PHNA_PSEAE
ID PHNA_PSEAE Reviewed; 530 AA.
AC P09785;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Anthranilate synthase component 1, pyocyanine specific;
DE Short=AS;
DE Short=ASI;
DE EC=4.1.3.27;
DE AltName: Full=Anthranilate synthase alpha subunit, pyocyanine specific {ECO:0000303|PubMed:2153661};
GN Name=phnA {ECO:0000303|PubMed:2153661};
GN Synonyms=trpE {ECO:0000303|PubMed:3127654}; OrderedLocusNames=PA1001;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROBABLE FUNCTION AS AN ANTHRANILATE
RP SYNTHASE, PATHWAY, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1, and PAC174;
RX PubMed=2153661; DOI=10.1128/jb.172.2.884-900.1990;
RA Essar D.W., Eberly L., Hadero A., Crawford I.P.;
RT "Identification and characterization of genes for a second anthranilate
RT synthase in Pseudomonas aeruginosa: interchangeability of the two
RT anthranilate synthases and evolutionary implications.";
RL J. Bacteriol. 172:884-900(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 383-530.
RC STRAIN=PAC174;
RX PubMed=3127654; DOI=10.1093/oxfordjournals.molbev.a040408;
RA Crawford I.P., Eberly L.;
RT "Structure and regulation of the anthranilate synthase genes in Pseudomonas
RT aeruginosa: I. Sequence of trpG encoding the glutamine amidotransferase
RT subunit.";
RL Mol. Biol. Evol. 3:436-448(1986).
RN [4]
RP DISCUSSION OF FUNCTION.
RX PubMed=11591691; DOI=10.1128/jb.183.21.6454-6465.2001;
RA Mavrodi D.V., Bonsall R.F., Delaney S.M., Soule M.J., Phillips G.,
RA Thomashow L.S.;
RT "Functional analysis of genes for biosynthesis of pyocyanin and phenazine-
RT 1-carboxamide from Pseudomonas aeruginosa PAO1.";
RL J. Bacteriol. 183:6454-6465(2001).
RN [5]
RP FUNCTION IN PQS BIOSYNTHESIS, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=UCBPP-PA14;
RX PubMed=23449919; DOI=10.1099/mic.0.063065-0;
RA Palmer G.C., Jorth P.A., Whiteley M.;
RT "The role of two Pseudomonas aeruginosa anthranilate synthases in
RT tryptophan and quorum signal production.";
RL Microbiology 159:959-969(2013).
CC -!- FUNCTION: Part of a heterotetrameric complex that catalyzes the two-
CC step biosynthesis of anthranilate, a precursor for Pseudomonas
CC quinolone signal (2-heptyl-3-hydroxy-4-quinolone; PQS) production which
CC is required to induce the genes for the biosynthesis of the virulence
CC factor pyocyanine (PCN), a characteristic blue-green phenazine pigment
CC produced by P.aeruginosa (PubMed:11591691, PubMed:2153661,
CC PubMed:23449919). In the first step, the glutamine-binding beta subunit
CC (PhnB) of anthranilate synthase (AS) provides the glutamine
CC amidotransferase activity which generates ammonia as a substrate that,
CC along with chorismate, is used in the second step, catalyzed by the
CC large alpha subunit of AS (PhnA) to produce anthranilate (By
CC similarity). {ECO:0000250|UniProtKB:P00897,
CC ECO:0000269|PubMed:11591691, ECO:0000269|PubMed:2153661,
CC ECO:0000269|PubMed:23449919}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chorismate + L-glutamine = anthranilate + H(+) + L-glutamate +
CC pyruvate; Xref=Rhea:RHEA:21732, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16567, ChEBI:CHEBI:29748, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:58359; EC=4.1.3.27;
CC Evidence={ECO:0000305|PubMed:2153661};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P00897};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P00897};
CC -!- PATHWAY: Secondary metabolite biosynthesis; pyocyanine biosynthesis.
CC {ECO:0000305|PubMed:2153661}.
CC -!- SUBUNIT: Heterotetramer consisting of two non-identical subunits: a
CC beta subunit (PhnB) and a large alpha subunit (PhnA).
CC {ECO:0000250|UniProtKB:P00897}.
CC -!- INDUCTION: Expression increases as cell grow from early to late log
CC phase and further increases in stationary phase; there is about 10-fold
CC more mRNA in stationary than early log phase.
CC {ECO:0000269|PubMed:2153661, ECO:0000269|PubMed:23449919}.
CC -!- DISRUPTION PHENOTYPE: Disruption of phnA alone yields 22-34%
CC pyocyanine. Double trpE-phnA disruption requires anthranilate or L-
CC tryptophan for growth on minimal medium and does not make pyocyanine
CC (PubMed:2153661). Double phnA-phnB deletions are tryptophan
CC prototrophs; they make less PQS (PubMed:23449919).
CC {ECO:0000269|PubMed:2153661, ECO:0000269|PubMed:23449919}.
CC -!- MISCELLANEOUS: PhnAB is not feedback inhibited by tryptophan.
CC {ECO:0000305|PubMed:2153661}.
CC -!- MISCELLANEOUS: The sequence shown is that of strain PAO.
CC -!- SIMILARITY: Belongs to the anthranilate synthase component I family.
CC {ECO:0000305}.
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DR EMBL; M33810; AAA88448.1; -; Genomic_DNA.
DR EMBL; M33811; AAA88451.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG04390.1; -; Genomic_DNA.
DR EMBL; M15733; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; B83519; B83519.
DR PIR; E35116; E35116.
DR RefSeq; NP_249692.1; NC_002516.2.
DR RefSeq; WP_010895533.1; NZ_QZGE01000006.1.
DR AlphaFoldDB; P09785; -.
DR SMR; P09785; -.
DR STRING; 287.DR97_946; -.
DR PaxDb; P09785; -.
DR PRIDE; P09785; -.
DR DNASU; 878421; -.
DR EnsemblBacteria; AAG04390; AAG04390; PA1001.
DR GeneID; 878421; -.
DR KEGG; pae:PA1001; -.
DR PATRIC; fig|208964.12.peg.1033; -.
DR PseudoCAP; PA1001; -.
DR HOGENOM; CLU_006493_9_4_6; -.
DR InParanoid; P09785; -.
DR OMA; AYRSFMN; -.
DR PhylomeDB; P09785; -.
DR BioCyc; MetaCyc:MON-16007; -.
DR BioCyc; PAER208964:G1FZ6-1020-MON; -.
DR BRENDA; 4.1.3.27; 5087.
DR UniPathway; UPA00235; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0004049; F:anthranilate synthase activity; IMP:PseudoCAP.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0002047; P:phenazine biosynthetic process; IMP:PseudoCAP.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.60.120.10; -; 1.
DR InterPro; IPR005801; ADC_synthase.
DR InterPro; IPR019999; Anth_synth_I-like.
DR InterPro; IPR006805; Anth_synth_I_N.
DR InterPro; IPR005257; Anth_synth_I_TrpE.
DR InterPro; IPR015890; Chorismate_C.
DR PANTHER; PTHR11236; PTHR11236; 1.
DR PANTHER; PTHR11236:SF22; PTHR11236:SF22; 1.
DR Pfam; PF04715; Anth_synt_I_N; 1.
DR Pfam; PF00425; Chorismate_bind; 1.
DR PIRSF; PIRSF001373; TrpE; 1.
DR PRINTS; PR00095; ANTSNTHASEI.
DR SUPFAM; SSF56322; SSF56322; 1.
DR TIGRFAMs; TIGR00565; trpE_proteo; 1.
PE 1: Evidence at protein level;
KW Lyase; Magnesium; Metal-binding; Reference proteome; Virulence.
FT CHAIN 1..530
FT /note="Anthranilate synthase component 1, pyocyanine
FT specific"
FT /id="PRO_0000058388"
FT BINDING 331..332
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 364
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 452
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 472
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 486..488
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 488
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 501
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT VARIANT 4
FT /note="R -> G (in strain: PAC174)"
FT VARIANT 91
FT /note="D -> A (in strain: PAC174)"
FT VARIANT 111
FT /note="Q -> P (in strain: PAC174)"
FT VARIANT 114
FT /note="S -> P (in strain: PAC174)"
FT VARIANT 145
FT /note="V -> A (in strain: PAC174)"
FT VARIANT 337
FT /note="R -> C (in strain: PAC174)"
SQ SEQUENCE 530 AA; 58670 MW; 0E6280AC3A23A066 CRC64;
MGARRWLVSG VGYRLEESLE YRTLVPEALS IWRMAGANRM LFDCFDVDSK AARRSVAILS
SCLRIECWGR DVVLRALNSN GRALLAPLSE DCPAQVTCLR DGDTLHWRFP QEESHADEWR
RLHGLSSLEA LRRVLGTLGD AEGPVLLGGL FSFDLAEQFE PLPAPAEPAR HCPDYLFLVP
ELLLDIDHLA RRTSLQAFVH DPAGHDRLAA SLRQCADEFH GAVEEASESP VAGVRAGNYQ
VDLDDASFAR QVERLQAHVR AGDVFQIVPS RSFSMPCADP WRAYRQLCLR NPSPYRFFLD
AGDFCLFGAS PESALKYDAE SREVELYPIA GTRPRGRDAR GAIDAELDNR LEAELRLDAK
EIAEHMMLVD LARNDLARVC RSGTRQVRDM LKVDRYSHVM HLVSRVAGEL HGELDALHAY
RACLNMGTLV GAPKVRAMQL LRQYEDGYRG SYGGAIGILD SAGNLDTSIV IRSAEVREGI
ARVRAGAGVV LDSDPRLEAE ETRNKALAVL TAVAAAERER GERDAHHAVG
