PHZD_PSECL
ID PHZD_PSECL Reviewed; 222 AA.
AC Q51521;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Dihydrophenazinedicarboxylate synthase {ECO:0000250|UniProtKB:Q51793};
DE EC=1.10.3.16 {ECO:0000250|UniProtKB:Q51793};
DE AltName: Full=Phenazine biosynthesis protein PhzD;
GN Name=phzD {ECO:0000303|PubMed:8586283};
OS Pseudomonas chlororaphis (Pseudomonas aureofaciens).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PATHWAY.
RC STRAIN=30-84;
RX PubMed=8586283; DOI=10.1111/j.1574-6968.1995.tb07954.x;
RA Pierson L.S. III, Gaffney T., Lam S., Gong F.;
RT "Molecular analysis of genes encoding phenazine biosynthesis in the
RT biological control bacterium. Pseudomonas aureofaciens 30-84.";
RL FEMS Microbiol. Lett. 134:299-307(1995).
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 (Probable). Catalyzes
CC several oxidations in the terminal steps of core phenazine
CC biosynthesis. It oxidizes both hexahydrophenazine-1,6-dicarboxylic acid
CC (HHPDC) and tetrahydrophenazine-1-carboxylic acid (THPCA) and thereby
CC contributes to the generation of both phenazine-1,6-dicarboxylic acid
CC (PDC) and phenazine-1-carboxylic acid (PCA) (By similarity).
CC {ECO:0000250|UniProtKB:Q51793, ECO:0000305|PubMed:8586283}.
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:0000250|UniProtKB:Q51793};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49889;
CC Evidence={ECO:0000250|UniProtKB:Q51793};
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:0000250|UniProtKB:Q51793};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49893;
CC Evidence={ECO:0000250|UniProtKB:Q51793};
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:0000250|UniProtKB:Q51793};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49941;
CC Evidence={ECO:0000250|UniProtKB:Q51793};
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:0000250|UniProtKB:Q51793};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49949;
CC Evidence={ECO:0000250|UniProtKB:Q51793};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:Q51793};
CC Note=Binds 1 FMN per subunit. {ECO:0000250|UniProtKB:Q51793};
CC -!- PATHWAY: Antibiotic biosynthesis; phenazine biosynthesis.
CC {ECO:0000305|PubMed:8586283}.
CC -!- SIMILARITY: Belongs to the pyridoxamine 5'-phosphate oxidase family.
CC {ECO:0000305}.
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DR EMBL; L48339; AAB00332.1; -; Genomic_DNA.
DR AlphaFoldDB; Q51521; -.
DR SMR; Q51521; -.
DR BRENDA; 3.3.2.15; 5105.
DR UniPathway; UPA00099; -.
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 3: Inferred from homology;
KW Antibiotic biosynthesis; Flavoprotein; FMN; Oxidoreductase; Virulence.
FT CHAIN 1..222
FT /note="Dihydrophenazinedicarboxylate synthase"
FT /id="PRO_0000167789"
FT BINDING 18
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q51793"
FT BINDING 73..76
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q51793"
FT BINDING 88..89
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q51793"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q51793"
FT BINDING 94..95
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q51793"
FT BINDING 117
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q51793"
FT BINDING 139
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q51793"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q51793"
FT BINDING 152..153
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q51793"
FT BINDING 205
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q51793"
SQ SEQUENCE 222 AA; 25030 MW; 2A42148E0A0B8D71 CRC64;
MNSSVLGKPL LGKGMSESLT GTLDAPFPEY QKPPADPMSV LHNWLERARR VGIREPRALA
LATADSQGRP STRIVVISEI SDTGVLFSTH AGSQKGRELT ENPWASGTLY WRETSQQIIL
NGQAVRMPDA KADEAWLKRP YATHPMSSVS RQSEELKDVQ AMRNAARELA EVQGPLPRPE
GYCVFELRLE SLEFWGNGEE RLHERLRYDR SAEGWKHRRL QP
