TRPG_PSEPU
ID TRPG_PSEPU Reviewed; 198 AA.
AC P00901;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 2.
DT 03-AUG-2022, entry version 101.
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;
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 23287 / C1S;
RX PubMed=2404959; DOI=10.1128/jb.172.2.867-883.1990;
RA Essar D.W., Eberly L., Crawford I.P.;
RT "Evolutionary differences in chromosomal locations of four early genes of
RT the tryptophan pathway in fluorescent pseudomonads: DNA sequences and
RT characterization of Pseudomonas putida trpE and trpGDC.";
RL J. Bacteriol. 172:867-883(1990).
RN [2]
RP PROTEIN SEQUENCE, AND ACTIVE SITE.
RX PubMed=659439; DOI=10.1016/s0021-9258(17)30440-4;
RA Kawamura M., Keim P.S., Goto Y., Zalkin H., Heinrikson R.L.;
RT "Anthranilate synthetase component II from Pseudomonas putida. Covalent
RT structure and identification of the cysteine residue involved in
RT catalysis.";
RL J. Biol. Chem. 253:4659-4668(1978).
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. In the first step, the glutamine-binding beta subunit
CC (TrpG) 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 (TrpE) to produce anthranilate. In the
CC absence of TrpG, TrpE can synthesize anthranilate directly from
CC chorismate and high concentrations of ammonia.
CC {ECO:0000269|PubMed:2404959}.
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.
CC -!- SUBUNIT: Heterotetramer consisting of two non-identical subunits: a
CC beta subunit (TrpG) and a large alpha subunit (TrpE). {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene fail to grow on low-
CC ammonia medium but grew on the high-ammonium medium.
CC {ECO:0000269|PubMed:2404959}.
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DR EMBL; M33799; AAA80553.1; -; Genomic_DNA.
DR PIR; A01122; NNPS2P.
DR AlphaFoldDB; P00901; -.
DR SMR; P00901; -.
DR STRING; 1240350.AMZE01000023_gene1386; -.
DR MEROPS; C26.955; -.
DR eggNOG; COG0512; Bacteria.
DR UniPathway; UPA00035; UER00040.
DR GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniPathway.
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 Direct protein sequencing; Glutamine amidotransferase; Lyase;
KW Tryptophan biosynthesis.
FT CHAIN 1..198
FT /note="Anthranilate synthase component 2"
FT /id="PRO_0000056896"
FT DOMAIN 2..198
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 80
FT /note="Nucleophile; for GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 174
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 176
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT BINDING 53..55
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00900"
FT BINDING 84
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00900"
FT BINDING 130..131
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00900"
FT CONFLICT 5
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 198 AA; 21824 MW; 6AA7BDC12ED02FB3 CRC64;
MLLMMIDNYD SFTYNVVQYL GELGAEVKVI RNDEMTIAQI EALNPERIVV SPGPCTPSEA
GVSIEAILHF AGKLPILGVC LGHQSIGQAF GGDVVRARQV MHGKTSPVHH RDLGVFTGLN
NPLTVTRYHS LVVKRETLPD CLEVTAWTAH EDGSVDEIMG LRHKTLNIEG VQFHPESILT
EQGHELFANF LKQTGGRR
