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Protein

Bifunctional protein TrpGD

Gene

trpGD

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
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.1 Publication

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.2 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 beta chain (trpB), Tryptophan synthase alpha chain (trpA)
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)DescriptionActionsGraphical viewLength
Active sitei84Nucleophile; for GATase activityBy similarity1
Binding sitei88GlutamineBy similarity1
Active sitei170For GATase activityBy similarity1
Active sitei172For GATase activityBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywords - Molecular functioni

Glycosyltransferase, Lyase, Transferase

Keywords - Biological processi

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

Enzyme and pathway databases

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:STM1724
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeSalmonella
Proteomesi
  • UP000001014 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000568972 – 531Bifunctional protein TrpGDAdd BLAST530

Proteomic databases

PaxDbiP00905.

Interactioni

Subunit structurei

Monomer. Heterotetramer consisting of two non-identical subunits: a beta subunit (TrpG) and a large alpha subunit (TrpE) (Probable).3 Publications

Protein-protein interaction databases

IntActiP00905. 1 interactor.
MINTiMINT-189132.
STRINGi99287.STM1724.

Structurei

Secondary structure

1531
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 8Combined sources6
Helixi14 – 23Combined sources10
Beta strandi27 – 32Combined sources6
Helixi38 – 44Combined sources7
Beta strandi48 – 54Combined sources7
Helixi61 – 63Combined sources3
Helixi67 – 74Combined sources8
Beta strandi80 – 83Combined sources4
Helixi85 – 93Combined sources9
Beta strandi106 – 114Combined sources9
Helixi118 – 120Combined sources3
Beta strandi125 – 131Combined sources7
Beta strandi145 – 150Combined sources6
Beta strandi153 – 159Combined sources7
Turni160 – 163Combined sources4
Beta strandi164 – 170Combined sources7
Helixi179 – 190Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1I1QX-ray1.90B2-193[»]
ProteinModelPortaliP00905.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00905.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini3 – 196Glutamine amidotransferase type-1Add BLAST194

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni57 – 59Glutamine bindingBy similarity3
Regioni134 – 135Glutamine bindingBy similarity2
Regioni202 – 531Anthranilate phosphoribosyltransferaseAdd BLAST330

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.
KOiK13497.
OMAiVIYRNHV.
PhylomeDBiP00905.

Family and domain databases

Gene3Di3.40.1030.10. 1 hit.
3.40.50.880. 1 hit.
HAMAPiMF_00211. TrpD. 1 hit.
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.

P00905-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADILLLDNI DSFTWNLADQ LRTNGHNVVI YRNHIPAQTL IDRLATMKNP
60 70 80 90 100
VLMLSPGPGV PSEAGCMPEL LTRLRGKLPI IGICLGHQAI VEAYGGYVGQ
110 120 130 140 150
AGEILHGKAS SIEHDGQAMF AGLANPLPVA RYHSLVGSNV PAGLTINAHF
160 170 180 190 200
NGMVMAVRHD ADRVCGFQFH PESILTTQGA RLLEQTLAWA QQKLEPTNTL
210 220 230 240 250
QPILEKLYQA QTLTQQESHQ LFSAVVRGEL KPEQLAAALV SMKIRGEHPN
260 270 280 290 300
EIAGAATALL ENAAPFPRPE YLFADIVGTG GDGSNSINIS TASAFVAAAC
310 320 330 340 350
GLKVAKHGNR SVSSKSGSSD LLAAFGINLD MNADKSRQAL DELGVCFLFA
360 370 380 390 400
PKYHTGLRHA MPVRQQLKTR TLFNVLGPLI NPAHPPLALI GVYSPELVLP
410 420 430 440 450
IAETLRVLGY QRAAVVHSGG MDEVSLHAPT IVAELHDGEI KSYQLTAEDF
460 470 480 490 500
GLTPYHQDQL AGGTPEENRD ILTRLLQGKG DAAHEAAVAA NVAMLMRLHG
510 520 530
QEDLKANAQT VLDVLRNGTA YDRVTALAAR G
Length:531
Mass (Da):56,918
Last modified:January 23, 2007 - v4
Checksum:i256D2409062CD4C7
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti191 – 192QQ → LA in AAA57312 (PubMed:7007652).Curated2
Sequence conflicti511V → L in AAA27236 (PubMed:6355484).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M30285 Genomic DNA. Translation: AAA27236.1.
AE006468 Genomic DNA. Translation: AAL20642.1.
J01811 Genomic DNA. Translation: AAA57312.1.
PIRiA92907. NNEB2T.
RefSeqiNP_460683.1. NC_003197.1.
WP_000763494.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL20642; AAL20642; STM1724.
GeneIDi1253243.
KEGGistm:STM1724.
PATRICi32381961. VBISalEnt20916_1820.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M30285 Genomic DNA. Translation: AAA27236.1.
AE006468 Genomic DNA. Translation: AAL20642.1.
J01811 Genomic DNA. Translation: AAA57312.1.
PIRiA92907. NNEB2T.
RefSeqiNP_460683.1. NC_003197.1.
WP_000763494.1. NC_003197.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1I1QX-ray1.90B2-193[»]
ProteinModelPortaliP00905.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP00905. 1 interactor.
MINTiMINT-189132.
STRINGi99287.STM1724.

Protein family/group databases

MEROPSiC26.960.

Proteomic databases

PaxDbiP00905.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL20642; AAL20642; STM1724.
GeneIDi1253243.
KEGGistm:STM1724.
PATRICi32381961. VBISalEnt20916_1820.

Phylogenomic databases

eggNOGiENOG4108EFP. Bacteria.
COG0512. LUCA.
COG0547. LUCA.
HOGENOMiHOG000230451.
KOiK13497.
OMAiVIYRNHV.
PhylomeDBiP00905.

Enzyme and pathway databases

UniPathwayiUPA00035; UER00040.
UPA00035; UER00041.

Miscellaneous databases

EvolutionaryTraceiP00905.

Family and domain databases

Gene3Di3.40.1030.10. 1 hit.
3.40.50.880. 1 hit.
HAMAPiMF_00211. TrpD. 1 hit.
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...

Entry informationi

Entry nameiTRPGD_SALTY
AccessioniPrimary (citable) accession number: P00905
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 151 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Allosteric enzyme, Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.