PHZG_PSEFL
ID PHZG_PSEFL Reviewed; 222 AA.
AC Q51793;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Dihydrophenazinedicarboxylate synthase {ECO:0000305};
DE EC=1.10.3.16 {ECO:0000269|PubMed:23897464};
DE AltName: Full=Phenazine biosynthesis protein PhzG;
GN Name=phzG {ECO:0000303|PubMed:9573209};
OS Pseudomonas fluorescens.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=294;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RC STRAIN=NRRL B-15132 / 2-79;
RX PubMed=9573209; DOI=10.1128/jb.180.9.2541-2548.1998;
RA Mavrodi D.V., Ksenzenko V.N., Bonsall R.F., Cook R.J., Boronin A.M.,
RA Thomashow L.S.;
RT "A seven-gene locus for synthesis of phenazine-1-carboxylic acid by
RT Pseudomonas fluorescens 2-79.";
RL J. Bacteriol. 180:2541-2548(1998).
RN [2] {ECO:0007744|PDB:1TY9}
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH FMN, COFACTOR, AND
RP SUBUNIT.
RX PubMed=15502343; DOI=10.1107/s0907444904022474;
RA Parsons J.F., Calabrese K., Eisenstein E., Ladner J.E.;
RT "Structure of the phenazine biosynthesis enzyme PhzG.";
RL Acta Crystallogr. D 60:2110-2113(2004).
RN [3] {ECO:0007744|PDB:4HMS, ECO:0007744|PDB:4HMT, ECO:0007744|PDB:4HMU, ECO:0007744|PDB:4HMV}
RP X-RAY CRYSTALLOGRAPHY (1.33 ANGSTROMS) IN COMPLEXES WITH FMN AND TRAPPED
RP UNSTABLE INTERMEDIATES, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND
RP PATHWAY.
RC STRAIN=NRRL B-15132 / 2-79;
RX PubMed=23897464; DOI=10.1107/s0907444913008354;
RA Xu N., Ahuja E.G., Janning P., Mavrodi D.V., Thomashow L.S.,
RA Blankenfeldt W.;
RT "Trapped intermediates in crystals of the FMN-dependent oxidase PhzG
RT provide insight into the final steps of phenazine biosynthesis.";
RL Acta Crystallogr. D 69:1403-1413(2013).
CC -!- FUNCTION: Involved in the biosynthesis of the antibiotic phenazine, a
CC nitrogen-containing heterocyclic molecule having important roles in
CC virulence, competition and biological control (PubMed:9573209,
CC PubMed:23897464). Catalyzes several oxidations in the terminal steps of
CC core phenazine biosynthesis. It oxidizes both hexahydrophenazine-1,6-
CC dicarboxylic acid (HHPDC) and tetrahydrophenazine-1-carboxylic acid
CC (THPCA) and thereby contributes to the generation of both phenazine-
CC 1,6-dicarboxylic acid (PDC) and phenazine-1-carboxylic acid (PCA). It
CC synthesizes phenazines in their reduced form, which are the likely end
CC products in vivo (PubMed:23897464). {ECO:0000269|PubMed:23897464,
CC ECO:0000269|PubMed:9573209}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(1R,6R)-1,4,5,5a,6,9-hexahydrophenazine-1,6-dicarboxylate + O2
CC = (1R,10aS)-1,4,10,10a-tetrahydrophenazine-1,6-dicarboxylate + H2O2;
CC Xref=Rhea:RHEA:49888, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:131971, ChEBI:CHEBI:131973; EC=1.10.3.16;
CC Evidence={ECO:0000269|PubMed:23897464};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49889;
CC Evidence={ECO:0000269|PubMed:23897464};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(1R,10aS)-1,4,10,10a-tetrahydrophenazine-1,6-dicarboxylate +
CC O2 = (5aS)-5,5a-dihydrophenazine-1,6-dicarboxylate + H2O2;
CC Xref=Rhea:RHEA:49892, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:131973, ChEBI:CHEBI:131978; EC=1.10.3.16;
CC Evidence={ECO:0000269|PubMed:23897464};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49893;
CC Evidence={ECO:0000269|PubMed:23897464};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(1R,10aS)-1,4,10,10a-tetrahydrophenazine-1-carboxylate + O2 =
CC (10aS)-10,10a-dihydrophenazine-1-carboxylate + H2O2;
CC Xref=Rhea:RHEA:49940, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:131981, ChEBI:CHEBI:132003; EC=1.10.3.16;
CC Evidence={ECO:0000269|PubMed:23897464};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49941;
CC Evidence={ECO:0000269|PubMed:23897464};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(1R)-1,4,5,10-tetrahydrophenazine-1-carboxylate + O2 = (10aS)-
CC 10,10a-dihydrophenazine-1-carboxylate + H2O2; Xref=Rhea:RHEA:49948,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:132003,
CC ChEBI:CHEBI:132005; EC=1.10.3.16;
CC Evidence={ECO:0000269|PubMed:23897464};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49949;
CC Evidence={ECO:0000269|PubMed:23897464};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:15502343, ECO:0000269|PubMed:23897464};
CC Note=Binds 1 FMN per subunit. {ECO:0000269|PubMed:15502343,
CC ECO:0000269|PubMed:23897464};
CC -!- PATHWAY: Antibiotic biosynthesis; phenazine biosynthesis.
CC {ECO:0000269|PubMed:23897464, ECO:0000269|PubMed:9573209}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15502343}.
CC -!- SIMILARITY: Belongs to the pyridoxamine 5'-phosphate oxidase family.
CC {ECO:0000305}.
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DR EMBL; L48616; AAC18906.1; -; Genomic_DNA.
DR RefSeq; WP_043050176.1; NZ_JXCQ01000041.1.
DR PDB; 1TY9; X-ray; 1.80 A; A/B=1-222.
DR PDB; 4HMS; X-ray; 1.33 A; A/B=1-222.
DR PDB; 4HMT; X-ray; 1.42 A; A/B=1-222.
DR PDB; 4HMU; X-ray; 1.56 A; A/B=1-222.
DR PDB; 4HMV; X-ray; 1.45 A; A/B=1-222.
DR PDBsum; 1TY9; -.
DR PDBsum; 4HMS; -.
DR PDBsum; 4HMT; -.
DR PDBsum; 4HMU; -.
DR PDBsum; 4HMV; -.
DR AlphaFoldDB; Q51793; -.
DR SMR; Q51793; -.
DR DrugBank; DB03247; Flavin mononucleotide.
DR BioCyc; MetaCyc:MON-16114; -.
DR BRENDA; 1.10.3.16; 5121.
DR UniPathway; UPA00099; -.
DR EvolutionaryTrace; Q51793; -.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0004733; F:pyridoxamine-phosphate oxidase activity; IEA:InterPro.
DR GO; GO:0002047; P:phenazine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:InterPro.
DR Gene3D; 2.30.110.10; -; 1.
DR InterPro; IPR000659; Pyridox_Oxase.
DR InterPro; IPR019740; Pyridox_Oxase_CS.
DR InterPro; IPR011576; Pyridox_Oxase_put.
DR InterPro; IPR019576; Pyridoxamine_oxidase_dimer_C.
DR InterPro; IPR012349; Split_barrel_FMN-bd.
DR PANTHER; PTHR10851; PTHR10851; 1.
DR Pfam; PF10590; PNP_phzG_C; 1.
DR Pfam; PF01243; Putative_PNPOx; 1.
DR PIRSF; PIRSF000190; Pyd_amn-ph_oxd; 1.
DR PROSITE; PS01064; PYRIDOX_OXIDASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic biosynthesis; Flavoprotein; FMN; Oxidoreductase;
KW Virulence.
FT CHAIN 1..222
FT /note="Dihydrophenazinedicarboxylate synthase"
FT /id="PRO_0000167790"
FT BINDING 18
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23897464,
FT ECO:0007744|PDB:4HMT, ECO:0007744|PDB:4HMU,
FT ECO:0007744|PDB:4HMV"
FT BINDING 73..76
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:15502343,
FT ECO:0000269|PubMed:23897464, ECO:0007744|PDB:1TY9,
FT ECO:0007744|PDB:4HMS, ECO:0007744|PDB:4HMT,
FT ECO:0007744|PDB:4HMU, ECO:0007744|PDB:4HMV"
FT BINDING 88..89
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:15502343,
FT ECO:0000269|PubMed:23897464, ECO:0007744|PDB:1TY9,
FT ECO:0007744|PDB:4HMS, ECO:0007744|PDB:4HMT,
FT ECO:0007744|PDB:4HMU, ECO:0007744|PDB:4HMV"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23897464,
FT ECO:0007744|PDB:4HMT"
FT BINDING 94..95
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:15502343,
FT ECO:0000269|PubMed:23897464, ECO:0007744|PDB:1TY9,
FT ECO:0007744|PDB:4HMS, ECO:0007744|PDB:4HMT,
FT ECO:0007744|PDB:4HMU, ECO:0007744|PDB:4HMV"
FT BINDING 117
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:15502343,
FT ECO:0000269|PubMed:23897464, ECO:0007744|PDB:1TY9,
FT ECO:0007744|PDB:4HMS, ECO:0007744|PDB:4HMT,
FT ECO:0007744|PDB:4HMU, ECO:0007744|PDB:4HMV"
FT BINDING 139
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23897464,
FT ECO:0007744|PDB:4HMT, ECO:0007744|PDB:4HMU,
FT ECO:0007744|PDB:4HMV"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23897464,
FT ECO:0007744|PDB:4HMT"
FT BINDING 152..153
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:15502343,
FT ECO:0000269|PubMed:23897464, ECO:0007744|PDB:1TY9,
FT ECO:0007744|PDB:4HMS, ECO:0007744|PDB:4HMT,
FT ECO:0007744|PDB:4HMU, ECO:0007744|PDB:4HMV"
FT BINDING 205
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:15502343,
FT ECO:0000269|PubMed:23897464, ECO:0007744|PDB:1TY9,
FT ECO:0007744|PDB:4HMS, ECO:0007744|PDB:4HMT,
FT ECO:0007744|PDB:4HMU, ECO:0007744|PDB:4HMV"
FT HELIX 29..32
FT /evidence="ECO:0007829|PDB:4HMS"
FT HELIX 37..51
FT /evidence="ECO:0007829|PDB:4HMS"
FT STRAND 58..64
FT /evidence="ECO:0007829|PDB:4HMS"
FT STRAND 70..76
FT /evidence="ECO:0007829|PDB:4HMS"
FT STRAND 82..90
FT /evidence="ECO:0007829|PDB:4HMS"
FT HELIX 94..101
FT /evidence="ECO:0007829|PDB:4HMS"
FT STRAND 104..111
FT /evidence="ECO:0007829|PDB:4HMS"
FT TURN 112..115
FT /evidence="ECO:0007829|PDB:4HMS"
FT STRAND 116..126
FT /evidence="ECO:0007829|PDB:4HMS"
FT HELIX 129..138
FT /evidence="ECO:0007829|PDB:4HMS"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:4HMS"
FT HELIX 144..149
FT /evidence="ECO:0007829|PDB:4HMS"
FT HELIX 159..170
FT /evidence="ECO:0007829|PDB:4HMS"
FT STRAND 182..199
FT /evidence="ECO:0007829|PDB:4HMS"
FT STRAND 202..210
FT /evidence="ECO:0007829|PDB:4HMS"
FT STRAND 212..220
FT /evidence="ECO:0007829|PDB:4HMS"
SQ SEQUENCE 222 AA; 24935 MW; 732F3DB6AB029AD4 CRC64;
MNGSIQGKPL LGKGMSESLT GTLDAPFPEY QTLPADPMSV LHNWLERARR VGIREPRALA
LATADSQGRP STRIVVISEI SDAGVVFSTH AGSQKGRELL HNPWASGVLY WRETSQQIIL
NGQAVRLPNA KADDAWLKRP YATHPMSSVS RQSEELQDVQ AMRNAARQLA ELQGPLPRPE
GYCVFELRLE SLEFWGNGQE RLHERLRYDR SDTGWNVRRL QP
