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Protein

Anthranilate synthase component II

Gene

trpG-TRPD

Organism
Shigella dysenteriae
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

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

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. Anthranilate synthase component II (trpG-TRPD)
  2. Anthranilate synthase component II (trpG-TRPD)
  3. no protein annotated in this organism
  4. no protein annotated in this organism
  5. Tryptophan synthase (trpB), Tryptophan synthase (trpB), Tryptophan synthase (trpB), Tryptophan synthase (trpB), Tryptophan synthase (trpB), Tryptophan synthase (trpB), Tryptophan synthase (trpB), Tryptophan synthase (trpB), Tryptophan synthase (trpB), Tryptophan synthase (trpB), Tryptophan synthase (trpA), Tryptophan synthase (trpB), Tryptophan synthase (trpA), Tryptophan synthase (trpB), Tryptophan synthase (trpA), Tryptophan synthase (trpA), Tryptophan synthase (trpA), Tryptophan synthase (trpB), Tryptophan synthase (trpA), Tryptophan synthase (trpA), Tryptophan synthase (trpB), Tryptophan synthase (trpA), Tryptophan synthase (trpA), Tryptophan synthase (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 activityPROSITE-ProRule annotation1
Binding sitei88GlutamineBy similarity1
Active sitei170For GATase activityPROSITE-ProRule annotation1
Active sitei172For GATase activityPROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywords - Molecular functioni

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:
Anthranilate synthase component II (EC:4.1.3.27)
Including the following 2 domains:
Glutamine amidotransferase
Anthranilate phosphoribosyltransferase (EC:2.4.2.18)
Gene namesi
Name:trpG-TRPD
OrganismiShigella dysenteriae
Taxonomic identifieri622 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeShigella

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00000568992 – ›201Anthranilate synthase component IIAdd BLAST›200

Interactioni

Subunit structurei

Tetramer of two components I and two components II.

Structurei

3D structure databases

ProteinModelPortaliP00906.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni57 – 59Glutamine bindingBy similarity3
Regioni134 – 135Glutamine bindingBy similarity2

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: Fragment.

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

P00906-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADILLLDNI DSFTYNLADQ LRSNGHNVVI YRNHIPAQTL IERLATMSNP
60 70 80 90 100
VLMLSPGPGV PSEAGCMPEL LTRLSGKLPI IGICLGHQAI VEAYGGYVGQ
110 120 130 140 150
AGEILHGKAS SIEHDGQAMF AGLTNPLPVA RYHSLVGSNI PAGLTINAHF
160 170 180 190 200
NGMVMAVRHD ADRICGFQFH PESILTTQGA RLLEQTLAWA QRKLEPTNTL

Q
Length:201
Mass (Da):21,700
Last modified:January 23, 2007 - v2
Checksum:i943E3DBE4F0E59AF
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei2011

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01787 Genomic DNA. Translation: AAA57307.1.
PIRiB92860. NNEB2D.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01787 Genomic DNA. Translation: AAA57307.1.
PIRiB92860. NNEB2D.

3D structure databases

ProteinModelPortaliP00906.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiC26.960.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00035; UER00040.
UPA00035; UER00041.

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_SHIDY
AccessioniPrimary (citable) accession number: P00906
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Component I catalyzes the formation of anthranilate using ammonia rather than glutamine, whereas component II provides glutamine amidotransferase activity.
In E.coli and certain other bacteria, component II is larger and its C-terminal two thirds has anthranilate phosphoribosyltransferase activity.

Keywords - Technical termi

Multifunctional enzyme

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.