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Protein

Bifunctional protein TrpGD

Gene

trpGD

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia. In addition to synthesizing anthranilate, it also catalyzes the second step of the pathway, the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate.3 Publications

Catalytic activityi

Chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate.
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate = anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate.

Enzyme regulationi

Cooperatively feedback inhibited by tryptophan.3 Publications

Kineticsi

  1. KM=1.2 µM for chorismate (at pH 7.5)3 Publications
  2. KM=5 µM for chorismate (at 25 degrees Celsius and at pH 7.8)3 Publications
  3. KM=360 µM for glutamine (at pH 7.5)3 Publications
  1. Vmax=0.53 nmol/min/mg enzyme (at 25 degrees Celsius and at pH 7.8)3 Publications

Pathwayi: L-tryptophan biosynthesis

This protein is involved in step 1 and 2 of the subpathway that synthesizes L-tryptophan from chorismate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Bifunctional protein TrpGD (trpGD), Anthranilate synthase component 1 (trpE)
  2. Bifunctional protein TrpGD (trpGD)
  3. Tryptophan biosynthesis protein TrpCF (trpC)
  4. Tryptophan biosynthesis protein TrpCF (trpC)
  5. Tryptophan synthase alpha chain (trpA), Tryptophan synthase beta chain (trpB)
This subpathway is part of the pathway L-tryptophan biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-tryptophan from chorismate, the pathway L-tryptophan biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei84 – 841Nucleophile; for GATase activityBy similarity
Binding sitei88 – 881GlutamineBy similarity
Active sitei170 – 1701For GATase activityBy similarity
Active sitei172 – 1721For GATase activityBy similarity

GO - Molecular functioni

  • anthranilate phosphoribosyltransferase activity Source: EcoCyc
  • anthranilate synthase activity Source: EcoCyc
  • magnesium ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  • glutamine metabolic process Source: UniProtKB-KW
  • tryptophan biosynthetic process Source: EcoCyc

Keywords - Molecular functioni

Glycosyltransferase, Lyase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Aromatic amino acid biosynthesis, Tryptophan biosynthesis

Enzyme and pathway databases

BioCyciEcoCyc:ANTHRANSYNCOMPII-MONOMER.
ECOL316407:JW1255-MONOMER.
MetaCyc:ANTHRANSYNCOMPII-MONOMER.
UniPathwayiUPA00035; UER00040.
UPA00035; UER00041.

Protein family/group databases

MEROPSiC26.960.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional protein TrpGD
Including the following 2 domains:
Anthranilate synthase component 2 (EC:4.1.3.27)
Short name:
AS
Short name:
ASII
Alternative name(s):
Anthranilate synthase, glutamine amidotransferase component
Anthranilate phosphoribosyltransferase (EC:2.4.2.18)
Gene namesi
Name:trpGD
Synonyms:trpD
Ordered Locus Names:b1263, JW1255
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11027. trpD.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 531530Bifunctional protein TrpGDPRO_0000056877Add
BLAST

Proteomic databases

PaxDbiP00904.
PRIDEiP00904.

2D gel databases

SWISS-2DPAGEP00904.

Interactioni

Subunit structurei

Heterotetramer consisting of two non-identical subunits: a beta subunit (TrpG) and a large alpha subunit (TrpE).By similarity

Protein-protein interaction databases

BioGridi4260123. 24 interactions.
STRINGi511145.b1263.

Structurei

3D structure databases

ProteinModelPortaliP00904.
SMRiP00904. Positions 2-193, 199-530.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 196194Glutamine amidotransferase type-1Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni57 – 593Glutamine bindingBy similarity
Regioni134 – 1352Glutamine bindingBy similarity
Regioni202 – 531330Anthranilate phosphoribosyltransferaseAdd
BLAST

Sequence similaritiesi

In the C-terminal section; belongs to the anthranilate phosphoribosyltransferase family.Curated

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

eggNOGiENOG4108EFP. Bacteria.
COG0512. LUCA.
COG0547. LUCA.
HOGENOMiHOG000230451.
InParanoidiP00904.
KOiK13497.
OMAiVIYRNHV.
OrthoDBiEOG6D5G6B.
PhylomeDBiP00904.

Family and domain databases

Gene3Di3.40.1030.10. 1 hit.
3.40.50.880. 1 hit.
HAMAPiMF_00211. TrpD.
InterProiIPR005940. Anthranilate_Pribosyl_Tfrase.
IPR029062. Class_I_gatase-like.
IPR017926. GATASE.
IPR000312. Glycosyl_Trfase_fam3.
IPR017459. Glycosyl_Trfase_fam3_N_dom.
IPR006221. TrpG/PapA_dom.
[Graphical view]
PfamiPF00117. GATase. 1 hit.
PF02885. Glycos_trans_3N. 1 hit.
PF00591. Glycos_transf_3. 1 hit.
[Graphical view]
SUPFAMiSSF47648. SSF47648. 1 hit.
SSF52317. SSF52317. 1 hit.
SSF52418. SSF52418. 1 hit.
TIGRFAMsiTIGR01245. trpD. 1 hit.
TIGR00566. trpG_papA. 1 hit.
PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00904-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADILLLDNI DSFTYNLADQ LRSNGHNVVI YRNHIPAQTL IERLATMSNP
60 70 80 90 100
VLMLSPGPGV PSEAGCMPEL LTRLRGKLPI IGICLGHQAI VEAYGGYVGQ
110 120 130 140 150
AGEILHGKAS SIEHDGQAMF AGLTNPLPVA RYHSLVGSNI PAGLTINAHF
160 170 180 190 200
NGMVMAVRHD ADRVCGFQFH PESILTTQGA RLLEQTLAWA QQKLEPANTL
210 220 230 240 250
QPILEKLYQA QTLSQQESHQ LFSAVVRGEL KPEQLAAALV SMKIRGEHPN
260 270 280 290 300
EIAGAATALL ENAAPFPRPD YLFADIVGTG GDGSNSINIS TASAFVAAAC
310 320 330 340 350
GLKVAKHGNR SVSSKSGSSD LLAAFGINLD MNADKSRQAL DELGVCFLFA
360 370 380 390 400
PKYHTGFRHA MPVRQQLKTR TLFNVLGPLI NPAHPPLALI GVYSPELVLP
410 420 430 440 450
IAETLRVLGY QRAAVVHSGG MDEVSLHAPT IVAELHDGEI KSYQLTAEDF
460 470 480 490 500
GLTPYHQEQL AGGTPEENRD ILTRLLQGKG DAAHEAAVAA NVAMLMRLHG
510 520 530
HEDLQANAQT VLEVLRSGSA YDRVTALAAR G
Length:531
Mass (Da):56,870
Last modified:January 23, 2007 - v3
Checksum:i10B02E455194F072
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti61 – 611P → A in CAA23665 (PubMed:6283099).Curated
Sequence conflicti192 – 1921Q → H in CAA23672 (PubMed:7038627).Curated
Sequence conflicti192 – 1921Q → H in CAA23665 (PubMed:6283099).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00372 Genomic DNA. Translation: CAA23672.1.
V00367 Genomic DNA. Translation: CAA23665.1.
J01714 Genomic DNA. Translation: AAA57298.1.
U00096 Genomic DNA. Translation: AAC74345.1.
AP009048 Genomic DNA. Translation: BAA14798.1.
PIRiB64874. NNEC2.
RefSeqiNP_415779.1. NC_000913.3.
WP_000763511.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74345; AAC74345; b1263.
BAA14798; BAA14798; BAA14798.
GeneIDi945109.
KEGGiecj:JW1255.
eco:b1263.
PATRICi32117786. VBIEscCol129921_1313.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00372 Genomic DNA. Translation: CAA23672.1.
V00367 Genomic DNA. Translation: CAA23665.1.
J01714 Genomic DNA. Translation: AAA57298.1.
U00096 Genomic DNA. Translation: AAC74345.1.
AP009048 Genomic DNA. Translation: BAA14798.1.
PIRiB64874. NNEC2.
RefSeqiNP_415779.1. NC_000913.3.
WP_000763511.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP00904.
SMRiP00904. Positions 2-193, 199-530.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260123. 24 interactions.
STRINGi511145.b1263.

Protein family/group databases

MEROPSiC26.960.

2D gel databases

SWISS-2DPAGEP00904.

Proteomic databases

PaxDbiP00904.
PRIDEiP00904.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74345; AAC74345; b1263.
BAA14798; BAA14798; BAA14798.
GeneIDi945109.
KEGGiecj:JW1255.
eco:b1263.
PATRICi32117786. VBIEscCol129921_1313.

Organism-specific databases

EchoBASEiEB1020.
EcoGeneiEG11027. trpD.

Phylogenomic databases

eggNOGiENOG4108EFP. Bacteria.
COG0512. LUCA.
COG0547. LUCA.
HOGENOMiHOG000230451.
InParanoidiP00904.
KOiK13497.
OMAiVIYRNHV.
OrthoDBiEOG6D5G6B.
PhylomeDBiP00904.

Enzyme and pathway databases

UniPathwayiUPA00035; UER00040.
UPA00035; UER00041.
BioCyciEcoCyc:ANTHRANSYNCOMPII-MONOMER.
ECOL316407:JW1255-MONOMER.
MetaCyc:ANTHRANSYNCOMPII-MONOMER.

Miscellaneous databases

PROiP00904.

Family and domain databases

Gene3Di3.40.1030.10. 1 hit.
3.40.50.880. 1 hit.
HAMAPiMF_00211. TrpD.
InterProiIPR005940. Anthranilate_Pribosyl_Tfrase.
IPR029062. Class_I_gatase-like.
IPR017926. GATASE.
IPR000312. Glycosyl_Trfase_fam3.
IPR017459. Glycosyl_Trfase_fam3_N_dom.
IPR006221. TrpG/PapA_dom.
[Graphical view]
PfamiPF00117. GATase. 1 hit.
PF02885. Glycos_trans_3N. 1 hit.
PF00591. Glycos_transf_3. 1 hit.
[Graphical view]
SUPFAMiSSF47648. SSF47648. 1 hit.
SSF52317. SSF52317. 1 hit.
SSF52418. SSF52418. 1 hit.
TIGRFAMsiTIGR01245. trpD. 1 hit.
TIGR00566. trpG_papA. 1 hit.
PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The complete nucleotide sequence of the tryptophan operon of Escherichia coli."
    Yanofsky C., Platt T., Crawford I.P., Nichols B.P., Christie G.E., Horowitz H., van Cleemput M., Wu A.M.
    Nucleic Acids Res. 9:6647-6668(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Nucleotide sequence of the trpD gene, encoding anthranilate synthetase component II of Escherichia coli."
    Horowitz H., Christie G.E., Platt T.
    J. Mol. Biol. 156:245-256(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "Structural homology of the glutamine amidotransferase subunits of the anthranilate synthetases of Escherichia coli, Salmonella typhimurium and Serratia marcescens."
    Li S.-L., Hanlon J., Yanofsky C.
    Nature 248:48-50(1974) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-62.
  7. "Anthranilate synthetase. Partial purification and some kinetic studies on the enzyme from Escherichia coli."
    Baker T.I., Crawford I.P.
    J. Biol. Chem. 241:5577-5584(1966) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
  8. "Feedback regulation in the anthranilate aggregate from wild type and mutant strains of Escherichia coli."
    Pabst M.J., Kuhn J.C., Somerville R.L.
    J. Biol. Chem. 248:901-914(1973) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
  9. "The anthranilate aggregate of Escherichia coli: kinetics of inhibition by tryptophan of phosphoribosyltransferase."
    Gonzalez J.E., Somerville R.L.
    Biochem. Cell Biol. 64:681-691(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
  10. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.

Entry informationi

Entry nameiTRPGD_ECOLI
AccessioniPrimary (citable) accession number: P00904
Secondary accession number(s): P76833, P76835, P78302
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: February 17, 2016
This is version 151 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.