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Protein

Phenazine biosynthesis protein PhzG

Gene

phzG

Organism
Pseudomonas fluorescens
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the biosynthesis of the antibiotic phenazine, a nitrogen-containing heterocyclic molecule having important roles in virulence, competition and biological control. Probably catalyzes the final step in the conversion of trans-2,3-dihydro-3-hydroxyanthranilic acid (DHHA) to phenazine-1-carboxylic acid (PCA).

Cofactori

FMN1 PublicationNote: Binds 1 FMN per subunit.1 Publication

Pathwayi: phenazine biosynthesis

This protein is involved in the pathway phenazine biosynthesis, which is part of Antibiotic biosynthesis.
View all proteins of this organism that are known to be involved in the pathway phenazine biosynthesis and in Antibiotic biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei95 – 951FMN1 Publication
Binding sitei117 – 1171FMN1 Publication
Binding sitei153 – 1531FMN1 Publication
Binding sitei205 – 2051FMN1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi73 – 764FMN1 Publication
Nucleotide bindingi88 – 892FMN1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Antibiotic biosynthesis, Virulence

Keywords - Ligandi

Flavoprotein, FMN

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16114.
UniPathwayiUPA00099.

Names & Taxonomyi

Protein namesi
Recommended name:
Phenazine biosynthesis protein PhzG (EC:1.4.-.-)
Gene namesi
Name:phzG
OrganismiPseudomonas fluorescens
Taxonomic identifieri294 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 222222Phenazine biosynthesis protein PhzGPRO_0000167790Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1
222
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi29 – 324Combined sources
Helixi37 – 5115Combined sources
Beta strandi58 – 647Combined sources
Beta strandi70 – 767Combined sources
Beta strandi82 – 909Combined sources
Helixi94 – 1018Combined sources
Beta strandi104 – 1118Combined sources
Turni112 – 1154Combined sources
Beta strandi116 – 12611Combined sources
Helixi129 – 13810Combined sources
Helixi141 – 1433Combined sources
Helixi144 – 1496Combined sources
Helixi159 – 17012Combined sources
Beta strandi182 – 19918Combined sources
Beta strandi202 – 2109Combined sources
Beta strandi212 – 2209Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TY9X-ray1.80A/B1-222[»]
4HMSX-ray1.33A/B1-222[»]
4HMTX-ray1.42A/B1-222[»]
4HMUX-ray1.56A/B1-222[»]
4HMVX-ray1.45A/B1-222[»]
ProteinModelPortaliQ51793.
SMRiQ51793. Positions 16-222.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ51793.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di2.30.110.10. 1 hit.
InterProiIPR000659. Pyridox_Oxase.
IPR019740. Pyridox_Oxase_CS.
IPR011576. Pyridox_Oxase_FMN-bd.
IPR019576. Pyridoxamine_oxidase_dimer_C.
IPR012349. Split_barrel_FMN-bd.
[Graphical view]
PfamiPF10590. PNPOx_C. 1 hit.
PF01243. Pyridox_oxidase. 1 hit.
[Graphical view]
PIRSFiPIRSF000190. Pyd_amn-ph_oxd. 1 hit.
SUPFAMiSSF50475. SSF50475. 1 hit.
PROSITEiPS01064. PYRIDOX_OXIDASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q51793-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNGSIQGKPL LGKGMSESLT GTLDAPFPEY QTLPADPMSV LHNWLERARR
60 70 80 90 100
VGIREPRALA LATADSQGRP STRIVVISEI SDAGVVFSTH AGSQKGRELL
110 120 130 140 150
HNPWASGVLY WRETSQQIIL NGQAVRLPNA KADDAWLKRP YATHPMSSVS
160 170 180 190 200
RQSEELQDVQ AMRNAARQLA ELQGPLPRPE GYCVFELRLE SLEFWGNGQE
210 220
RLHERLRYDR SDTGWNVRRL QP
Length:222
Mass (Da):24,935
Last modified:November 1, 1997 - v1
Checksum:i732F3DB6AB029AD4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L48616 Genomic DNA. Translation: AAC18906.1.
RefSeqiWP_043050176.1. NZ_JXCQ01000041.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L48616 Genomic DNA. Translation: AAC18906.1.
RefSeqiWP_043050176.1. NZ_JXCQ01000041.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TY9X-ray1.80A/B1-222[»]
4HMSX-ray1.33A/B1-222[»]
4HMTX-ray1.42A/B1-222[»]
4HMUX-ray1.56A/B1-222[»]
4HMVX-ray1.45A/B1-222[»]
ProteinModelPortaliQ51793.
SMRiQ51793. Positions 16-222.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00099.
BioCyciMetaCyc:MONOMER-16114.

Miscellaneous databases

EvolutionaryTraceiQ51793.

Family and domain databases

Gene3Di2.30.110.10. 1 hit.
InterProiIPR000659. Pyridox_Oxase.
IPR019740. Pyridox_Oxase_CS.
IPR011576. Pyridox_Oxase_FMN-bd.
IPR019576. Pyridoxamine_oxidase_dimer_C.
IPR012349. Split_barrel_FMN-bd.
[Graphical view]
PfamiPF10590. PNPOx_C. 1 hit.
PF01243. Pyridox_oxidase. 1 hit.
[Graphical view]
PIRSFiPIRSF000190. Pyd_amn-ph_oxd. 1 hit.
SUPFAMiSSF50475. SSF50475. 1 hit.
PROSITEiPS01064. PYRIDOX_OXIDASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "A seven-gene locus for synthesis of phenazine-1-carboxylic acid by Pseudomonas fluorescens 2-79."
    Mavrodi D.V., Ksenzenko V.N., Bonsall R.F., Cook R.J., Boronin A.M., Thomashow L.S.
    J. Bacteriol. 180:2541-2548(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: NRRL B-15132 / 2-79.
  2. Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH FMN, COFACTOR, SUBUNIT.

Entry informationi

Entry nameiPHZG_PSEFL
AccessioniPrimary (citable) accession number: Q51793
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: November 11, 2015
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.