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Flavin-dependent tryptophan halogenase PrnA (EC 1.14.19.9)

 PRNA_PSEFL              Reviewed;         538 AA.
P95480;
29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
01-MAY-1997, sequence version 1.
20-JUN-2018, entry version 63.
RecName: Full=Flavin-dependent tryptophan halogenase PrnA;
EC=1.14.19.9;
Name=prnA;
Pseudomonas fluorescens.
Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
Pseudomonadaceae; Pseudomonas.
NCBI_TaxID=294;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, AND
NOMENCLATURE.
STRAIN=Bl915;
PubMed=9172332;
Hammer P.E., Hill D.S., Lam S.T., Van Pee K.H., Ligon J.M.;
"Four genes from Pseudomonas fluorescens that encode the biosynthesis
of pyrrolnitrin.";
Appl. Environ. Microbiol. 63:2147-2154(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
DISRUPTION PHENOTYPE, AND COFACTOR.
STRAIN=Bl915;
PubMed=9537395;
Kirner S., Hammer P.E., Hill D.S., Altmann A., Fischer I.,
Weislo L.J., Lanahan M., van Pee K.H., Ligon J.M.;
"Functions encoded by pyrrolnitrin biosynthetic genes from Pseudomonas
fluorescens.";
J. Bacteriol. 180:1939-1943(1998).
[3]
FUNCTION, AND COFACTOR.
PubMed=10941070;
DOI=10.1002/1521-3773(20000703)39:13<2300::AID-ANIE2300>3.0.CO;2-I;
Keller S., Wage T., Hohaus K., Holzer M., Eichhorn E., van Pee K.H.;
"Purification and partial characterization of tryptophan 7-halogenase
(PrnA) from Pseudomonas fluorescens.";
Angew. Chem. Int. Ed. 39:2300-2302(2000).
[4]
CRYSTALLIZATION.
PubMed=15272170; DOI=10.1107/S0907444904012521;
Dong C., Kotzsch A., Dorward M., van Pee K.H., Naismith J.H.;
"Crystallization and X-ray diffraction of a halogenating enzyme,
tryptophan 7-halogenase, from Pseudomonas fluorescens.";
Acta Crystallogr. D 60:1438-1440(2004).
[5]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH FAD, CHLORIDE
AND TRYPTOPHAN, ACTIVE SITE, MUTAGENESIS OF LYS-79 AND GLU-346, AND
SUBUNIT.
PubMed=16195462; DOI=10.1126/science.1116510;
Dong C., Flecks S., Unversucht S., Haupt C., van Pee K.H.,
Naismith J.H.;
"Tryptophan 7-halogenase (PrnA) structure suggests a mechanism for
regioselective chlorination.";
Science 309:2216-2219(2005).
[6]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF MUTANT ASP-346 IN COMPLEX
WITH FAD AND TRYPTOPHAN, MUTAGENESIS OF TRP-272; TRP-274; GLU-346 AND
SER-347, BIOPHYSICOCHEMICAL PROPERTIES, AND REACTION MECHANISM.
PubMed=18979475; DOI=10.1002/anie.200802466;
Flecks S., Patallo E.P., Zhu X., Ernyei A.J., Seifert G.,
Schneider A., Dong C., Naismith J.H., van Pee K.H.;
"New insights into the mechanism of enzymatic chlorination of
tryptophan.";
Angew. Chem. Int. Ed. 47:9533-9536(2008).
-!- FUNCTION: Involved in the biosynthesis of the antifungal
antibiotic pyrrolnitrin. Catalyzes the chlorination of tryptophan
(Trp) at C7 position to yield 7-chloro-L-tryptophan (7-CLT). The
reaction between FADH2, Cl-, and O2 generates the powerful oxidant
HOCl, which is presumed to carry out the chlorination reaction.
The reaction of HOCl with the active site Lys-79 generates a
lysine chloramine, which plays a key role in directing
regiospecific chlorination of substrate in this important class of
biosynthetic enzymes. It is also able to use bromide ions to
generate monobrominated Trp. {ECO:0000269|PubMed:10941070,
ECO:0000269|PubMed:9172332, ECO:0000269|PubMed:9537395}.
-!- CATALYTIC ACTIVITY: Tryptophan + FADH(2) + chloride + O(2) + H(+)
= 7-chloro-L-tryptophan + FAD + 2 H(2)O.
{ECO:0000269|PubMed:9537395}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000269|PubMed:10941070,
ECO:0000269|PubMed:9537395};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=17.1 uM for tryptophan (with FAD at pH 7.2 and 30 degrees
Celsius) {ECO:0000269|PubMed:18979475};
Vmax=43 pmol/min/mg enzyme {ECO:0000269|PubMed:18979475};
-!- PATHWAY: Antibiotic biosynthesis.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16195462,
ECO:0000269|PubMed:18979475}.
-!- DISRUPTION PHENOTYPE: Cells lacking this gene lose the ability to
produce pyrrolnitrin. {ECO:0000269|PubMed:9172332,
ECO:0000269|PubMed:9537395}.
-!- SIMILARITY: Belongs to the flavin-dependent halogenase family.
Bacterial tryptophan halogenase subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; U74493; AAB97504.1; -; Genomic_DNA.
PDB; 2APG; X-ray; 1.90 A; A=1-538.
PDB; 2AQJ; X-ray; 1.80 A; A=1-538.
PDB; 2AR8; X-ray; 2.20 A; A=1-538.
PDB; 2ARD; X-ray; 2.60 A; A=1-538.
PDB; 2JKC; X-ray; 2.30 A; A=1-538.
PDB; 4Z43; X-ray; 2.29 A; A=1-538.
PDB; 4Z44; X-ray; 2.20 A; A=1-538.
PDBsum; 2APG; -.
PDBsum; 2AQJ; -.
PDBsum; 2AR8; -.
PDBsum; 2ARD; -.
PDBsum; 2JKC; -.
PDBsum; 4Z43; -.
PDBsum; 4Z44; -.
ProteinModelPortal; P95480; -.
SMR; P95480; -.
KEGG; ag:AAB97504; -.
eggNOG; ENOG4105QV4; Bacteria.
eggNOG; ENOG410XSYF; LUCA.
KO; K14266; -.
BioCyc; MetaCyc:MONOMER-16710; -.
BRENDA; 1.14.14.7; 5121.
SABIO-RK; P95480; -.
EvolutionaryTrace; P95480; -.
GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
Gene3D; 3.50.50.60; -; 1.
InterPro; IPR036188; FAD/NAD-bd_sf.
InterPro; IPR006905; Flavin_halogenase.
InterPro; IPR033856; Trp_halogen.
Pfam; PF04820; Trp_halogenase; 1.
PIRSF; PIRSF011396; Trp_halogenase; 1.
SUPFAM; SSF51905; SSF51905; 3.
1: Evidence at protein level;
3D-structure; Antibiotic biosynthesis; FAD; Flavoprotein;
Nucleotide-binding; Oxidoreductase.
CHAIN 1 538 Flavin-dependent tryptophan halogenase
PrnA.
/FTId=PRO_0000422330.
NP_BIND 13 16 FAD. {ECO:0000269|PubMed:16195462,
ECO:0000269|PubMed:18979475}.
NP_BIND 39 50 FAD. {ECO:0000269|PubMed:16195462,
ECO:0000269|PubMed:18979475}.
REGION 348 349 Chloride binding.
REGION 443 444 L-tryptophan binding.
ACT_SITE 79 79 {ECO:0000269|PubMed:16195462}.
BINDING 79 79 L-tryptophan.
BINDING 187 187 FAD; via amide nitrogen and carbonyl
oxygen. {ECO:0000269|PubMed:16195462,
ECO:0000269|PubMed:18979475}.
BINDING 337 337 FAD; via amide nitrogen.
{ECO:0000269|PubMed:16195462,
ECO:0000269|PubMed:18979475}.
BINDING 346 346 L-tryptophan; via carbonyl oxygen.
BINDING 350 350 FAD; via amide nitrogen.
{ECO:0000269|PubMed:16195462,
ECO:0000269|PubMed:18979475}.
BINDING 450 450 L-tryptophan.
BINDING 454 454 L-tryptophan; via carbonyl oxygen.
SITE 79 79 Role in guiding and activating HOCl.
SITE 346 346 Role in stabilization and deprotonation
of the intermediate.
MUTAGEN 79 79 K->A: Loss of halogenase activity.
{ECO:0000269|PubMed:16195462}.
MUTAGEN 272 272 W->A: No change in halogenase activity.
{ECO:0000269|PubMed:18979475}.
MUTAGEN 272 272 W->F: No change in halogenase activity.
{ECO:0000269|PubMed:18979475}.
MUTAGEN 274 274 W->A: No change in halogenase activity.
{ECO:0000269|PubMed:18979475}.
MUTAGEN 274 274 W->F: No change in halogenase activity.
{ECO:0000269|PubMed:18979475}.
MUTAGEN 346 346 E->D: Loss of halogenase activity.
{ECO:0000269|PubMed:16195462,
ECO:0000269|PubMed:18979475}.
MUTAGEN 346 346 E->Q: The catalytic efficiency decreases
by about two orders of magnitude, however
the binding affinity is unchanged.
{ECO:0000269|PubMed:16195462,
ECO:0000269|PubMed:18979475}.
MUTAGEN 347 347 S->A: Does not completely abolish
halogenase activity.
{ECO:0000269|PubMed:18979475}.
STRAND 7 11 {ECO:0000244|PDB:2AQJ}.
HELIX 15 27 {ECO:0000244|PDB:2AQJ}.
TURN 28 30 {ECO:0000244|PDB:2JKC}.
STRAND 33 38 {ECO:0000244|PDB:2AQJ}.
STRAND 40 42 {ECO:0000244|PDB:2AQJ}.
HELIX 54 58 {ECO:0000244|PDB:2AQJ}.
HELIX 60 63 {ECO:0000244|PDB:2AQJ}.
HELIX 67 70 {ECO:0000244|PDB:2AQJ}.
HELIX 71 74 {ECO:0000244|PDB:2AQJ}.
STRAND 77 79 {ECO:0000244|PDB:2AQJ}.
STRAND 81 86 {ECO:0000244|PDB:2AQJ}.
STRAND 88 90 {ECO:0000244|PDB:2AQJ}.
STRAND 98 104 {ECO:0000244|PDB:2AQJ}.
STRAND 108 113 {ECO:0000244|PDB:4Z44}.
HELIX 114 123 {ECO:0000244|PDB:2AQJ}.
HELIX 130 134 {ECO:0000244|PDB:2AQJ}.
HELIX 138 142 {ECO:0000244|PDB:2AQJ}.
STRAND 159 162 {ECO:0000244|PDB:2AQJ}.
HELIX 164 177 {ECO:0000244|PDB:2AQJ}.
STRAND 181 184 {ECO:0000244|PDB:2AQJ}.
STRAND 187 192 {ECO:0000244|PDB:2AQJ}.
STRAND 194 196 {ECO:0000244|PDB:2ARD}.
STRAND 198 203 {ECO:0000244|PDB:2AQJ}.
STRAND 208 210 {ECO:0000244|PDB:4Z44}.
STRAND 212 216 {ECO:0000244|PDB:2AQJ}.
HELIX 219 221 {ECO:0000244|PDB:2AQJ}.
HELIX 223 228 {ECO:0000244|PDB:2AQJ}.
STRAND 233 235 {ECO:0000244|PDB:2AQJ}.
TURN 237 239 {ECO:0000244|PDB:2AQJ}.
STRAND 244 251 {ECO:0000244|PDB:2AQJ}.
HELIX 254 257 {ECO:0000244|PDB:2AQJ}.
STRAND 261 267 {ECO:0000244|PDB:2AQJ}.
STRAND 269 278 {ECO:0000244|PDB:2AQJ}.
STRAND 281 288 {ECO:0000244|PDB:2AQJ}.
TURN 290 292 {ECO:0000244|PDB:2AQJ}.
HELIX 295 306 {ECO:0000244|PDB:2AQJ}.
STRAND 315 318 {ECO:0000244|PDB:2AQJ}.
STRAND 322 325 {ECO:0000244|PDB:2AQJ}.
STRAND 327 329 {ECO:0000244|PDB:2AQJ}.
STRAND 332 334 {ECO:0000244|PDB:2AQJ}.
HELIX 336 338 {ECO:0000244|PDB:2AQJ}.
HELIX 344 346 {ECO:0000244|PDB:2APG}.
HELIX 349 362 {ECO:0000244|PDB:2AQJ}.
HELIX 371 397 {ECO:0000244|PDB:2AQJ}.
HELIX 405 412 {ECO:0000244|PDB:2AQJ}.
HELIX 418 429 {ECO:0000244|PDB:2AQJ}.
HELIX 440 445 {ECO:0000244|PDB:2AQJ}.
HELIX 447 452 {ECO:0000244|PDB:2AQJ}.
HELIX 457 467 {ECO:0000244|PDB:2AQJ}.
HELIX 476 480 {ECO:0000244|PDB:2AQJ}.
HELIX 482 505 {ECO:0000244|PDB:2AQJ}.
HELIX 509 516 {ECO:0000244|PDB:2AQJ}.
SEQUENCE 538 AA; 61075 MW; 03AAAC041A00CE7B CRC64;
MNKPIKNIVI VGGGTAGWMA ASYLVRALQQ QANITLIESA AIPRIGVGEA TIPSLQKVFF
DFLGIPEREW MPQVNGAFKA AIKFVNWRKS PDPSRDDHFY HLFGNVPNCD GVPLTHYWLR
KREQGFQQPM EYACYPQPGA LDGKLAPCLS DGTRQMSHAW HFDAHLVADF LKRWAVERGV
NRVVDEVVDV RLNNRGYISN LLTKEGRTLE ADLFIDCSGM RGLLINQALK EPFIDMSDYL
LCDSAVASAV PNDDARDGVE PYTSSIAMNS GWTWKIPMLG RFGSGYVFSS HFTSRDQATA
DFLKLWGLSD NQPLNQIKFR VGRNKRAWVN NCVSIGLSSC FLEPLESTGI YFIYAALYQL
VKHFPDTSFD PRLSDAFNAE IVHMFDDCRD FVQAHYFTTS RDDTPFWLAN RHDLRLSDAI
KEKVQRYKAG LPLTTTSFDD STYYETFDYE FKNFWLNGNY YCIFAGLGML PDRSLPLLQH
RPESIEKAEA MFASIRREAE RLRTSLPTNY DYLRSLRDGD AGLSRGQRGP KLAAQESL


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