TRPE_PSEAE
ID TRPE_PSEAE Reviewed; 492 AA.
AC P20580;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Anthranilate synthase component 1;
DE Short=AS;
DE Short=ASI;
DE EC=4.1.3.27;
GN Name=trpE {ECO:0000303|PubMed:2105306}; OrderedLocusNames=PA0609;
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], FUNCTION, PATHWAY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=2105306; DOI=10.1128/jb.172.2.853-866.1990;
RA Essar D.W., Eberly L., Han C.Y., Crawford I.P.;
RT "DNA sequences and characterization of four early genes of the tryptophan
RT pathway in Pseudomonas aeruginosa.";
RL J. Bacteriol. 172:853-866(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RA Nakayama K., Takashima K., Ishihara H., Shinomiya T., Kageyama M.,
RA Kanaya S., Ohnishi M., Murata T., Terawaki Y., Mori H., Hayashi T.;
RT "Genetic relationship between bacteriocins and bacteriophages.";
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 207-492.
RX PubMed=8444788; DOI=10.1128/jb.175.5.1257-1263.1993;
RA Matsui H., Sano Y., Ishihara H., Shinomiya T.;
RT "Regulation of pyocin genes in Pseudomonas aeruginosa by positive (prtN)
RT and negative (prtR) regulatory genes.";
RL J. Bacteriol. 175:1257-1263(1993).
RN [5]
RP 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 [6]
RP FUNCTION IN TRYPTOPHAN BIOSYNTHESIS, PATHWAY, INDUCTION, AND DISRUPTION
RP 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, an intermediate in the biosynthesis
CC of L-tryptophan (PubMed:2105306, PubMed:23449919). In the first step,
CC the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS)
CC provides the glutamine amidotransferase activity which generates
CC ammonia as a substrate that, along with chorismate, is used in the
CC second step, catalyzed by the large alpha subunit of AS (TrpE) to
CC produce anthranilate. In the absence of TrpG, TrpE can synthesize
CC anthranilate directly from chorismate and high concentrations of
CC ammonia (By similarity). {ECO:0000250|UniProtKB:P00897,
CC ECO:0000269|PubMed:2105306, 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 -!- 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 -!- ACTIVITY REGULATION: Feedback inhibited by tryptophan. {ECO:0000250}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 1/5. {ECO:0000269|PubMed:23449919,
CC ECO:0000305|PubMed:2105306}.
CC -!- SUBUNIT: Heterotetramer consisting of two non-identical subunits: a
CC beta subunit (TrpG) and a large alpha subunit (TrpE).
CC {ECO:0000250|UniProtKB:P00897}.
CC -!- INDUCTION: Expression decreases as cell grow from early to late
CC logphase and further decreases in stationary phase.
CC {ECO:0000269|PubMed:23449919}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene do not grow without
CC tryptophan (auxotrophs) (PubMed:2105306, PubMed:23449919). About 10%
CC decrease in pyocyanine production; double trpE-phnA disruption requires
CC anthranilate or L-tryptophan for growth on minimal medium and does not
CC make pyocyanine (PubMed:2153661). {ECO:0000269|PubMed:2105306,
CC ECO:0000269|PubMed:2153661, ECO:0000269|PubMed:23449919}.
CC -!- SIMILARITY: Belongs to the anthranilate synthase component I family.
CC {ECO:0000305}.
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DR EMBL; M33814; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB030825; BAA83144.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG03998.1; -; Genomic_DNA.
DR EMBL; D12706; BAA02200.1; -; Genomic_DNA.
DR PIR; D35114; D35114.
DR RefSeq; NP_249300.1; NC_002516.2.
DR RefSeq; WP_003113204.1; NZ_QZGE01000010.1.
DR AlphaFoldDB; P20580; -.
DR SMR; P20580; -.
DR STRING; 287.DR97_3578; -.
DR PaxDb; P20580; -.
DR PRIDE; P20580; -.
DR DNASU; 879191; -.
DR EnsemblBacteria; AAG03998; AAG03998; PA0609.
DR GeneID; 879191; -.
DR KEGG; pae:PA0609; -.
DR PATRIC; fig|208964.12.peg.645; -.
DR PseudoCAP; PA0609; -.
DR HOGENOM; CLU_006493_9_3_6; -.
DR InParanoid; P20580; -.
DR OMA; GCVGYLD; -.
DR PhylomeDB; P20580; -.
DR BioCyc; MetaCyc:MON-16005; -.
DR BioCyc; PAER208964:G1FZ6-616-MON; -.
DR BRENDA; 4.1.3.27; 5087.
DR UniPathway; UPA00035; UER00040.
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:0000162; P:tryptophan biosynthetic process; IMP:PseudoCAP.
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; IPR005256; Anth_synth_I_PabB.
DR InterPro; IPR015890; Chorismate_C.
DR PANTHER; PTHR11236; PTHR11236; 1.
DR Pfam; PF04715; Anth_synt_I_N; 1.
DR Pfam; PF00425; Chorismate_bind; 1.
DR PRINTS; PR00095; ANTSNTHASEI.
DR SUPFAM; SSF56322; SSF56322; 1.
DR TIGRFAMs; TIGR00564; trpE_most; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW Magnesium; Metal-binding; Reference proteome; Tryptophan biosynthesis.
FT CHAIN 1..492
FT /note="Anthranilate synthase component 1"
FT /id="PRO_0000154106"
FT BINDING 48
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 273..275
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 308..309
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 335
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 423
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 443
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 457..459
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 459
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 472
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00897"
SQ SEQUENCE 492 AA; 54555 MW; 60FEAABF37C2CD13 CRC64;
MNREEFLRLA ADGYNRIPLS FETLADFDTP LSIYLKLADA PNSYLLESVQ GGEKWGRYSI
IGLPCRTVLR VYDHQVRISI DGVETERFDC ADPLAFVEEF KARYQVPTVP GLPRFDGGLV
GYFGYDCVRY VEKRLATCPN PDPLGNPDIL LMVSDAVVVF DNLAGKIHAI VLADPSEENA
YERGQARLEE LLERLRQPIT PRRGLDLEAA QGREPAFRAS FTREDYENAV GRIKDYILAG
DCMQVVPSQR MSIEFKAAPI DLYRALRCFN PTPYMYFFNF GDFHVVGSSP EVLVRVEDGL
VTVRPIAGTR PRGINEEADL ALEQDLLSDA KEIAEHLMLI DLGRNDVGRV SDIGAVKVTE
KMVIERYSNV MHIVSNVTGQ LREGLSAMDA LRAILPAGTL SGAPKIRAME IIDELEPVKR
GVYGGAVGYL AWNGNMDTAI AIRTAVIKNG ELHVQAGGGI VADSVPALEW EETINKRRAM
FRAVALAEQS VE
