Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Anthranilate synthase component 1

Gene

trpE

Organism
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Status
Reviewed-Annotation score: Annotation score: 3 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 (By similarity).By similarity

Catalytic activityi

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

Cofactori

Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit.By similarity

Enzyme regulationi

Feedback inhibited by tryptophan.By similarity

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)
  2. Anthranilate phosphoribosyltransferase (trpD)
  3. Phosphoribosyl isomerase A (priA), Phosphoribosyl isomerase A (priA)
  4. Indole-3-glycerol phosphate synthase (trpC)
  5. Tryptophan synthase alpha chain (trpA), Tryptophan synthase beta chain (trpB), Tryptophan synthase (MSMEG_3309)
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
Binding sitei74 – 741TryptophanBy similarity
Metal bindingi366 – 3661MagnesiumBy similarity
Binding sitei454 – 4541ChorismateBy similarity
Binding sitei474 – 4741ChorismateBy similarity
Binding sitei490 – 4901Chorismate; via amide nitrogenBy similarity
Metal bindingi503 – 5031MagnesiumBy similarity

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

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciMSME246196:GJ4Y-3217-MONOMER.
UniPathwayiUPA00035; UER00040.

Names & Taxonomyi

Protein namesi
Recommended name:
Anthranilate synthase component 1 (EC:4.1.3.27)
Short name:
AS
Short name:
ASI
Gene namesi
Name:trpE
Ordered Locus Names:MSMEG_3217, MSMEI_3135
OrganismiMycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Taxonomic identifieri246196 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium
Proteomesi
  • UP000006158 Componenti: Chromosome
  • UP000000757 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 524524Anthranilate synthase component 1PRO_0000396112Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki355 – 355Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)1 Publication

Keywords - PTMi

Isopeptide bond, Ubl conjugation

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

STRINGi246196.MSMEG_3217.

Structurei

3D structure databases

ProteinModelPortaliA0QX93.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni298 – 3003Tryptophan bindingBy similarity
Regioni339 – 3402Chorismate bindingBy similarity
Regioni488 – 4903Chorismate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CRQ. Bacteria.
COG0147. LUCA.
HOGENOMiHOG000025142.
KOiK01657.
OMAiMLRASNP.
OrthoDBiEOG6D5G6B.

Family and domain databases

Gene3Di3.60.120.10. 1 hit.
InterProiIPR005801. ADC_synthase.
IPR019999. Anth_synth_I-like.
IPR006805. Anth_synth_I_N.
IPR005256. Anth_synth_I_PabB.
IPR015890. Chorismate_C.
[Graphical view]
PfamiPF04715. Anth_synt_I_N. 1 hit.
PF00425. Chorismate_bind. 1 hit.
[Graphical view]
PRINTSiPR00095. ANTSNTHASEI.
SUPFAMiSSF56322. SSF56322. 1 hit.
TIGRFAMsiTIGR00564. trpE_most. 1 hit.

Sequencei

Sequence statusi: Complete.

A0QX93-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQTTANHSSR STQTGTRAHG AALAETTSRE DFRALATEHR VVPVIRKVLA
60 70 80 90 100
DSETPLSAYR KLAANRPGTF LLESAENGRS WSRWSFIGAG APSALTVRDN
110 120 130 140 150
AAAWLGTAPE GAPSGGDPLD ALRATLDLLK TEAMAGLPPL SSGLVGFFAY
160 170 180 190 200
DMVRRLERLP ELAVDDLGLP DMLLLLATDI AAVDHHEGTI TLIANAVNWN
210 220 230 240 250
GTDERVDWAY DDAVARLDVM TKALGQPLTS AVATFSRPAP DHRAQRTMEE
260 270 280 290 300
YTEIVDKLVG DIEAGEAFQV VPSQRFEMDT AADPLDVYRI LRVTNPSPYM
310 320 330 340 350
YLLNIPDADG GLDFSIVGSS PEALVTVKDG RATTHPIAGT RWRGATEEED
360 370 380 390 400
VLLEKELLAD EKERAEHLML VDLGRNDLGR VCRPGTVRVD DYSHIERYSH
410 420 430 440 450
VMHLVSTVTG ELAEDKTALD AVTACFPAGT LSGAPKVRAM ELIEEVEKTR
460 470 480 490 500
RGLYGGVVGY LDFAGNADFA IAIRTALMRN GTAYVQAGGG VVADSNGPYE
510 520
YTEAANKARA VLNAIAAAAT LAEP
Length:524
Mass (Da):56,311
Last modified:January 9, 2007 - v1
Checksum:i20535CB359AF510F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000480 Genomic DNA. Translation: ABK74885.1.
CP001663 Genomic DNA. Translation: AFP39599.1.
RefSeqiWP_003894606.1. NZ_CP009494.1.
YP_887531.1. NC_008596.1.

Genome annotation databases

EnsemblBacteriaiABK74885; ABK74885; MSMEG_3217.
AFP39599; AFP39599; MSMEI_3135.
GeneIDi4531670.
KEGGimsb:LJ00_15995.
msg:MSMEI_3135.
msm:MSMEG_3217.
PATRICi18078862. VBIMycSme59918_3179.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000480 Genomic DNA. Translation: ABK74885.1.
CP001663 Genomic DNA. Translation: AFP39599.1.
RefSeqiWP_003894606.1. NZ_CP009494.1.
YP_887531.1. NC_008596.1.

3D structure databases

ProteinModelPortaliA0QX93.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi246196.MSMEG_3217.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABK74885; ABK74885; MSMEG_3217.
AFP39599; AFP39599; MSMEI_3135.
GeneIDi4531670.
KEGGimsb:LJ00_15995.
msg:MSMEI_3135.
msm:MSMEG_3217.
PATRICi18078862. VBIMycSme59918_3179.

Phylogenomic databases

eggNOGiENOG4105CRQ. Bacteria.
COG0147. LUCA.
HOGENOMiHOG000025142.
KOiK01657.
OMAiMLRASNP.
OrthoDBiEOG6D5G6B.

Enzyme and pathway databases

UniPathwayiUPA00035; UER00040.
BioCyciMSME246196:GJ4Y-3217-MONOMER.

Family and domain databases

Gene3Di3.60.120.10. 1 hit.
InterProiIPR005801. ADC_synthase.
IPR019999. Anth_synth_I-like.
IPR006805. Anth_synth_I_N.
IPR005256. Anth_synth_I_PabB.
IPR015890. Chorismate_C.
[Graphical view]
PfamiPF04715. Anth_synt_I_N. 1 hit.
PF00425. Chorismate_bind. 1 hit.
[Graphical view]
PRINTSiPR00095. ANTSNTHASEI.
SUPFAMiSSF56322. SSF56322. 1 hit.
TIGRFAMsiTIGR00564. trpE_most. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., Fraser C.M.
    Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700084 / mc(2)155.
  2. "Interrupted coding sequences in Mycobacterium smegmatis: authentic mutations or sequencing errors?"
    Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C., Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.
    Genome Biol. 8:R20.1-R20.9(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700084 / mc(2)155.
  3. "Ortho-proteogenomics: multiple proteomes investigation through orthology and a new MS-based protocol."
    Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M., Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.
    Genome Res. 19:128-135(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700084 / mc(2)155.
  4. Cited for: PUPYLATION AT LYS-355, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiTRPE_MYCS2
AccessioniPrimary (citable) accession number: A0QX93
Secondary accession number(s): I7GAR3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 10, 2010
Last sequence update: January 9, 2007
Last modified: January 20, 2016
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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.