TRPGD_SALTY
ID TRPGD_SALTY Reviewed; 531 AA.
AC P00905;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Bifunctional protein TrpGD;
DE Includes:
DE RecName: Full=Anthranilate synthase component 2;
DE Short=AS;
DE Short=ASII;
DE EC=4.1.3.27;
DE AltName: Full=Anthranilate synthase, glutamine amidotransferase component;
DE Includes:
DE RecName: Full=Anthranilate phosphoribosyltransferase;
DE EC=2.4.2.18;
GN Name=trpGD; Synonyms=trpD; OrderedLocusNames=STM1724;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6355484; DOI=10.1016/s0022-2836(83)80136-3;
RA Horowitz H., van Arsdell J., Platt T.;
RT "Nucleotide sequence of the trpD and trpC genes of Salmonella
RT typhimurium.";
RL J. Mol. Biol. 169:775-797(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-201.
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).
RN [4]
RP FUNCTION, ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=4914739; DOI=10.1016/s0021-9258(18)63027-3;
RA Nagano H., Zalkin H.;
RT "Some physicochemical properties of anthranilate synthetase component I
RT from Salmonella typhimurium.";
RL J. Biol. Chem. 245:3097-3103(1970).
RN [5]
RP ACTIVITY REGULATION.
RX PubMed=2022650; DOI=10.1016/s0021-9258(18)92979-0;
RA Caligiuri M.G., Bauerle R.;
RT "Identification of amino acid residues involved in feedback regulation of
RT the anthranilate synthase complex from Salmonella typhimurium. Evidence for
RT an amino-terminal regulatory site.";
RL J. Biol. Chem. 266:8328-8335(1991).
RN [6]
RP CRYSTALLIZATION, AND SUBUNIT.
RX PubMed=10089433; DOI=10.1107/s0907444998010233;
RA Tolbert W.D., Chatterji S., Bauerle R., Kretsinger R.;
RT "Crystallization and preliminary crystallographic studies of the
RT anthranilate synthase partial complex from Salmonella typhimurium.";
RL Acta Crystallogr. D 55:305-306(1999).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), AND SUBUNIT.
RX PubMed=11224570; DOI=10.1038/84988;
RA Morollo A.A., Eck M.J.;
RT "Structure of the cooperative allosteric anthranilate synthase from
RT Salmonella typhimurium.";
RL Nat. Struct. Biol. 8:243-247(2001).
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. In addition to
CC synthesizing anthranilate, it also catalyzes the second step of the
CC pathway, the transfer of the phosphoribosyl group of 5-
CC phosphorylribose-1-pyrophosphate (PRPP) to anthranilate.
CC {ECO:0000269|PubMed:4914739}.
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 -!- ACTIVITY REGULATION: Cooperatively feedback inhibited by tryptophan.
CC {ECO:0000269|PubMed:2022650, ECO:0000269|PubMed:4914739}.
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: Monomer. Heterotetramer consisting of two non-identical
CC subunits: a beta subunit (TrpG) and a large alpha subunit (TrpE)
CC (Probable). {ECO:0000305|PubMed:10089433, ECO:0000305|PubMed:11224570,
CC ECO:0000305|PubMed:4914739}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the anthranilate
CC phosphoribosyltransferase family. {ECO:0000305}.
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DR EMBL; M30285; AAA27236.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20642.1; -; Genomic_DNA.
DR EMBL; J01811; AAA57312.1; -; Genomic_DNA.
DR PIR; A92907; NNEB2T.
DR RefSeq; NP_460683.1; NC_003197.2.
DR RefSeq; WP_000763494.1; NC_003197.2.
DR PDB; 1I1Q; X-ray; 1.90 A; B=2-193.
DR PDBsum; 1I1Q; -.
DR AlphaFoldDB; P00905; -.
DR SMR; P00905; -.
DR IntAct; P00905; 1.
DR MINT; P00905; -.
DR STRING; 99287.STM1724; -.
DR MEROPS; C26.960; -.
DR PaxDb; P00905; -.
DR EnsemblBacteria; AAL20642; AAL20642; STM1724.
DR GeneID; 1253243; -.
DR KEGG; stm:STM1724; -.
DR PATRIC; fig|99287.12.peg.1820; -.
DR HOGENOM; CLU_014340_4_0_6; -.
DR PhylomeDB; P00905; -.
DR BioCyc; SENT99287:STM1724-MON; -.
DR SABIO-RK; P00905; -.
DR UniPathway; UPA00035; UER00040.
DR UniPathway; UPA00035; UER00041.
DR EvolutionaryTrace; P00905; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0004048; F:anthranilate phosphoribosyltransferase activity; IBA:GO_Central.
DR GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0002047; P:phenazine biosynthetic process; IBA:GO_Central.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central.
DR CDD; cd01743; GATase1_Anthranilate_Synthase; 1.
DR Gene3D; 3.40.1030.10; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR HAMAP; MF_00211; TrpD; 1.
DR InterPro; IPR005940; Anthranilate_Pribosyl_Tfrase.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR000312; Glycosyl_Trfase_fam3.
DR InterPro; IPR017459; Glycosyl_Trfase_fam3_N_dom.
DR InterPro; IPR036320; Glycosyl_Trfase_fam3_N_dom_sf.
DR InterPro; IPR035902; Nuc_phospho_transferase.
DR InterPro; IPR006221; TrpG/PapA_dom.
DR Pfam; PF00117; GATase; 1.
DR Pfam; PF02885; Glycos_trans_3N; 1.
DR Pfam; PF00591; Glycos_transf_3; 1.
DR SUPFAM; SSF47648; SSF47648; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR SUPFAM; SSF52418; SSF52418; 1.
DR TIGRFAMs; TIGR01245; trpD; 1.
DR TIGRFAMs; TIGR00566; trpG_papA; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allosteric enzyme; Amino-acid biosynthesis;
KW Aromatic amino acid biosynthesis; Glutamine amidotransferase;
KW Glycosyltransferase; Lyase; Multifunctional enzyme; Reference proteome;
KW Transferase; Tryptophan biosynthesis.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..531
FT /note="Bifunctional protein TrpGD"
FT /id="PRO_0000056897"
FT DOMAIN 3..196
FT /note="Glutamine amidotransferase type-1"
FT REGION 202..531
FT /note="Anthranilate phosphoribosyltransferase"
FT ACT_SITE 84
FT /note="Nucleophile; for GATase activity"
FT /evidence="ECO:0000250|UniProtKB:P00900"
FT ACT_SITE 170
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 172
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
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 CONFLICT 191..192
FT /note="QQ -> LA (in Ref. 3; AAA57312)"
FT /evidence="ECO:0000305"
FT CONFLICT 511
FT /note="V -> L (in Ref. 1; AAA27236)"
FT /evidence="ECO:0000305"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:1I1Q"
FT HELIX 14..23
FT /evidence="ECO:0007829|PDB:1I1Q"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:1I1Q"
FT HELIX 38..44
FT /evidence="ECO:0007829|PDB:1I1Q"
FT STRAND 48..54
FT /evidence="ECO:0007829|PDB:1I1Q"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:1I1Q"
FT HELIX 67..74
FT /evidence="ECO:0007829|PDB:1I1Q"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:1I1Q"
FT HELIX 85..93
FT /evidence="ECO:0007829|PDB:1I1Q"
FT STRAND 106..114
FT /evidence="ECO:0007829|PDB:1I1Q"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:1I1Q"
FT STRAND 125..131
FT /evidence="ECO:0007829|PDB:1I1Q"
FT STRAND 145..150
FT /evidence="ECO:0007829|PDB:1I1Q"
FT STRAND 153..159
FT /evidence="ECO:0007829|PDB:1I1Q"
FT TURN 160..163
FT /evidence="ECO:0007829|PDB:1I1Q"
FT STRAND 164..170
FT /evidence="ECO:0007829|PDB:1I1Q"
FT HELIX 179..190
FT /evidence="ECO:0007829|PDB:1I1Q"
SQ SEQUENCE 531 AA; 56918 MW; 256D2409062CD4C7 CRC64;
MADILLLDNI DSFTWNLADQ LRTNGHNVVI YRNHIPAQTL IDRLATMKNP VLMLSPGPGV
PSEAGCMPEL LTRLRGKLPI IGICLGHQAI VEAYGGYVGQ AGEILHGKAS SIEHDGQAMF
AGLANPLPVA RYHSLVGSNV PAGLTINAHF NGMVMAVRHD ADRVCGFQFH PESILTTQGA
RLLEQTLAWA QQKLEPTNTL QPILEKLYQA QTLTQQESHQ LFSAVVRGEL KPEQLAAALV
SMKIRGEHPN EIAGAATALL ENAAPFPRPE YLFADIVGTG GDGSNSINIS TASAFVAAAC
GLKVAKHGNR SVSSKSGSSD LLAAFGINLD MNADKSRQAL DELGVCFLFA PKYHTGLRHA
MPVRQQLKTR TLFNVLGPLI NPAHPPLALI GVYSPELVLP IAETLRVLGY QRAAVVHSGG
MDEVSLHAPT IVAELHDGEI KSYQLTAEDF GLTPYHQDQL AGGTPEENRD ILTRLLQGKG
DAAHEAAVAA NVAMLMRLHG QEDLKANAQT VLDVLRNGTA YDRVTALAAR G
