ID   TRPG_CYAPA              Reviewed;         190 AA.
AC   P48261;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Anthranilate synthase component 2;
DE            Short=AS;
DE            EC=4.1.3.27;
DE   AltName: Full=Anthranilate synthase, glutamine amidotransferase component;
GN   Name=trpG;
OS   Cyanophora paradoxa.
OG   Plastid; Cyanelle.
OC   Eukaryota; Glaucocystophyceae; Cyanophoraceae; Cyanophora.
OX   NCBI_TaxID=2762;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTEX LB 555 / Pringsheim;
RA   Stirewalt V.L., Michalowski C.B., Loeffelhardt W., Bohnert H.J.,
RA   Bryant D.A.;
RT   "Nucleotide sequence of the cyanelle DNA from Cyanophora paradoxa.";
RL   Plant Mol. Biol. Rep. 13:327-332(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTEX LB 555 / Pringsheim;
RA   Loeffelhardt W., Stirewalt V.L., Michalowski C.B., Annarella M.,
RA   Farley J.Y., Schluchter W.M., Chung S., Newmann-Spallart C., Steiner J.M.,
RA   Jakowitsch J., Bohnert H.J., Bryant D.A.;
RT   "The complete sequence of the cyanelle genome of Cyanophora paradoxa: the
RT   genetic complexity of a primitive plastid.";
RL   (In) Schenk H.E.A., Herrmann R., Jeon K.W., Mueller N.E., Schwemmler W.
RL   (eds.);
RL   Eukaryotism and symbiosis, pp.40-48, Springer-Verlag, Heidelberg (1997).
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: Tetramer of two components I and two components II.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, cyanelle.
CC   -!- MISCELLANEOUS: Component I catalyzes the formation of anthranilate
CC       using ammonia rather than glutamine, whereas component II provides
CC       glutamine amidotransferase activity.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U30821; AAA81296.1; -; Genomic_DNA.
DR   PIR; T06953; T06953.
DR   RefSeq; NP_043265.1; NC_001675.1.
DR   AlphaFoldDB; P48261; -.
DR   SMR; P48261; -.
DR   GeneID; 801682; -.
DR   UniPathway; UPA00035; UER00040.
DR   GO; GO:0009842; C:cyanelle; IEA:UniProtKB-SubCell.
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   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Cyanelle;
KW   Glutamine amidotransferase; Lyase; Plastid; Tryptophan biosynthesis.
FT   CHAIN           1..190
FT                   /note="Anthranilate synthase component 2"
FT                   /id="PRO_0000056892"
FT   DOMAIN          1..190
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:0000250|UniProtKB:P00900"
FT   ACT_SITE        169
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        171
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"
SQ   SEQUENCE   190 AA;  21202 MW;  3289F865BD830334 CRC64;
     MILLIDNYDS FTYNLAQYLS ELNIKVLVKR NDKITLDEIK NLNIQGIIIS PCPGGPEDSG
     ISQGIIKYLG NQIPILGVCL GHQTIGHVFG GKIIKAPKLI HGKPSIIFHD GKGVFQNLKN
     PITATRYHSL IIEKESCPDE LEITAWTEDG LIMGIQHKKY KQLQGIQFHP ESILTESGKQ
     ILQNFINCLN