ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P00898


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name TRPE_SALTY
Primary accession number P00898
Secondary accession numbers None
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on January 23, 2002 (Sequence version 3)
Annotations were last modified on    December 16, 2008 (Entry version 83)
Name and origin of the protein
Protein name Anthranilate synthase component 1
Synonyms EC 4.1.3.27
Anthranilate synthase component I
Gene name
Name: trpE
OrderedLocusNames: STM1723
From
Salmonella typhimurium [TaxID: 602] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Salmonella.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0022-2836(82)90003-1; PubMed=7042989 [NCBI, ExPASy, EBI, Israel, Japan]
Yanofsky C., van Cleemput M.;
"Nucleotide sequence of trpE of Salmonella typhimurium and its homology with the corresponding sequence of Escherichia coli.";
J. Mol. Biol. 155:235-246(1982).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=LT2 / SGSC1412 / ATCC 700720;
DOI=10.1038/35101614; PubMed=11677609 [NCBI, ExPASy, EBI, Israel, Japan]
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E., Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.;
"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
Nature 413:852-856(2001).
[3]
PROTEIN SEQUENCE OF 1-25.
STRAIN=ST-13;
DOI=10.1021/bi00705a028; PubMed=4598537 [NCBI, ExPASy, EBI, Israel, Japan]
Li S.-L., Hanlon J., Yanofsky C.;
"Separation of anthranilate synthetase components I and II of Escherichia coli, Salmonella typhimurium, and Serratia marcescens and determination of their amino-terminal sequences by automatic Edman degradation.";
Biochemistry 13:1736-1744(1974).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-39.
DOI=10.1016/S0022-2836(78)80005-9; PubMed=351195 [NCBI, ExPASy, EBI, Israel, Japan]
Lee F., Bertrand K., Bennett G.N., Yanofsky C.;
"Comparison of the nucleotide sequences of the initial transcribed regions of the tryptophan operons of Escherichia coli and Salmonella typhimurium.";
J. Mol. Biol. 121:193-217(1978).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 495-520.
STRAIN=LT2;
DOI=10.1016/0022-2836(80)90260-0; PubMed=7007652 [NCBI, ExPASy, EBI, Israel, Japan]
Nichols B.P., Miozzari G.F., van Cleemput M., Bennett G.N., Yanofsky C.;
"Nucleotide sequences of the trpG regions of Escherichia coli, Shigella dysenteriae, Salmonella typhimurium and Serratia marcescens.";
J. Mol. Biol. 142:503-517(1980).
[6]
ENZYME REGULATION, AND MUTAGENESIS OF GLU-39; SER-40; ALA-41; ARG-128; CYS-174; ASN-288; PRO-289; MET-293; PHE-294; GLY-305; ARG-402; GLY-460; CYS-465 AND HIS-515.
PubMed=2022650 [NCBI, ExPASy, EBI, Israel, Japan]
Caligiuri M.G., Bauerle R.;
"Identification of amino acid residues involved in feedback regulation of the anthranilate synthase complex from Salmonella typhimurium. Evidence for an amino-terminal regulatory site.";
J. Biol. Chem. 266:8328-8335(1991).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
V01378; CAA24668.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE008776; AAL20641.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M24960; AAA27238.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J01811; AAA57311.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A92878; NNEB1T.
RefSeq NP_460682.1; -.
3D structure databases
PDB
1I1Q; X-ray; 1.90 A; A=1-520.[ExPASy / RCSB / EBI]
PDBsum 1I1Q; -.
ModBase P00898.
Protein-protein interaction databases
IntAct P00898; 1.
Enzyme and pathway databases
BioCyc STYP99287:STM1723-MON; -.
Organism-specific databases
StyGene SG10392; trpE.
Ontologies
GO
GO:0004049; Molecular function: anthranilate synthase activity (inferred from electronic annotation from InterPro).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0000162; Biological process: tryptophan biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR006805; Anth_synth_I_N.
IPR015890; Chorismate-bd_C.
IPR005801; TRPE_1_chor_bd.
IPR005257; TrpE_synth.
Graphical view of domain structure.
Gene3D G3DSA:3.60.120.10; TRPE_1_chor_bd; 1.
PANTHER PTHR11236; TRPE_1_chor_bd; 1.
Pfam PF04715; Anth_synt_I_N; 1.
PF00425; Chorismate_bind; 1.
Pfam graphical view of domain structure.
PRINTS PR00095; ANTSNTHASEI.
ProDom PD000779; Anth_synth_chor; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR00565; trpE_proteo; 1.
Proteomics databases
PRIDE P00898; -.
Genome annotation databases
GeneID 1253242; -.
GenomeReviews AE006468_GR; STM1723.
KEGG stm:STM1723; -.
NMPDR fig|99287.1.peg.1669; -.
Phylogenomic databases
HOGENOM P00898; -.
Genome annotation databases
CMR P00898; STM1723.
Other
ProtoNet P00898.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Complete proteome; Direct protein sequencing; Lyase; Tryptophan biosynthesis.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   520  520     Anthranilate synthase component 1. PRO_0000154110
MUTAGEN   39    39        E->K: Complete loss of feedback control by tryptophan. Loss of tryptophan binding. 
MUTAGEN   40    40        S->F: Complete loss of feedback control by tryptophan. Loss of tryptophan binding. 
MUTAGEN   41    41        A->V: Decrease in feedback control by tryptophan. 
MUTAGEN   128   128        R->H: Almost no change in feedback control by tryptophan. 
MUTAGEN   174   174        C->Y: Almost no change in feedback control by tryptophan. 
MUTAGEN   288   288        N->D: Decrease in feedback control by tryptophan. 
MUTAGEN   289   289        P->L: Decrease in feedback control by tryptophan. 
MUTAGEN   293   293        M->T: Complete loss of feedback control by tryptophan. Loss of tryptophan binding. 
MUTAGEN   294   294        F->L: Decrease in feedback control by tryptophan. 
MUTAGEN   305   305        G->S: Decrease in feedback control by tryptophan. 
MUTAGEN   402   402        R->W: Almost no change in feedback control by tryptophan. 
MUTAGEN   460   460        G->D: Almost no change in feedback control by tryptophan. 
MUTAGEN   465   465        C->Y: Complete loss of feedback control by tryptophan. Loss of tryptophan binding. 
MUTAGEN   515   515        H->Y: Almost no change in feedback control by tryptophan. 
CONFLICT   61    61        I -> F (in Ref. 1; CAA24668). 
CONFLICT   70    70        I -> S (in Ref. 1; CAA24668). 
CONFLICT   164   164        L -> H (in Ref. 1; CAA24668). 
CONFLICT   179   179        E -> G (in Ref. 1; CAA24668). 
CONFLICT   187   187        Q -> R (in Ref. 1; CAA24668). 
CONFLICT   348   348        I -> T (in Ref. 1; CAA24668). 
CONFLICT   359   360        LS -> PC (in Ref. 1; CAA24668). 
CONFLICT   368   368        L -> P (in Ref. 1; CAA24668). 
CONFLICT   395   395        Y -> C (in Ref. 1). 
CONFLICT   397   397        M -> I (in Ref. 1). 
CONFLICT   481   481        Q -> R (in Ref. 1; CAA24668). 
STRAND   9    15  7      
HELIX   21    29  9      
STRAND   33    39  7      
HELIX   43    45  3      
STRAND   50    64  15      
STRAND   67    74  8      
HELIX   75    78  4      
HELIX   80    85  6      
STRAND   93    97  5      
STRAND   100   104  5      
HELIX   114   118  5      
HELIX   125   132  8      
STRAND   143   150  8      
HELIX   152   157  6      
STRAND   167   169  3      
STRAND   172   185  14      
TURN   186   189  4      
STRAND   190   197  8      
HELIX   202   220  19      
STRAND   237   240  4      
HELIX   242   257  16      
STRAND   262   264  3      
STRAND   267   273  7      
HELIX   277   287  11      
STRAND   291   297  7      
STRAND   302   309  8      
STRAND   311   315  5      
TURN   316   319  4      
STRAND   320   323  4      
STRAND   326   331  6      
HELIX   342   354  13      
HELIX   356   376  21      
STRAND   383   392  10      
STRAND   394   407  14      
HELIX   413   420  8      
HELIX   424   426  3      
STRAND   427   430  4      
HELIX   431   442  12      
TURN   447   450  4      
STRAND   451   457  7      
STRAND   462   466  5      
STRAND   469   474  6      
STRAND   477   483  7      
HELIX   492   513  22      
Sequence information
Length: 520 AA [This is the length of the unprocessed precursor] Molecular weight: 57088 Da [This is the MW of the unprocessed precursor] CRC64: B120E903DB7F8329 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MQTPKPTLEL LTCDAAYREN PTALFHQVCG DRPATLLLES ADIDSKDDLK SLLLVDSALR 

        70         80         90        100        110        120 
ITALGDTVTI QALSDNGASL LPLLDTALPA GVENDVLPAG RVLRFPPVSP LLDEDARLCS 

       130        140        150        160        170        180 
LSVFDAFRLL QGVVNIPTQE REAMFFGGLF AYDLVAGFEA LPHLEAGNNC PDYCFYLAET 

       190        200        210        220        230        240 
LMVIDHQKKS TRIQASLFTA SDREKQRLNA RLAYLSQQLT QPAPPLPVTP VPDMRCECNQ 

       250        260        270        280        290        300 
SDDAFGAVVR QLQKAIRAGE IFQVVPSRRF SLPCPSPLAA YYVLKKSNPS PYMFFMQDND 

       310        320        330        340        350        360 
FTLFGASPES SLKYDAASRQ IEIYPIAGTR PRGRRADGTL DRDLDSRIEL DMRTDHKELS 

       370        380        390        400        410        420 
EHLMLVDLAR NDLARICTPG SRYVADLTKV DRYSYVMHLV SRVVGELRHD LDALHAYRAC 

       430        440        450        460        470        480 
MNMGTLSGAP KVRAMQLIAD AEGQRRGSYG GAVGYFTAHG DLDTCIVIRS ALVENGIATV 

       490        500        510        520 
QAGAGIVLDS VPQSEADETR NKARAVLRAI ATAHHAQETF 

P00898 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ca flag CBR Canada Mirror sites: Australia  Brazil  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!