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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)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

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

BioCyciSENT99287:GCTI-1733-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:STM1724
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
Proteomesi
  • UP000001014 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 531530Bifunctional protein TrpGDPRO_0000056897Add
BLAST

Proteomic databases

PaxDbiP00905.
PRIDEiP00905.

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 interaction.
MINTiMINT-189132.
STRINGi99287.STM1724.

Structurei

Secondary structure

1
531
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 86Combined sources
Helixi14 – 2310Combined sources
Beta strandi27 – 326Combined sources
Helixi38 – 447Combined sources
Beta strandi48 – 547Combined sources
Helixi61 – 633Combined sources
Helixi67 – 748Combined sources
Beta strandi80 – 834Combined sources
Helixi85 – 939Combined sources
Beta strandi106 – 1149Combined sources
Helixi118 – 1203Combined sources
Beta strandi125 – 1317Combined sources
Beta strandi145 – 1506Combined sources
Beta strandi153 – 1597Combined sources
Turni160 – 1634Combined sources
Beta strandi164 – 1707Combined sources
Helixi179 – 19012Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1I1QX-ray1.90B2-193[»]
ProteinModelPortaliP00905.
SMRiP00905. Positions 2-193, 199-530.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00905.

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.
KOiK13497.
OMAiVIYRNHV.
OrthoDBiEOG6D5G6B.
PhylomeDBiP00905.

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.

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti191 – 1922QQ → LA in AAA57312 (PubMed:7007652).Curated
Sequence conflicti511 – 5111V → L in AAA27236 (PubMed:6355484).Curated

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1I1QX-ray1.90B2-193[»]
ProteinModelPortaliP00905.
SMRiP00905. Positions 2-193, 199-530.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Protein family/group databases

MEROPSiC26.960.

Proteomic databases

PaxDbiP00905.
PRIDEiP00905.

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.
OrthoDBiEOG6D5G6B.
PhylomeDBiP00905.

Enzyme and pathway databases

UniPathwayiUPA00035; UER00040.
UPA00035; UER00041.
BioCyciSENT99287:GCTI-1733-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP00905.

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. "Nucleotide sequence of the trpD and trpC genes of Salmonella typhimurium."
    Horowitz H., van Arsdell J., Platt T.
    J. Mol. Biol. 169:775-797(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: LT2 / SGSC1412 / ATCC 700720.
  3. "Nucleotide sequences of the trpG regions of Escherichia coli, Shigella dysenteriae, Salmonella typhimurium and Serratia marcescens."
    Nichols B.P., Miozzari G.F., van Cleemput M., Bennett G.N., Yanofsky C.
    J. Mol. Biol. 142:503-517(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-201.
  4. "Some physicochemical properties of anthranilate synthetase component I from Salmonella typhimurium."
    Nagano H., Zalkin H.
    J. Biol. Chem. 245:3097-3103(1970) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, SUBUNIT.
  5. "Identification of amino acid residues involved in feedback regulation of the anthranilate synthase complex from Salmonella typhimurium. Evidence for an amino-terminal regulatory site."
    Caligiuri M.G., Bauerle R.
    J. Biol. Chem. 266:8328-8335(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  6. "Crystallization and preliminary crystallographic studies of the anthranilate synthase partial complex from Salmonella typhimurium."
    Tolbert W.D., Chatterji S., Bauerle R., Kretsinger R.
    Acta Crystallogr. D 55:305-306(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CRYSTALLIZATION, SUBUNIT.
  7. "Structure of the cooperative allosteric anthranilate synthase from Salmonella typhimurium."
    Morollo A.A., Eck M.J.
    Nat. Struct. Biol. 8:243-247(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), SUBUNIT.

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: June 8, 2016
This is version 148 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.