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P09786 (PHNB_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Anthranilate synthase component II, pyocyanin specific

EC=4.1.3.27
Alternative name(s):
Glutamine amidotransferase
Gene names
Name:phnB
Ordered Locus Names:PA1002
OrganismPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) [Reference proteome] [HAMAP]
Taxonomic identifier208964 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length200 AA.
Sequence statusComplete.
Protein existencePredicted

General annotation (Comments)

Function

Participates in the biosynthesis of pyocyanin, a characteristic blue-green phenazine pigment produced by P.aeruginosa.

Catalytic activity

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

Pathway

Secondary metabolite biosynthesis; pyocyanine biosynthesis.

Subunit structure

Tetramer of two components I and two components II.

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.

Ontologies

Keywords
   DomainGlutamine amidotransferase
   Molecular functionLyase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processglutamine metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionanthranilate synthase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 200200Anthranilate synthase component II, pyocyanin specific
PRO_0000056906

Regions

Domain2 – 195194Glutamine amidotransferase type-1

Sites

Active site831 By similarity
Active site1691 By similarity
Active site1711 By similarity

Experimental info

Sequence conflict148 – 1492DA → ES in AAA26018. Ref.2
Sequence conflict1951R → A in AAA88449. Ref.1
Sequence conflict1951R → A in AAA88452. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P09786 [UniParc].

Last modified December 8, 2000. Version 3.
Checksum: 9D9E218DDE8D7E30

FASTA20021,845
        10         20         30         40         50         60 
MRITLLDNFD SFTYNLVEQF CLLGAEVRVM RNDTPLPTIQ AALLADGCEL LVLSPGPGRP 

        70         80         90        100        110        120 
EDAGCMLELL AWARGRLPVL GVCLGHQALA LAAGGAVGEA RKPLHGKSTS LRFDQRHPLF 

       130        140        150        160        170        180 
DGIADLRVAR YHSLVVSRLP EGFDCLADAD GEIMAMADPR NRQLGLQFHP ESILTTHGQR 

       190        200 
LLENALLWCG ALAVRERLRA 

« Hide

References

« Hide 'large scale' references
[1]"Identification and characterization of genes for a second anthranilate synthase in Pseudomonas aeruginosa: interchangeability of the two anthranilate synthases and evolutionary implications."
Essar D.W., Eberly L., Hadero A., Crawford I.P.
J. Bacteriol. 172:884-900(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228 and PAC174.
[2]"Structure and regulation of the anthranilate synthase genes in Pseudomonas aeruginosa: I. Sequence of trpG encoding the glutamine amidotransferase subunit."
Crawford I.P., Eberly L.
Mol. Biol. Evol. 3:436-448(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen."
Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. expand/collapse author list , Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.
Nature 406:959-964(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M15733 Genomic DNA. Translation: AAA26018.1.
M33810 Genomic DNA. Translation: AAA88449.1.
M33811 Genomic DNA. Translation: AAA88452.1.
AE004091 Genomic DNA. Translation: AAG04391.1.
PIRB35116.
C83519.
RefSeqNP_249693.1. NC_002516.2.

3D structure databases

ProteinModelPortalP09786.
SMRP09786. Positions 3-188.
ModBaseSearch...

Protein-protein interaction databases

STRING208964.PA1002.

Protein family/group databases

MEROPSC26.955.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID880689.
KEGGpae:PA1002.
PATRIC19836294. VBIPseAer58763_1034.

Organism-specific databases

PseudoCAPPA1002.

Phylogenomic databases

eggNOGCOG0512.
HOGENOMHOG000025029.
KOK01658.
OMAYLIGLMN.
ProtClustDBCLSK866272.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-16008.
UniPathwayUPA00235.

Family and domain databases

InterProIPR017926. GATASE.
IPR006221. TrpG/PapA_dom.
[Graphical view]
PfamPF00117. GATase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00566. trpG_papA. 1 hit.
PROSITEPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePHNB_PSEAE
AccessionPrimary (citable) accession number: P09786
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: December 8, 2000
Last modified: May 29, 2013
This is version 94 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families