PHZG_BURL3
ID PHZG_BURL3 Reviewed; 212 AA.
AC Q396C5;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Dihydrophenazinedicarboxylate synthase {ECO:0000305};
DE EC=1.10.3.16 {ECO:0000269|PubMed:23897464};
GN Name=phzG {ECO:0000303|PubMed:23897464};
GN OrderedLocusNames=Bcep18194_B1572 {ECO:0000312|EMBL:ABB11686.1};
OS Burkholderia lata (strain ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 /
OS R18194 / 383).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=482957;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 / R18194 / 383;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A.,
RA Richardson P.;
RT "Complete sequence of chromosome 2 of Burkholderia sp. 383.";
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007744|PDB:4HMW, ECO:0007744|PDB:4HMX}
RP X-RAY CRYSTALLOGRAPHY (1.53 ANGSTROMS) IN COMPLEX WITH FMN AND TRAPPED
RP UNSTABLE INTERMEDIATE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND PATHWAY.
RC STRAIN=ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 / R18194 / 383;
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:23897464).
CC Catalyzes 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). It synthesizes phenazines
CC in their reduced form, which are the likely end products in vivo
CC (PubMed:23897464). {ECO:0000269|PubMed:23897464}.
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:23897464};
CC Note=Binds 1 FMN per subunit. {ECO:0000269|PubMed:23897464};
CC -!- PATHWAY: Antibiotic biosynthesis; phenazine biosynthesis.
CC {ECO:0000269|PubMed:23897464}.
CC -!- SIMILARITY: Belongs to the pyridoxamine 5'-phosphate oxidase family.
CC {ECO:0000305}.
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DR EMBL; CP000152; ABB11686.1; -; Genomic_DNA.
DR RefSeq; WP_011355175.1; NC_007511.1.
DR PDB; 4HMW; X-ray; 1.53 A; A/B=1-212.
DR PDB; 4HMX; X-ray; 1.59 A; A/B=1-212.
DR PDBsum; 4HMW; -.
DR PDBsum; 4HMX; -.
DR AlphaFoldDB; Q396C5; -.
DR SMR; Q396C5; -.
DR EnsemblBacteria; ABB11686; ABB11686; Bcep18194_B1572.
DR GeneID; 45097913; -.
DR KEGG; bur:Bcep18194_B1572; -.
DR PATRIC; fig|482957.22.peg.5285; -.
DR HOGENOM; CLU_032263_2_3_4; -.
DR OMA; FYWPVLG; -.
DR OrthoDB; 1542844at2; -.
DR BRENDA; 1.10.3.16; 13531.
DR UniPathway; UPA00099; -.
DR Proteomes; UP000002705; Chromosome 2.
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; 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.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic biosynthesis; Flavoprotein; FMN; Oxidoreductase;
KW Virulence.
FT CHAIN 1..212
FT /note="Dihydrophenazinedicarboxylate synthase"
FT /id="PRO_0000452088"
FT BINDING 8
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q51793"
FT BINDING 63..66
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:23897464,
FT ECO:0007744|PDB:4HMW, ECO:0007744|PDB:4HMX"
FT BINDING 78..79
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:23897464,
FT ECO:0007744|PDB:4HMW, ECO:0007744|PDB:4HMX"
FT BINDING 80
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q51793"
FT BINDING 84..85
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:23897464,
FT ECO:0007744|PDB:4HMW, ECO:0007744|PDB:4HMX"
FT BINDING 107
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:23897464,
FT ECO:0007744|PDB:4HMW, ECO:0007744|PDB:4HMX"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q51793"
FT BINDING 137
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q51793"
FT BINDING 142..143
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:23897464,
FT ECO:0007744|PDB:4HMW, ECO:0007744|PDB:4HMX"
FT BINDING 195
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:23897464,
FT ECO:0007744|PDB:4HMW, ECO:0007744|PDB:4HMX"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:4HMW"
FT HELIX 27..40
FT /evidence="ECO:0007829|PDB:4HMW"
FT STRAND 48..54
FT /evidence="ECO:0007829|PDB:4HMW"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:4HMW"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:4HMW"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:4HMW"
FT HELIX 84..92
FT /evidence="ECO:0007829|PDB:4HMW"
FT STRAND 94..101
FT /evidence="ECO:0007829|PDB:4HMW"
FT TURN 102..105
FT /evidence="ECO:0007829|PDB:4HMW"
FT STRAND 106..116
FT /evidence="ECO:0007829|PDB:4HMW"
FT HELIX 119..127
FT /evidence="ECO:0007829|PDB:4HMW"
FT HELIX 131..139
FT /evidence="ECO:0007829|PDB:4HMW"
FT HELIX 149..161
FT /evidence="ECO:0007829|PDB:4HMW"
FT STRAND 172..186
FT /evidence="ECO:0007829|PDB:4HMW"
FT STRAND 194..201
FT /evidence="ECO:0007829|PDB:4HMW"
FT STRAND 204..210
FT /evidence="ECO:0007829|PDB:4HMW"
SQ SEQUENCE 212 AA; 23910 MW; 02BB4C2E50EAA423 CRC64;
MNTSRFESLT GSVDVLFPEY DDPPSEPITL LKRWLATADV ARVREPKALA LATATSDGRI
SSRVIAFSSI DDRGVIFCTH STSRKGRELT ETGWASGLLY WRETGQQIMI SGQAVPLEES
ENDKLWFGRS VPMHAMSSAS HQSDELVDRE ALRAHAAELL ALGVALPRPP RFVGYRLEPH
EMEFWAASSD RLHRRLRYER DGNDWKTTQL QP
