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   02-SEP-2026, entry version 151.
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; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Pseudomonadales; 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 /
RC   1C / 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 /
RC   1C / 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 + pyruvate + L-
CC         glutamate + H(+); Xref=Rhea:RHEA:21732, ChEBI:CHEBI:15361,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16567, ChEBI:CHEBI:29748,
CC         ChEBI:CHEBI:29985, 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; NC_002516.2.
DR   AlphaFoldDB; P09785; -.
DR   SMR; P09785; -.
DR   FunCoup; P09785; 480.
DR   STRING; 208964.PA1001; -.
DR   PaxDb; 208964-PA1001; -.
DR   DNASU; 878421; -.
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   OrthoDB; 9803598at2; -.
DR   PhylomeDB; P09785; -.
DR   BioCyc; MetaCyc:MONOMER-16007; -.
DR   BioCyc; PAER208964:G1FZ6-1020-MONOMER; -.
DR   BRENDA; 4.1.3.27; 5087.
DR   UniPathway; UPA00235; -.
DR   Proteomes; UP000002438; Chromosome.
DR   AbasyAtlas; P09785; -.
DR   GO; GO:0004049; F:anthranilate synthase activity; IMP:PseudoCAP.
DR   GO; GO:0002047; P:phenazine biosynthetic process; IMP:PseudoCAP.
DR   Gene3D; 3.60.120.10; Anthranilate synthase; 1.
DR   InterPro; IPR005801; ADC_synthase.
DR   InterPro; IPR015890; Anth_synth-like_dom.
DR   InterPro; IPR019999; Anth_synth_I-like.
DR   InterPro; IPR005257; Anth_synth_I_TrpE.
DR   NCBIfam; NF010079; PRK13564.1; 1.
DR   NCBIfam; TIGR00565; trpE_proteo; 1.
DR   PANTHER; PTHR11236; AMINOBENZOATE/ANTHRANILATE SYNTHASE; 1.
DR   PANTHER; PTHR11236:SF49; ANTHRANILATE SYNTHASE COMPONENT 1; 1.
DR   Pfam; PF00425; Chorismate_bind; 1.
DR   PIRSF; PIRSF001373; TrpE; 1.
DR   PRINTS; PR00095; ANTSNTHASEI.
DR   SUPFAM; SSF56322; ADC synthase; 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
//