ID   TRPG_SHIDY              Reviewed;         201 AA.
AC   P00906;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   13-SEP-2023, entry version 108.
DE   RecName: Full=Anthranilate synthase component II;
DE            EC=4.1.3.27;
DE   Includes:
DE     RecName: Full=Glutamine amidotransferase;
DE   Includes:
DE     RecName: Full=Anthranilate phosphoribosyltransferase;
DE              EC=2.4.2.18;
DE   Flags: Fragment;
GN   Name=trpG-TRPD;
OS   Shigella dysenteriae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=622;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7007652; DOI=10.1016/0022-2836(80)90260-0;
RA   Nichols B.P., Miozzari G.F., van Cleemput M., Bennett G.N., Yanofsky C.;
RT   "Nucleotide sequences of the trpG regions of Escherichia coli, Shigella
RT   dysenteriae, Salmonella typhimurium and Serratia marcescens.";
RL   J. Mol. Biol. 142:503-517(1980).
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=diphosphate + N-(5-phospho-beta-D-ribosyl)anthranilate = 5-
CC         phospho-alpha-D-ribose 1-diphosphate + anthranilate;
CC         Xref=Rhea:RHEA:11768, ChEBI:CHEBI:16567, ChEBI:CHEBI:18277,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58017; EC=2.4.2.18;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 1/5.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 2/5.
CC   -!- SUBUNIT: Tetramer of two components I and two components II.
CC   -!- MISCELLANEOUS: Component I catalyzes the formation of anthranilate
CC       using ammonia rather than glutamine, whereas component II provides
CC       glutamine amidotransferase activity.
CC   -!- MISCELLANEOUS: In E.coli and certain other bacteria, component II is
CC       larger and its C-terminal two thirds has anthranilate
CC       phosphoribosyltransferase activity.
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DR   EMBL; J01787; AAA57307.1; -; Genomic_DNA.
DR   PIR; B92860; NNEB2D.
DR   AlphaFoldDB; P00906; -.
DR   SMR; P00906; -.
DR   MEROPS; C26.960; -.
DR   UniPathway; UPA00035; UER00040.
DR   UniPathway; UPA00035; UER00041.
DR   GO; GO:0004048; F:anthranilate phosphoribosyltransferase activity; IEA:UniProtKB-EC.
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   NCBIfam; TIGR00566; trpG_papA; 1.
DR   PANTHER; PTHR43418:SF2; BIFUNCTIONAL PROTEIN TRPGD; 1.
DR   PANTHER; PTHR43418; MULTIFUNCTIONAL TRYPTOPHAN BIOSYNTHESIS PROTEIN-RELATED; 1.
DR   Pfam; PF00117; GATase; 1.
DR   PRINTS; PR00097; ANTSNTHASEII.
DR   PRINTS; PR00099; CPSGATASE.
DR   PRINTS; PR00096; GATASE.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   4: Predicted;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Glutamine amidotransferase; Lyase; Multifunctional enzyme; Transferase;
KW   Tryptophan biosynthesis.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..>201
FT                   /note="Anthranilate synthase component II"
FT                   /id="PRO_0000056899"
FT   DOMAIN          3..196
FT                   /note="Glutamine amidotransferase type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        84
FT                   /note="Nucleophile; for GATase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        170
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        172
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   BINDING         57..59
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000250|UniProtKB:P00900"
FT   BINDING         88
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000250|UniProtKB:P00900"
FT   BINDING         134..135
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000250|UniProtKB:P00900"
FT   NON_TER         201
SQ   SEQUENCE   201 AA;  21700 MW;  943E3DBE4F0E59AF CRC64;
     MADILLLDNI DSFTYNLADQ LRSNGHNVVI YRNHIPAQTL IERLATMSNP VLMLSPGPGV
     PSEAGCMPEL LTRLSGKLPI IGICLGHQAI VEAYGGYVGQ AGEILHGKAS SIEHDGQAMF
     AGLTNPLPVA RYHSLVGSNI PAGLTINAHF NGMVMAVRHD ADRICGFQFH PESILTTQGA
     RLLEQTLAWA QRKLEPTNTL Q
//