TRPG_NEOYE
ID TRPG_NEOYE Reviewed; 189 AA.
AC Q1XDC5;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 56.
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 Neopyropia yezoensis (Susabi-nori) (Pyropia yezoensis).
OG Plastid; Chloroplast.
OC Eukaryota; Rhodophyta; Bangiophyceae; Bangiales; Bangiaceae; Neopyropia.
OX NCBI_TaxID=2788;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U-51;
RA Kunimoto M., Morishima K., Yoshikawa M., Fukuda S., Kobayashi T.,
RA Kobayashi M., Okazaki T., Ohara I., Nakayama I.;
RT "Whole genome sequence of Porphyra yezoensis chloroplast.";
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
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; AP006715; BAE92486.1; -; Genomic_DNA.
DR RefSeq; YP_537043.1; NC_007932.1.
DR AlphaFoldDB; Q1XDC5; -.
DR SMR; Q1XDC5; -.
DR GeneID; 3978746; -.
DR UniPathway; UPA00035; UER00040.
DR GO; GO:0009507; C:chloroplast; 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 4: Predicted;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Chloroplast;
KW Glutamine amidotransferase; Lyase; Plastid; Tryptophan biosynthesis.
FT CHAIN 1..189
FT /note="Anthranilate synthase component 2"
FT /id="PRO_0000277284"
FT DOMAIN 1..189
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 189 AA; 21305 MW; E78D807C7F9B2B84 CRC64;
MILIIDNYDS FTYNLAQCVG ELGYDVLVCR NDEIDIPTIK QLNPNKIIIS PGPGKPSDSG
ISLDVISSFS DSIPILGVCL GHQSIGYLNG GRIIKVSEIM HGKTSKIYHN NEDLFKTLPN
PFIATRYHSL IIDNLNFPSS LAITAWTENN IIMACRHKDN QMLRGIQFHP ESLWTFYGQQ
LLRNFLEYS