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UniProtKB/Swiss-Prot entry O94582


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

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Entry information
Entry name TRPE_SCHPO
Primary accession number O94582
Secondary accession number P78905
Integrated into Swiss-Prot on May 16, 2003
Sequence was last modified on May 1, 1999 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 51)
Name and origin of the protein
Protein name Probable anthranilate synthase component 1
Synonyms EC 4.1.3.27
Anthranilate synthase component I
Gene name
Name: trp3
ORFNames: SPCC1442.09
From
Schizosaccharomyces pombe (Fission yeast) [TaxID: 4896] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; Schizosaccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 38366 / 972;
DOI=10.1038/nature724; PubMed=11859360 [NCBI, ExPASy, EBI, Israel, Japan]
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 126-489.
STRAIN=PR745;
DOI=10.1093/dnares/4.6.363; PubMed=9501991 [NCBI, ExPASy, EBI, Israel, Japan]
Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
"Identification of open reading frames in Schizosaccharomyces pombe cDNAs.";
DNA Res. 4:363-369(1997).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390; SER-392 AND SER-488, AND MASS SPECTROMETRY.
DOI=10.1021/pr7006335; PubMed=18257517 [NCBI, ExPASy, EBI, Israel, Japan]
Wilson-Grady J.T., Villen J., Gygi S.P.;
"Phosphoproteome analysis of fission yeast.";
J. Proteome Res. 7:1088-1097(2008).
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
CU329672; CAA21443.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D89256; BAA13917.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T40974; T40974.
T43181; T43181.
RefSeq NP_588323.1; -.
3D structure databases
HSSP P05041; 1K0E. [HSSP ENTRY / PDB]
ModBase O94582.
Enzyme and pathway databases
BioCyc SPOM-XXX-01:SPOM-XXX-01-000246-MON; -.
Organism-specific databases
GeneDB_Spombe SPCC1442.09; -.
Gene expression databases
ArrayExpress O94582; -.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from direct assay from GeneDB_SPombe).
GO:0005634; Cellular component: nucleus (inferred from direct assay from GeneDB_SPombe).
GO:0004049; Molecular function: anthranilate synthase activity (inferred from electronic annotation from InterPro).
GO:0000162; Biological process: tryptophan biosynthetic process (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR006805; Anth_synth_I_N.
IPR005256; Anth_synthI.
IPR015890; Chorismate-bd_C.
IPR005801; TRPE_1_chor_bd.
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 TIGR00564; trpE_most; 1.
Genome annotation databases
GeneID 2538842; -.
KEGG spo:SPCC1442.09; -.
NMPDR fig|4896.1.peg.661; -.
Other
ProtoNet O94582.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Complete proteome; Lyase; Phosphoprotein; Tryptophan biosynthesis.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   489  489     Probable anthranilate synthase component 1. PRO_0000154133
MOD_RES   390   390        Phosphoserine. 
MOD_RES   392   392        Phosphoserine. 
MOD_RES   488   488        Phosphoserine. 
CONFLICT   144   144        D -> N (in Ref. 2; BAA13917). 
CONFLICT   156   156        K -> Q (in Ref. 2; BAA13917). 
CONFLICT   263   263        Y -> F (in Ref. 2; BAA13917). 
CONFLICT   305   305        K -> E (in Ref. 2; BAA13917). 
CONFLICT   320   320        K -> Q (in Ref. 2; BAA13917). 
CONFLICT   351   351        M -> R (in Ref. 2; BAA13917). 
CONFLICT   402   402        Y -> N (in Ref. 2; BAA13917). 
CONFLICT   411   411        I -> R (in Ref. 2; BAA13917). 
Sequence information
Length: 489 AA [This is the length of the unprocessed precursor] Molecular weight: 54960 Da [This is the MW of the unprocessed precursor] CRC64: 442D522BA59EBA31 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKIYPDLKQV QELAEKHKAN KIPIYGVIPA DMLTPSVAYL KLNQGKKYSF ILESVTQGES 

        70         80         90        100        110        120 
VSRYSFIGSP YRILMANGKT DPLARLEREL KEVKTAPVEG LPSFSGGAVG YVSYDCIKYF 

       130        140        150        160        170        180 
EPTTEMPLED TLGLPEAMFF MTDDLVAFDH AYQTVKIISH VCIQQGRPIE EAYEAAVFKI 

       190        200        210        220        230        240 
NMLKKKLESP EIPLPEQKKV HLGYEAKSNV GEDGYKAFVS NLKEHIFNGD IFQAVPSQRI 

       250        260        270        280        290        300 
ARRTDLHPFN LYRHLRTVNP SPYMFYIHCD DFDIIGASPE LLVKSEHGRI INHPIAGTVP 

       310        320        330        340        350        360 
RGKTKEEDEA YAKDLLASVK DRAEHVMLVD LARNDVSRVC DLDTTSVDKL MTIEKFSHVQ 

       370        380        390        400        410        420 
HLVSQVSGVL RPDKTRFDAF RSIFPAGTVS GSPKVRAIQL VYGLEKEKRG IYAGAVGRWG 

       430        440        450        460        470        480 
YEDDNMDTCI AIRTMVYKDG TVYLQAGGGI VFDSDEQDEY VETLNKLRSN VTAIEETEKL 


YAEEENSSA 

O94582 in FASTA format

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