TRPGD_ECOLI
ID TRPGD_ECOLI Reviewed; 531 AA.
AC P00904; P76833; P76835; P78302;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 191.
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 {ECO:0000269|PubMed:4567790, ECO:0000269|PubMed:5333199};
DE AltName: Full=Anthranilate synthase, glutamine amidotransferase component;
DE Includes:
DE RecName: Full=Anthranilate phosphoribosyltransferase;
DE EC=2.4.2.18 {ECO:0000269|PubMed:2428387, ECO:0000269|PubMed:4567790};
GN Name=trpGD; Synonyms=trpD; OrderedLocusNames=b1263, JW1255;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7038627; DOI=10.1093/nar/9.24.6647;
RA Yanofsky C., Platt T., Crawford I.P., Nichols B.P., Christie G.E.,
RA Horowitz H., van Cleemput M., Wu A.M.;
RT "The complete nucleotide sequence of the tryptophan operon of Escherichia
RT coli.";
RL Nucleic Acids Res. 9:6647-6668(1981).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6283099; DOI=10.1016/0022-2836(82)90326-6;
RA Horowitz H., Christie G.E., Platt T.;
RT "Nucleotide sequence of the trpD gene, encoding anthranilate synthetase
RT component II of Escherichia coli.";
RL J. Mol. Biol. 156:245-256(1982).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP PROTEIN SEQUENCE OF 2-62.
RX PubMed=4594441; DOI=10.1038/248048a0;
RA Li S.-L., Hanlon J., Yanofsky C.;
RT "Structural homology of the glutamine amidotransferase subunits of the
RT anthranilate synthetases of Escherichia coli, Salmonella typhimurium and
RT Serratia marcescens.";
RL Nature 248:48-50(1974).
RN [7]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND CATALYTIC
RP ACTIVITY.
RX PubMed=5333199; DOI=10.1016/s0021-9258(18)96383-0;
RA Baker T.I., Crawford I.P.;
RT "Anthranilate synthetase. Partial purification and some kinetic studies on
RT the enzyme from Escherichia coli.";
RL J. Biol. Chem. 241:5577-5584(1966).
RN [8]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND CATALYTIC
RP ACTIVITY.
RX PubMed=4567790; DOI=10.1016/s0021-9258(19)44352-4;
RA Pabst M.J., Kuhn J.C., Somerville R.L.;
RT "Feedback regulation in the anthranilate aggregate from wild type and
RT mutant strains of Escherichia coli.";
RL J. Biol. Chem. 248:901-914(1973).
RN [9]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND CATALYTIC
RP ACTIVITY.
RX PubMed=2428387; DOI=10.1139/o86-094;
RA Gonzalez J.E., Somerville R.L.;
RT "The anthranilate aggregate of Escherichia coli: kinetics of inhibition by
RT tryptophan of phosphoribosyltransferase.";
RL Biochem. Cell Biol. 64:681-691(1986).
RN [10]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
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:2428387, ECO:0000269|PubMed:4567790,
CC ECO:0000269|PubMed:5333199}.
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; Evidence={ECO:0000269|PubMed:4567790,
CC ECO:0000269|PubMed:5333199};
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 Evidence={ECO:0000269|PubMed:2428387, ECO:0000269|PubMed:4567790};
CC -!- ACTIVITY REGULATION: Cooperatively feedback inhibited by tryptophan.
CC {ECO:0000269|PubMed:2428387, ECO:0000269|PubMed:4567790,
CC ECO:0000269|PubMed:5333199}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.2 uM for chorismate (at pH 7.5) {ECO:0000269|PubMed:2428387,
CC ECO:0000269|PubMed:4567790, ECO:0000269|PubMed:5333199};
CC KM=5 uM for chorismate (at 25 degrees Celsius and at pH 7.8)
CC {ECO:0000269|PubMed:2428387, ECO:0000269|PubMed:4567790,
CC ECO:0000269|PubMed:5333199};
CC KM=360 uM for glutamine (at pH 7.5) {ECO:0000269|PubMed:2428387,
CC ECO:0000269|PubMed:4567790, ECO:0000269|PubMed:5333199};
CC Vmax=0.53 nmol/min/mg enzyme (at 25 degrees Celsius and at pH 7.8)
CC {ECO:0000269|PubMed:2428387, ECO:0000269|PubMed:4567790,
CC ECO:0000269|PubMed:5333199};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 1/5. {ECO:0000305|PubMed:2428387,
CC ECO:0000305|PubMed:4567790, ECO:0000305|PubMed:5333199}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 2/5. {ECO:0000305|PubMed:2428387,
CC ECO:0000305|PubMed:4567790, ECO:0000305|PubMed:5333199}.
CC -!- SUBUNIT: Heterotetramer consisting of two non-identical subunits: a
CC beta subunit (TrpG) and a large alpha subunit (TrpE). {ECO:0000250}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the anthranilate
CC phosphoribosyltransferase family. {ECO:0000305}.
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DR EMBL; V00372; CAA23672.1; -; Genomic_DNA.
DR EMBL; V00367; CAA23665.1; -; Genomic_DNA.
DR EMBL; J01714; AAA57298.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74345.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA14798.1; -; Genomic_DNA.
DR PIR; B64874; NNEC2.
DR RefSeq; NP_415779.1; NC_000913.3.
DR RefSeq; WP_000763511.1; NZ_STEB01000005.1.
DR AlphaFoldDB; P00904; -.
DR SMR; P00904; -.
DR BioGRID; 4260123; 27.
DR ComplexPortal; CPX-4783; Anthranilate synthase complex.
DR STRING; 511145.b1263; -.
DR MEROPS; C26.960; -.
DR SWISS-2DPAGE; P00904; -.
DR jPOST; P00904; -.
DR PaxDb; P00904; -.
DR PRIDE; P00904; -.
DR EnsemblBacteria; AAC74345; AAC74345; b1263.
DR EnsemblBacteria; BAA14798; BAA14798; BAA14798.
DR GeneID; 66674914; -.
DR GeneID; 945109; -.
DR KEGG; ecj:JW1255; -.
DR KEGG; eco:b1263; -.
DR PATRIC; fig|1411691.4.peg.1020; -.
DR EchoBASE; EB1020; -.
DR eggNOG; COG0512; Bacteria.
DR eggNOG; COG0547; Bacteria.
DR HOGENOM; CLU_014340_4_0_6; -.
DR InParanoid; P00904; -.
DR OMA; VIYRNHV; -.
DR PhylomeDB; P00904; -.
DR BioCyc; EcoCyc:ANTHRANSYNCOMPII-MON; -.
DR BioCyc; MetaCyc:ANTHRANSYNCOMPII-MON; -.
DR SABIO-RK; P00904; -.
DR UniPathway; UPA00035; UER00040.
DR UniPathway; UPA00035; UER00041.
DR PRO; PR:P00904; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005950; C:anthranilate synthase complex; IC:ComplexPortal.
DR GO; GO:0004048; F:anthranilate phosphoribosyltransferase activity; IDA:EcoCyc.
DR GO; GO:0004049; F:anthranilate synthase activity; IDA:EcoCyc.
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; IDA:EcoCyc.
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 Allosteric enzyme; Amino-acid biosynthesis;
KW Aromatic amino acid biosynthesis; Direct protein sequencing;
KW Glutamine amidotransferase; Glycosyltransferase; Lyase;
KW Multifunctional enzyme; Reference proteome; Transferase;
KW Tryptophan biosynthesis.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:4594441"
FT CHAIN 2..531
FT /note="Bifunctional protein TrpGD"
FT /id="PRO_0000056877"
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 61
FT /note="P -> A (in Ref. 2; CAA23665)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="Q -> H (in Ref. 1; CAA23672 and 2; CAA23665)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 531 AA; 56870 MW; 10B02E455194F072 CRC64;
MADILLLDNI DSFTYNLADQ LRSNGHNVVI YRNHIPAQTL IERLATMSNP VLMLSPGPGV
PSEAGCMPEL LTRLRGKLPI IGICLGHQAI VEAYGGYVGQ AGEILHGKAS SIEHDGQAMF
AGLTNPLPVA RYHSLVGSNI PAGLTINAHF NGMVMAVRHD ADRVCGFQFH PESILTTQGA
RLLEQTLAWA QQKLEPANTL QPILEKLYQA QTLSQQESHQ LFSAVVRGEL KPEQLAAALV
SMKIRGEHPN EIAGAATALL ENAAPFPRPD YLFADIVGTG GDGSNSINIS TASAFVAAAC
GLKVAKHGNR SVSSKSGSSD LLAAFGINLD MNADKSRQAL DELGVCFLFA PKYHTGFRHA
MPVRQQLKTR TLFNVLGPLI NPAHPPLALI GVYSPELVLP IAETLRVLGY QRAAVVHSGG
MDEVSLHAPT IVAELHDGEI KSYQLTAEDF GLTPYHQEQL AGGTPEENRD ILTRLLQGKG
DAAHEAAVAA NVAMLMRLHG HEDLQANAQT VLEVLRSGSA YDRVTALAAR G
