PLTA_PSEF5
ID PLTA_PSEF5 Reviewed; 449 AA.
AC Q4KCZ0; Q9X3R1;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=1H-pyrrole-2-carbonyl-[peptidyl-carrier protein] chlorinase {ECO:0000305};
DE EC=1.14.19.56 {ECO:0000269|PubMed:16162666};
DE AltName: Full=FADH2-dependent halogenase PltA {ECO:0000303|PubMed:16162666};
GN Name=pltA {ECO:0000303|PubMed:10094695};
GN OrderedLocusNames=PFL_2787 {ECO:0000312|EMBL:AAY92059.1};
OS Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=220664;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5;
RX PubMed=10094695; DOI=10.1128/jb.181.7.2166-2174.1999;
RA Nowak-Thompson B., Chaney N., Wing J.S., Gould S.J., Loper J.E.;
RT "Characterization of the pyoluteorin biosynthetic gene cluster of
RT Pseudomonas fluorescens Pf-5.";
RL J. Bacteriol. 181:2166-2174(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5;
RX PubMed=15980861; DOI=10.1038/nbt1110;
RA Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.A.,
RA Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A., Rosovitz M.J.,
RA Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W., Nelson W.C.,
RA Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A., Pierson L.S. III,
RA Thomashow L.S., Loper J.E.;
RT "Complete genome sequence of the plant commensal Pseudomonas fluorescens
RT Pf-5.";
RL Nat. Biotechnol. 23:873-878(2005).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5;
RX PubMed=16162666; DOI=10.1073/pnas.0506964102;
RA Dorrestein P.C., Yeh E., Garneau-Tsodikova S., Kelleher N.L., Walsh C.T.;
RT "Dichlorination of a pyrrolyl-S-carrier protein by FADH2-dependent
RT halogenase PltA during pyoluteorin biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:13843-13848(2005).
RN [4] {ECO:0007744|PDB:5DBJ}
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) IN COMPLEX WITH FAD AND CHLORIDE,
RP SUBUNIT, AND DOMAIN.
RC STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5;
RX PubMed=26416533; DOI=10.1016/j.jsb.2015.09.013;
RA Pang A.H., Garneau-Tsodikova S., Tsodikov O.V.;
RT "Crystal structure of halogenase PltA from the pyoluteorin biosynthetic
RT pathway.";
RL J. Struct. Biol. 192:349-357(2015).
CC -!- FUNCTION: Involved in the biosynthesis of the antibiotic pyoluteorin
CC (PubMed:16162666). Catalyzes the dichlorination of the pyrrole ring of
CC pyrrolyl-S-PltL, generating the 5-chloropyrrolyl-S-PltL intermediate
CC and then the 4,5-dichloropyrrolyl-S-PltL product (PubMed:16162666).
CC {ECO:0000269|PubMed:16162666}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(1H-pyrrole-2-carbonyl)-[peptidyl-carrier protein] + 2
CC chloride + 2 FADH2 + 2 O2 = (4,5-dichloro-1H-pyrrole-2-carbonyl)-
CC [peptidyl-carrier protein] + 2 FAD + 4 H2O; Xref=Rhea:RHEA:56380,
CC Rhea:RHEA-COMP:14110, Rhea:RHEA-COMP:14498, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17996, ChEBI:CHEBI:57692,
CC ChEBI:CHEBI:58307, ChEBI:CHEBI:138623, ChEBI:CHEBI:140219;
CC EC=1.14.19.56; Evidence={ECO:0000269|PubMed:16162666};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56381;
CC Evidence={ECO:0000269|PubMed:16162666};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(1H-pyrrole-2-carbonyl)-[peptidyl-carrier protein] + chloride
CC + FADH2 + O2 = (5-chloro-1H-pyrrole-2-carbonyl)-[peptidyl-carrier
CC protein] + FAD + 2 H2O; Xref=Rhea:RHEA:56384, Rhea:RHEA-COMP:14110,
CC Rhea:RHEA-COMP:14497, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:17996, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC ChEBI:CHEBI:138623, ChEBI:CHEBI:140221;
CC Evidence={ECO:0000269|PubMed:16162666};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56385;
CC Evidence={ECO:0000269|PubMed:16162666};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5-chloro-1H-pyrrole-2-carbonyl)-[peptidyl-carrier protein] +
CC chloride + FADH2 + O2 = (4,5-dichloro-1H-pyrrole-2-carbonyl)-
CC [peptidyl-carrier protein] + FAD + 2 H2O; Xref=Rhea:RHEA:56388,
CC Rhea:RHEA-COMP:14497, Rhea:RHEA-COMP:14498, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17996, ChEBI:CHEBI:57692,
CC ChEBI:CHEBI:58307, ChEBI:CHEBI:140219, ChEBI:CHEBI:140221;
CC Evidence={ECO:0000269|PubMed:16162666};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56389;
CC Evidence={ECO:0000269|PubMed:16162666};
CC -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000269|PubMed:16162666}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:26416533}.
CC -!- DOMAIN: Contains an additional unique helical region at the C-terminus.
CC This C-terminal region blocks a putative substrate-binding cleft,
CC suggesting that a conformational change involving repositioning of this
CC region is necessary to allow binding of the pyrrolyl-S-PltL substrate
CC for its dichlorination by PltA. {ECO:0000269|PubMed:26416533}.
CC -!- SIMILARITY: Belongs to the flavin-dependent halogenase family.
CC {ECO:0000305}.
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DR EMBL; AF081920; AAD24884.1; -; Genomic_DNA.
DR EMBL; CP000076; AAY92059.1; -; Genomic_DNA.
DR PIR; T17419; T17419.
DR RefSeq; WP_011061079.1; NC_004129.6.
DR PDB; 5DBJ; X-ray; 2.75 A; A/B/C/D/E=1-449.
DR PDBsum; 5DBJ; -.
DR AlphaFoldDB; Q4KCZ0; -.
DR SMR; Q4KCZ0; -.
DR STRING; 220664.PFL_2787; -.
DR PRIDE; Q4KCZ0; -.
DR EnsemblBacteria; AAY92059; AAY92059; PFL_2787.
DR GeneID; 57475838; -.
DR KEGG; pfl:PFL_2787; -.
DR PATRIC; fig|220664.5.peg.2843; -.
DR eggNOG; COG0644; Bacteria.
DR HOGENOM; CLU_024648_4_0_6; -.
DR OMA; RFVDPIF; -.
DR OrthoDB; 1770293at2; -.
DR BioCyc; MetaCyc:MON-20315; -.
DR BRENDA; 1.14.19.56; 5121.
DR Proteomes; UP000008540; Chromosome.
DR GO; GO:0047651; F:alkylhalidase activity; IDA:JCVI.
DR GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR006905; Flavin_halogenase.
DR Pfam; PF04820; Trp_halogenase; 2.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic biosynthesis; Chloride; FAD; Flavoprotein;
KW Nucleotide-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..449
FT /note="1H-pyrrole-2-carbonyl-[peptidyl-carrier protein]
FT chlorinase"
FT /id="PRO_0000452248"
FT BINDING 15..16
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:26416533,
FT ECO:0007744|PDB:5DBJ"
FT BINDING 36
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:26416533,
FT ECO:0007744|PDB:5DBJ"
FT BINDING 41..47
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:26416533,
FT ECO:0007744|PDB:5DBJ"
FT BINDING 123
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:26416533,
FT ECO:0007744|PDB:5DBJ"
FT BINDING 147
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:26416533,
FT ECO:0007744|PDB:5DBJ"
FT BINDING 316
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:26416533,
FT ECO:0007744|PDB:5DBJ"
FT BINDING 327..328
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000269|PubMed:26416533,
FT ECO:0007744|PDB:5DBJ"
FT BINDING 329
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:26416533,
FT ECO:0007744|PDB:5DBJ"
FT STRAND 5..11
FT /evidence="ECO:0007829|PDB:5DBJ"
FT HELIX 15..26
FT /evidence="ECO:0007829|PDB:5DBJ"
FT STRAND 31..37
FT /evidence="ECO:0007829|PDB:5DBJ"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:5DBJ"
FT HELIX 53..58
FT /evidence="ECO:0007829|PDB:5DBJ"
FT HELIX 62..66
FT /evidence="ECO:0007829|PDB:5DBJ"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:5DBJ"
FT STRAND 75..82
FT /evidence="ECO:0007829|PDB:5DBJ"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:5DBJ"
FT STRAND 95..104
FT /evidence="ECO:0007829|PDB:5DBJ"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:5DBJ"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:5DBJ"
FT HELIX 123..136
FT /evidence="ECO:0007829|PDB:5DBJ"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:5DBJ"
FT STRAND 146..154
FT /evidence="ECO:0007829|PDB:5DBJ"
FT STRAND 157..166
FT /evidence="ECO:0007829|PDB:5DBJ"
FT STRAND 168..178
FT /evidence="ECO:0007829|PDB:5DBJ"
FT HELIX 185..189
FT /evidence="ECO:0007829|PDB:5DBJ"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:5DBJ"
FT STRAND 201..209
FT /evidence="ECO:0007829|PDB:5DBJ"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:5DBJ"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:5DBJ"
FT STRAND 237..246
FT /evidence="ECO:0007829|PDB:5DBJ"
FT STRAND 248..255
FT /evidence="ECO:0007829|PDB:5DBJ"
FT HELIX 256..262
FT /evidence="ECO:0007829|PDB:5DBJ"
FT HELIX 266..274
FT /evidence="ECO:0007829|PDB:5DBJ"
FT HELIX 278..286
FT /evidence="ECO:0007829|PDB:5DBJ"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:5DBJ"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:5DBJ"
FT STRAND 301..304
FT /evidence="ECO:0007829|PDB:5DBJ"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:5DBJ"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:5DBJ"
FT HELIX 315..317
FT /evidence="ECO:0007829|PDB:5DBJ"
FT HELIX 328..349
FT /evidence="ECO:0007829|PDB:5DBJ"
FT HELIX 354..357
FT /evidence="ECO:0007829|PDB:5DBJ"
FT HELIX 358..381
FT /evidence="ECO:0007829|PDB:5DBJ"
FT HELIX 382..384
FT /evidence="ECO:0007829|PDB:5DBJ"
FT HELIX 385..390
FT /evidence="ECO:0007829|PDB:5DBJ"
FT HELIX 392..402
FT /evidence="ECO:0007829|PDB:5DBJ"
FT HELIX 414..427
FT /evidence="ECO:0007829|PDB:5DBJ"
FT STRAND 429..431
FT /evidence="ECO:0007829|PDB:5DBJ"
FT HELIX 434..436
FT /evidence="ECO:0007829|PDB:5DBJ"
SQ SEQUENCE 449 AA; 50677 MW; 0D761E587B9B16DE CRC64;
MSDHDYDVVI IGGGPAGSTM ASYLAKAGVK CAVFEKELFE REHVGESLVP ATTPVLLEIG
VMEKIEKANF PKKFGAAWTS ADSGPEDKMG FQGLDHDFRS AEILFNERKQ EGVDRDFTFH
VDRGKFDRIL LEHAGSLGAK VFQGVEIADV EFLSPGNVIV NAKLGKRSVE IKAKMVVDAS
GRNVLLGRRL GLREKDPVFN QFAIHSWFDN FDRKSATQSP DKVDYIFIHF LPMTNTWVWQ
IPITETITSV GVVTQKQNYT NSDLTYEEFF WEAVKTRENL HDALKASEQV RPFKKEADYS
YGMKEVCGDS FVLIGDAARF VDPIFSSGVS VALNSARIAS GDIIEAVKNN DFSKSSFTHY
EGMIRNGIKN WYEFITLYYR LNILFTAFVQ DPRYRLDILQ LLQGDVYSGK RLEVLDKMRE
IIAAVESDPE HLWHKYLGDM QVPTAKPAF
