PRNB_PSEFL
ID PRNB_PSEFL Reviewed; 361 AA.
AC P95481;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Monodechloroaminopyrrolnitrin synthase PrnB;
DE EC=1.14.19.- {ECO:0000269|PubMed:17924666, ECO:0000269|PubMed:9537395};
DE AltName: Full=7-chloro-L-tryptophan dioxygenase PrnB {ECO:0000305};
GN Name=prnB;
OS Pseudomonas fluorescens.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=294;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, AND
RP NOMENCLATURE.
RC STRAIN=Bl915;
RX PubMed=9172332; DOI=10.1128/aem.63.6.2147-2154.1997;
RA Hammer P.E., Hill D.S., Lam S.T., Van Pee K.H., Ligon J.M.;
RT "Four genes from Pseudomonas fluorescens that encode the biosynthesis of
RT pyrrolnitrin.";
RL Appl. Environ. Microbiol. 63:2147-2154(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, DISRUPTION
RP PHENOTYPE, AND SUBSTRATE SPECIFICITY.
RC STRAIN=Bl915;
RX PubMed=9537395; DOI=10.1128/jb.180.7.1939-1943.1998;
RA Kirner S., Hammer P.E., Hill D.S., Altmann A., Fischer I., Weislo L.J.,
RA Lanahan M., van Pee K.H., Ligon J.M.;
RT "Functions encoded by pyrrolnitrin biosynthetic genes from Pseudomonas
RT fluorescens.";
RL J. Bacteriol. 180:1939-1943(1998).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH HEME AND SUBSTRATE
RP ANALOGS, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF HIS-313, REACTION
RP MECHANISM, SUBUNIT, AND COFACTOR.
RX PubMed=17924666; DOI=10.1021/bi7012189;
RA De Laurentis W., Khim L., Anderson J.L., Adam A., Johnson K.A.,
RA Phillips R.S., Chapman S.K., van Pee K.H., Naismith J.H.;
RT "The second enzyme in pyrrolnitrin biosynthetic pathway is related to the
RT heme-dependent dioxygenase superfamily.";
RL Biochemistry 46:12393-12404(2007).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) IN COMPLEX WITH HEME AND SUBSTRATE
RP ANALOGS, MUTAGENESIS OF TYR-321 AND SER-332, SUBUNIT, AND COFACTOR.
RX PubMed=20421301; DOI=10.1074/jbc.m110.120485;
RA Zhu X., van Pee K.H., Naismith J.H.;
RT "The ternary complex of PrnB (the second enzyme in the pyrrolnitrin
RT biosynthesis pathway), tryptophan, and cyanide yields new mechanistic
RT insights into the indolamine dioxygenase superfamily.";
RL J. Biol. Chem. 285:21126-21133(2010).
CC -!- FUNCTION: Involved in the biosynthesis of the antifungal antibiotic
CC pyrrolnitrin. Catalyzes the ring rearrangement and decarboxylation to
CC convert 7-chloro-L-tryptophan (7-CLT) to monodechloroaminopyrrolnitrin
CC (MDA). It can also use 7-chloro-D-tryptophan, but 7-chloro-L-tryptophan
CC is the preferred natural enantiomer. {ECO:0000269|PubMed:17924666,
CC ECO:0000269|PubMed:9172332, ECO:0000269|PubMed:9537395}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7-chloro-L-tryptophan + AH2 + O2 = A + CO2 + 2 H2O +
CC monodechloroaminopyrrolnitrin; Xref=Rhea:RHEA:50952,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:17499, ChEBI:CHEBI:58713,
CC ChEBI:CHEBI:85785; Evidence={ECO:0000269|PubMed:17924666,
CC ECO:0000269|PubMed:9537395};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000269|PubMed:17924666, ECO:0000269|PubMed:20421301};
CC -!- PATHWAY: Antibiotic biosynthesis.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17924666,
CC ECO:0000269|PubMed:20421301}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene lose the ability to
CC produce pyrrolnitrin. {ECO:0000269|PubMed:9172332,
CC ECO:0000269|PubMed:9537395}.
CC -!- SIMILARITY: Belongs to the PrnB family. {ECO:0000305}.
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DR EMBL; U74493; AAB97505.1; -; Genomic_DNA.
DR PDB; 2V7I; X-ray; 1.75 A; A=1-361.
DR PDB; 2V7J; X-ray; 2.00 A; A=1-361.
DR PDB; 2V7K; X-ray; 1.70 A; A=1-361.
DR PDB; 2V7L; X-ray; 2.40 A; A=1-361.
DR PDB; 2V7M; X-ray; 2.00 A; A=1-361.
DR PDB; 2X66; X-ray; 2.09 A; A=1-361.
DR PDB; 2X67; X-ray; 2.16 A; A=1-361.
DR PDB; 2X68; X-ray; 2.13 A; A=1-361.
DR PDBsum; 2V7I; -.
DR PDBsum; 2V7J; -.
DR PDBsum; 2V7K; -.
DR PDBsum; 2V7L; -.
DR PDBsum; 2V7M; -.
DR PDBsum; 2X66; -.
DR PDBsum; 2X67; -.
DR PDBsum; 2X68; -.
DR AlphaFoldDB; P95481; -.
DR SMR; P95481; -.
DR PRIDE; P95481; -.
DR KEGG; ag:AAB97505; -.
DR BioCyc; MetaCyc:MON-16708; -.
DR EvolutionaryTrace; P95481; -.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0019441; P:tryptophan catabolic process to kynurenine; IEA:InterPro.
DR InterPro; IPR015029; PrnB.
DR InterPro; IPR037217; Trp/Indoleamine_2_3_dOase-like.
DR Pfam; PF08933; DUF1864; 1.
DR SUPFAM; SSF140959; SSF140959; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic biosynthesis; Heme; Iron; Metal-binding;
KW Oxidoreductase.
FT CHAIN 1..361
FT /note="Monodechloroaminopyrrolnitrin synthase PrnB"
FT /id="PRO_0000422331"
FT BINDING 222..225
FT /ligand="substrate"
FT BINDING 313
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 321
FT /ligand="substrate"
FT BINDING 332
FT /ligand="substrate"
FT MUTAGEN 313
FT /note="H->A: Loss of synthase activity."
FT /evidence="ECO:0000269|PubMed:17924666"
FT MUTAGEN 321
FT /note="Y->F: Loss of synthase activity."
FT /evidence="ECO:0000269|PubMed:20421301"
FT MUTAGEN 332
FT /note="S->A: Loss of synthase activity."
FT /evidence="ECO:0000269|PubMed:20421301"
FT HELIX 8..19
FT /evidence="ECO:0007829|PDB:2V7K"
FT HELIX 27..30
FT /evidence="ECO:0007829|PDB:2V7K"
FT HELIX 33..38
FT /evidence="ECO:0007829|PDB:2V7K"
FT HELIX 42..50
FT /evidence="ECO:0007829|PDB:2V7K"
FT HELIX 64..83
FT /evidence="ECO:0007829|PDB:2V7K"
FT HELIX 88..91
FT /evidence="ECO:0007829|PDB:2V7K"
FT HELIX 95..106
FT /evidence="ECO:0007829|PDB:2V7K"
FT HELIX 114..117
FT /evidence="ECO:0007829|PDB:2V7K"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:2V7K"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:2V7K"
FT HELIX 135..162
FT /evidence="ECO:0007829|PDB:2V7K"
FT HELIX 169..195
FT /evidence="ECO:0007829|PDB:2V7K"
FT HELIX 198..204
FT /evidence="ECO:0007829|PDB:2V7K"
FT HELIX 206..209
FT /evidence="ECO:0007829|PDB:2V7K"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:2V7K"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:2V7K"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:2V7K"
FT HELIX 229..236
FT /evidence="ECO:0007829|PDB:2V7K"
FT TURN 237..240
FT /evidence="ECO:0007829|PDB:2V7K"
FT HELIX 244..253
FT /evidence="ECO:0007829|PDB:2V7K"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:2V7K"
FT HELIX 259..269
FT /evidence="ECO:0007829|PDB:2V7K"
FT HELIX 274..285
FT /evidence="ECO:0007829|PDB:2V7K"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:2V7M"
FT HELIX 290..321
FT /evidence="ECO:0007829|PDB:2V7K"
FT HELIX 338..356
FT /evidence="ECO:0007829|PDB:2V7K"
SQ SEQUENCE 361 AA; 39921 MW; 17C3152231E8E2DE CRC64;
MERTLDRVGV FAATHAAVAA CDPLQARALV LQLPGLNRNK DVPGIVGLLR EFLPVRGLPC
GWGFVEAAAA MRDIGFFLGS LKRHGHEPAE VVPGLEPVLL DLARATNLPP RETLLHVTVW
NPTAADAQRS YTGLPDEAHL LESVRISMAA LEAAIALTVE LFDVSLRSPE FAQRCDELEA
YLQKMVESIV YAYRFISPQV FYDELRPFYE PIRVGGQSYL GPGAVEMPLF VLEHVLWGSQ
SDDQTYREFK ETYLPYVLPA YRAVYARFSG EPALIDRALD EARAVGTRDE HVRAGLTALE
RVFKVLLRFR APHLKLAERA YEVGQSGPEI GSGGYAPSML GELLTLTYAA RSRVRAALDE
S
