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Reviewed, UniProtKB/Swiss-Prot Q51791 (PHZE_PSEFL)

Last modified January 19, 2010. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Anthranilate synthase, phenazine specific
    EC=4.1.3.27
Including the following 1 domains:
    1- Recommended name:
            Glutamine amidotransferase
Gene names
Name: phzE
OrganismPseudomonas fluorescens
Taxonomic identifier294 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length637 AA.
Sequence statusComplete.
Protein existencePredicted.

General annotation (Comments)

Function

Involved in the biosynthesis of the antibiotic, phenazine, a nitrogen-containing heterocyclic molecule having important roles in virulence, competition and biological control.

Catalytic activity

Chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate.

Pathway

Antibiotic biosynthesis; phenazine biosynthesis.

Miscellaneous

Component I catalyzes the formation of anthranilate using ammonia rather than glutamine, whereas component II provides glutamine amidotransferase activity.

Sequence similarities

Contains 1 glutamine amidotransferase type-1 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 637637Anthranilate synthase, phenazine specific
PRO_0000056908

Regions

Domain437 – 628192Glutamine amidotransferase type-1
Region1 – 434434Anthranilate synthase component I

Sites

Active site5171For GATase activity By similarity
Active site6021For GATase activity By similarity
Active site6041For GATase activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q51791-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: D65235CA6139E0FE

FASTA63769,873
        10         20         30         40         50         60 
MSQAAARLME RILQPVPEPF ALLYRPESSG PGLLNVLIGE MSQPQVLADI DLPAPSIGAP 

        70         80         90        100        110        120 
RLDVLTLIPY CQIAERGFAA VDDQSPLLAM NITEQQTISI EQMLALLPNV PIQLNNERFD 

       130        140        150        160        170        180 
LSDASYAEIV SQVIANEIGS GEGANFVIKR TFLAEISEYQ PASALSFFRH LLEREKGVYW 

       190        200        210        220        230        240 
TFIIHTGSRT FVGASPERHI SVKDGLAVMN PISGTYRYPP AGPSLTEVMD FLADRKEADE 

       250        260        270        280        290        300 
LYMVVDEELK MMARICEDGG HVLGPYLKEM THLAHTEYFI EGRTRRDVRE ILHETLFAPT 

       310        320        330        340        350        360 
VTGSPLESAC RVIERYEPQG RAYYSGMAAL IGSDGKGGRS LDSAILIRTA DIDNCGQVRI 

       370        380        390        400        410        420 
SVGSTIVRHS EPLTEAAESR AKAAGLIAAL KNQAASRFGD HLQVRAALAS RNAYVSDFWL 

       430        440        450        460        470        480 
MNSQQRQQTQ SDFSGRQVLI VDAEDTFTSM IAKQLRALGL VVTVRSFSDE YSFDGYDLVI 

       490        500        510        520        530        540 
MGPGPGNPSD VQLPKIDHLH VAIRSLLNQQ RPFLAVCLSH QVLSLCLGLE LQRKAIPNQG 

       550        560        570        580        590        600 
VQKQIDLFGN AERVGFYNTF AARSSSDRLD IDGIGTVEIS RDSETGEVHA LRGPAFASMQ 

       610        620        630 
FHAESLLTQE GPRIIADLLR HALIHTPVDS SVSAAGR 

« Hide

References

[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: 9573209] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: NRRL B-15132 / 2-79.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L48616 Genomic DNA. Translation: AAC18904.1.

3D structure databases

SMRQ51791. Positions 117-391, 351-491, 437-622.
ModBaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-13690.
BRENDA4.1.3.27. 329.

Family and domain databases

InterProIPR005801. ADC_synthase.
IPR006220. Anth_synthII.
IPR001317. CarbamoylP_synth_GATase_dom.
IPR015890. Chorismate-bd_C.
IPR011702. GATASE.
IPR017926. GATASE_1.
IPR000991. GATase_class1_C.
[Graphical view]
Gene3DG3DSA:3.60.120.10. TRPE_1_chor_bd. 1 hit.
PANTHERPTHR11236. TRPE_1_chor_bd. 1 hit.
PfamPF00425. Chorismate_bind. 1 hit.
PF00117. GATase. 1 hit.
[Graphical view]
PRINTSPR00097. ANTSNTHASEII.
PR00099. CPSGATASE.
PR00096. GATASE.
PROSITEPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePHZE_PSEFL
AccessionPrimary (citable) accession number: Q51791
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: January 19, 2010
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents