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Protein

Anthranilate synthase component 2

Gene

trpG

Organism
Serratia marcescens
Status
Reviewed-Annotation score: Annotation score: 4 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 (Probable).1 Publication

Catalytic activityi

Chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate.

Pathwayi: L-tryptophan biosynthesis

This protein is involved in step 1 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. Anthranilate synthase component 1 (trpE), Anthranilate synthase component 1 (trpE), Anthranilate synthase component 2 (trpG), Anthranilate synthase component 1 (trpE), Anthranilate synthase component 1 (trpE), Anthranilate synthase component 1 (AAY84_22430), Anthranilate synthase component 1 (AR325_16160), Anthranilate synthase component 1 (trpE), Anthranilate synthase component 1 (AYJ10_05620)
  2. Anthranilate phosphoribosyltransferase (trpGD), Anthranilate phosphoribosyltransferase (trpD), Anthranilate phosphoribosyltransferase (trpD), Anthranilate phosphoribosyltransferase (trpD), Anthranilate phosphoribosyltransferase (trpD), Anthranilate phosphoribosyltransferase (trpD), Anthranilate phosphoribosyltransferase (trpD2), Anthranilate phosphoribosyltransferase (trpD), Anthranilate phosphoribosyltransferase (trpD)
  3. N-(5'-phosphoribosyl)anthranilate isomerase (trpF), N-(5'-phosphoribosyl)anthranilate isomerase (trpF)
  4. Indole-3-glycerol phosphate synthase (AAY84_22415), Tryptophan biosynthesis protein TrpCF (trpC), Tryptophan biosynthesis protein TrpCF (trpC), Indole-3-glycerol phosphate synthase (AR325_16175), Bifunctional indole-3-glycerol phosphate synthase/phosphoribosylanthranilate isomerase (AYJ10_05635), Tryptophan biosynthesis protein TrpCF (trpC), Tryptophan biosynthesis protein TrpCF (trpC)
  5. Tryptophan synthase alpha chain (trpA), Tryptophan synthase beta chain (trpB), Tryptophan synthase alpha chain (trpA), Tryptophan synthase alpha chain (trpA), Tryptophan synthase beta chain (trpB), Tryptophan synthase alpha chain (trpA), Tryptophan synthase beta chain (trpB), Tryptophan synthase alpha chain (trpA), Tryptophan synthase beta chain (trpB), Tryptophan synthase alpha chain (trpA), Tryptophan synthase beta chain (trpB), 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)DescriptionActionsGraphical viewLength
Active sitei84Nucleophile; for GATase activity1 Publication1
Binding sitei88Glutamine1 Publication1
Active sitei170For GATase activityPROSITE-ProRule annotation1
Active sitei172For GATase activityPROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

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

Enzyme and pathway databases

UniPathwayiUPA00035; UER00040.

Protein family/group databases

MEROPSiC26.960.

Names & Taxonomyi

Protein namesi
Recommended name:
Anthranilate synthase component 2 (EC:4.1.3.27)
Short name:
AS
Short name:
ASII
Alternative name(s):
Anthranilate synthase, GATase component
Anthranilate synthase, glutamine amidotransferase component
Gene namesi
Name:trpG
OrganismiSerratia marcescens
Taxonomic identifieri615 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesYersiniaceaeSerratia

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00000568982 – 193Anthranilate synthase component 2Add BLAST192

Proteomic databases

PRIDEiP00900.

Interactioni

Subunit structurei

Heterotetramer consisting of two non-identical subunits: a beta subunit (TrpG) and a large alpha subunit (TrpE).1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
trpEP008972EBI-1031352,EBI-1031345

Protein-protein interaction databases

IntActiP00900. 1 interactor.

Structurei

Secondary structure

1193
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
Helixi37 – 46Combined sources10
Beta strandi48 – 54Combined sources7
Helixi61 – 63Combined sources3
Helixi67 – 74Combined sources8
Turni75 – 77Combined sources3
Beta strandi80 – 83Combined sources4
Helixi85 – 93Combined sources9
Beta strandi97 – 114Combined sources18
Helixi118 – 120Combined sources3
Beta strandi125 – 139Combined sources15
Beta strandi144 – 150Combined sources7
Beta strandi153 – 159Combined sources7
Turni160 – 163Combined sources4
Beta strandi164 – 169Combined sources6
Helixi179 – 191Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1I7QX-ray1.95B/D1-193[»]
1I7SX-ray2.40B/D1-193[»]
ProteinModelPortaliP00900.
SMRiP00900.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00900.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini3 – 193Glutamine amidotransferase type-1PROSITE-ProRule annotationAdd BLAST191

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni57 – 59Glutamine binding1 Publication3
Regioni134 – 135Glutamine binding1 Publication2

Sequence similaritiesi

Contains 1 glutamine amidotransferase type-1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Glutamine amidotransferase

Family and domain databases

Gene3Di3.40.50.880. 1 hit.
InterProiIPR029062. Class_I_gatase-like.
IPR017926. GATASE.
IPR006221. TrpG/PapA_dom.
[Graphical view]
PfamiPF00117. GATase. 1 hit.
[Graphical view]
SUPFAMiSSF52317. SSF52317. 1 hit.
TIGRFAMsiTIGR00566. 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.

P00900-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADILLLDNV DSFTYNLVDQ LRASGHQVVI YRNQIGAEVI IERLQHMEQP
60 70 80 90 100
VLMLSPGPGT PSEAGCMPEL LQRLRGQLPI IGICLGHQAI VEAYGGQVGQ
110 120 130 140 150
AGEILHGKAS AIAHDGEGMF AGMANPLPVA RYHSLVGSNI PADLTVNARS
160 170 180 190
GEMVMAVRDD RRRVCGFQFH PESILTTHGA RLLEQTLAWA LAK
Length:193
Mass (Da):20,868
Last modified:January 23, 2007 - v2
Checksum:i8F53EBFEC7F4524A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti36G → A AA sequence (PubMed:6986371).Curated1
Sequence conflicti38E → Q AA sequence (PubMed:6986371).Curated1
Sequence conflicti38E → Q AA sequence (PubMed:4598537).Curated1
Sequence conflicti45Q → E AA sequence (PubMed:6986371).Curated1
Sequence conflicti46H → Q AA sequence (PubMed:4598537).Curated1
Sequence conflicti48E → T AA sequence (PubMed:6986371).Curated1
Sequence conflicti60 – 62TPS → ASV AA sequence (PubMed:4598537).Curated3
Sequence conflicti77Q → R AA sequence (PubMed:6986371).Curated1
Sequence conflicti150S → F AA sequence (PubMed:6986371).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY027546 Genomic DNA. Translation: AAK37409.1.
PIRiD92860. NNSE2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY027546 Genomic DNA. Translation: AAK37409.1.
PIRiD92860. NNSE2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1I7QX-ray1.95B/D1-193[»]
1I7SX-ray2.40B/D1-193[»]
ProteinModelPortaliP00900.
SMRiP00900.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP00900. 1 interactor.

Protein family/group databases

MEROPSiC26.960.

Proteomic databases

PRIDEiP00900.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00035; UER00040.

Miscellaneous databases

EvolutionaryTraceiP00900.

Family and domain databases

Gene3Di3.40.50.880. 1 hit.
InterProiIPR029062. Class_I_gatase-like.
IPR017926. GATASE.
IPR006221. TrpG/PapA_dom.
[Graphical view]
PfamiPF00117. GATase. 1 hit.
[Graphical view]
SUPFAMiSSF52317. SSF52317. 1 hit.
TIGRFAMsiTIGR00566. trpG_papA. 1 hit.
PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTRPG_SERMA
AccessioniPrimary (citable) accession number: P00900
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

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.