiotics.57.205;
RA Freitag A., Galm U., Li S.M., Heide L.;
RT "New aminocoumarin antibiotics from a cloQ-defective mutant of the
RT clorobiocin producer Streptomyces roseochromogenes DS12.976.";
RL J. Antibiot. 57:205-209(2004).
RN [4]
RP PRELIMINARY CRYSTALLIZATION, AND SUBUNIT.
RX PubMed=17077503; DOI=10.1107/s1744309106042527;
RA Keller S., Pojer F., Heide L., Lawson D.M.;
RT "Crystallization and preliminary X-ray analysis of the aromatic
RT prenyltransferase CloQ from the clorobiocin biosynthetic cluster of
RT Streptomyces roseochromogenes.";
RL Acta Crystallogr. F 62:1153-1155(2006).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH
RP 4-HYDROXYPHENYLPYRUVATE, AND MUTAGENESIS OF LYS-54; ARG-66; PHE-68;
RP ARG-160; CYS-215 AND GLU-281.
RC STRAIN=DS 12.976;
RX PubMed=20946900; DOI=10.1016/j.jmb.2010.09.067;
RA Metzger U., Keller S., Stevenson C.E., Heide L., Lawson D.M.;
RT "Structure and mechanism of the magnesium-independent aromatic
RT prenyltransferase CloQ from the clorobiocin biosynthetic pathway.";
RL J. Mol. Biol. 404:611-626(2010).
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
CC clorobiocin biosynthesis pathway. Clorobiocin is an aminocoumarin
CC family antibiotic. {ECO:0000269|PubMed:12618544}.
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:12618544};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=25 uM for 4-hydroxyphenylpyruvate {ECO:0000269|PubMed:12618544};
CC KM=35 uM for dimethylallyl diphosphate {ECO:0000269|PubMed:12618544};
CC -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000269|PubMed:12618544}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12618544,
CC ECO:0000269|PubMed:17077503, ECO:0000269|PubMed:20946900}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene produce antibiotic
CC compounds (vanillobiocin, isovanillobiocin and declovanillobiocin) with
CC a methoxy instead of the dimethylallyl group at the position 3 of the
CC 4-hydroxybenzoic acid moiety of clorobiocin.
CC {ECO:0000269|PubMed:15152806}.
CC -!- SIMILARITY: Belongs to the aromatic prenyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AF329398; AAN65239.1; -; Genomic_DNA.
DR PDB; 2XLQ; X-ray; 2.22 A; A=1-324.
DR PDB; 2XLY; X-ray; 3.10 A; A=1-324.
DR PDB; 2XM5; X-ray; 1.85 A; A=1-324.
DR PDB; 2XM7; X-ray; 2.22 A; A=1-324.
DR PDBsum; 2XLQ; -.
DR PDBsum; 2XLY; -.
DR PDBsum; 2XM5; -.
DR PDBsum; 2XM7; -.
DR AlphaFoldDB; Q8GHB2; -.
DR SMR; Q8GHB2; -.
DR KEGG; ag:AAN65239; -.
DR BRENDA; 2.5.1.111; 13262.
DR EvolutionaryTrace; Q8GHB2; -.
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:0017000; P:antibiotic 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 3D-structure; Antibiotic biosynthesis; Prenyltransferase; Transferase.
FT CHAIN 1..324
FT /note="4-hydroxyphenylpyruvate 3-dimethylallyltransferase"
FT /id="PRO_0000423992"
FT BINDING 160
FT /ligand="substrate"
FT BINDING 281
FT /ligand="substrate"
FT MUTAGEN 54
FT /note="K->S: Abolishes prenyltransferase activity."
FT /evidence="ECO:0000269|PubMed:20946900"
FT MUTAGEN 66
FT /note="R->S: Abolishes prenyltransferase activity."
FT /evidence="ECO:0000269|PubMed:20946900"
FT MUTAGEN 68
FT /note="F->S: Almost abolishes prenyltransferase activity."
FT /evidence="ECO:0000269|PubMed:20946900"
FT MUTAGEN 160
FT /note="R->A,Q: Impaired prenyltransferase activity."
FT /evidence="ECO:0000269|PubMed:20946900"
FT MUTAGEN 215
FT /note="C->A,S: Does not affect prenyltransferase activity."
FT /evidence="ECO:0000269|PubMed:20946900"
FT MUTAGEN 281
FT /note="E->G: Abolishes prenyltransferase activity."
FT /evidence="ECO:0000269|PubMed:20946900"
FT STRAND 7..9
FT /evidence="ECO:0007829|PDB:2XM5"
FT HELIX 12..26
FT /evidence="ECO:0007829|PDB:2XM5"
FT HELIX 32..48
FT /evidence="ECO:0007829|PDB:2XM5"
FT STRAND 49..58
FT /evidence="ECO:0007829|PDB:2XM5"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:2XM5"
FT HELIX 75..81
FT /evidence="ECO:0007829|PDB:2XM5"
FT HELIX 92..104
FT /evidence="ECO:0007829|PDB:2XM5"
FT STRAND 107..113
FT /evidence="ECO:0007829|PDB:2XM5"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:2XM5"
FT STRAND 117..130
FT /evidence="ECO:0007829|PDB:2XM5"
FT HELIX 131..135
FT /evidence="ECO:0007829|PDB:2XM5"
FT HELIX 142..145
FT /evidence="ECO:0007829|PDB:2XM5"
FT HELIX 148..153
FT /evidence="ECO:0007829|PDB:2XM5"
FT STRAND 158..165
FT /evidence="ECO:0007829|PDB:2XM5"
FT TURN 166..169
FT /evidence="ECO:0007829|PDB:2XM5"
FT STRAND 170..176
FT /evidence="ECO:0007829|PDB:2XM5"
FT HELIX 183..191
FT /evidence="ECO:0007829|PDB:2XM5"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:2XM5"
FT HELIX 200..208
FT /evidence="ECO:0007829|PDB:2XM5"
FT STRAND 215..221
FT /evidence="ECO:0007829|PDB:2XM5"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:2XM5"
FT STRAND 227..236
FT /evidence="ECO:0007829|PDB:2XM5"
FT HELIX 239..241
FT /evidence="ECO:0007829|PDB:2XM5"
FT HELIX 247..255
FT /evidence="ECO:0007829|PDB:2XM5"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:2XM7"
FT STRAND 265..272
FT /evidence="ECO:0007829|PDB:2XM5"
FT STRAND 277..286
FT /evidence="ECO:0007829|PDB:2XM5"
FT HELIX 288..294
FT /evidence="ECO:0007829|PDB:2XM5"
FT HELIX 307..314
FT /evidence="ECO:0007829|PDB:2XM5"
SQ 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
