TRPG_SHIDY
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 03-AUG-2022, entry version 104.
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; Proteobacteria; 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 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;
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