TRPG_PSEAE
ID TRPG_PSEAE Reviewed; 201 AA.
AC P20576;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 08-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Anthranilate synthase component 2;
DE Short=AS;
DE Short=ASII;
DE EC=4.1.3.27;
DE AltName: Full=Anthranilate synthase, GATase component;
DE AltName: Full=Anthranilate synthase, glutamine amidotransferase component;
GN Name=trpG {ECO:0000303|PubMed:2105306}; OrderedLocusNames=PA0649;
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 [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 INDUCTION.
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 [4]
RP FUNCTION IN TRYPTOPHAN BIOSYNTHESIS.
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:23449919, PubMed:2105306). 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:P00900,
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 -!- 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:P00900}.
CC -!- INDUCTION: Expression decreases as cell grow from early to late log
CC phase and further decreases in stationary phase; there is about 5-fold
CC less mRNA in stationary than early log phase.
CC {ECO:0000269|PubMed:2153661}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene fail to grow on low-
CC ammonia medium but grew on high-ammonium medium.
CC {ECO:0000269|PubMed:2105306}.
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DR EMBL; M33814; AAA25823.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG04038.1; -; Genomic_DNA.
DR PIR; A35114; A35114.
DR PIR; G83563; G83563.
DR RefSeq; NP_249340.1; NC_002516.2.
DR RefSeq; WP_003113175.1; NZ_QZGE01000010.1.
DR AlphaFoldDB; P20576; -.
DR SMR; P20576; -.
DR STRING; 287.DR97_3602; -.
DR MEROPS; C26.955; -.
DR PaxDb; P20576; -.
DR PRIDE; P20576; -.
DR DNASU; 878400; -.
DR EnsemblBacteria; AAG04038; AAG04038; PA0649.
DR GeneID; 878400; -.
DR KEGG; pae:PA0649; -.
DR PATRIC; fig|208964.12.peg.680; -.
DR PseudoCAP; PA0649; -.
DR HOGENOM; CLU_014340_1_2_6; -.
DR InParanoid; P20576; -.
DR OMA; TEHGHAM; -.
DR PhylomeDB; P20576; -.
DR BioCyc; MetaCyc:MON-16006; -.
DR BioCyc; PAER208964:G1FZ6-654-MON; -.
DR BRENDA; 4.1.3.27; 5087.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0046820; F:4-amino-4-deoxychorismate synthase activity; IBA:GO_Central.
DR GO; GO:0004049; F:anthranilate synthase activity; IMP:PseudoCAP.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IBA:GO_Central.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IMP:PseudoCAP.
DR CDD; cd01743; GATase1_Anthranilate_Synthase; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR006221; TrpG/PapA_dom.
DR Pfam; PF00117; GATase; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR TIGRFAMs; TIGR00566; trpG_papA; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Glutamine amidotransferase; Lyase; Reference proteome;
KW Tryptophan biosynthesis.
FT CHAIN 1..201
FT /note="Anthranilate synthase component 2"
FT /id="PRO_0000056895"
FT DOMAIN 1..199
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 79
FT /note="Nucleophile; for GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 173
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 175
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT BINDING 52..54
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00900"
FT BINDING 83
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00900"
FT BINDING 129..130
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00900"
FT CONFLICT 177
FT /note="I -> V (in Ref. 1; AAA25823)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 201 AA; 22046 MW; 730A4AA52F4348C1 CRC64;
MLLMIDNYDS FTYNLVQYFG ELKAEVKVVR NDELSVEQIE ALAPERIVLS PGPCTPNEAG
VSLAVIERFA GKLPLLGVCL GHQSIGQAFG GEVVRARQVM HGKTSPIHHK DLGVFAGLAN
PLTVTRYHSL VVKRESLPEC LEVTAWTQHA DGSLDEIMGV RHKTLNVEGV QFHPESILTE
QGHELLANFL RQQGGVRGEG N
