ID   TRPE_SCHPO              Reviewed;         489 AA.
AC   O94582; P78905;
DT   16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   16-JUN-2009, entry version 54.
DE   RecName: Full=Probable anthranilate synthase component 1;
DE            EC=4.1.3.27;
DE   AltName: Full=Anthranilate synthase component I;
GN   Name=trp3; ORFNames=SPCC1442.09;
OS   Schizosaccharomyces pombe (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=4896;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 38366 / 972;
RX   MEDLINE=21848401; PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 126-489.
RC   STRAIN=PR745;
RX   MEDLINE=98162722; PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA   Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT   "Identification of open reading frames in Schizosaccharomyces pombe
RT   cDNAs.";
RL   DNA Res. 4:363-369(1997).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390; SER-392 AND
RP   SER-488, AND MASS SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
CC   -!- CATALYTIC ACTIVITY: Chorismate + L-glutamine = anthranilate +
CC       pyruvate + L-glutamate.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 1/5.
CC   -!- SUBUNIT: Tetramer of two components I and two components II (By
CC       similarity).
CC   -!- MISCELLANEOUS: Component I catalyzes the formation of anthranilate
CC       using ammonia rather than glutamine, whereas component II provides
CC       glutamine amidotransferase activity.
CC   -!- SIMILARITY: Belongs to the anthranilate synthase component I
CC       family.
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DR   EMBL; CU329672; CAA21443.1; -; Genomic_DNA.
DR   EMBL; D89256; BAA13917.1; -; mRNA.
DR   PIR; T40974; T40974.
DR   PIR; T43181; T43181.
DR   RefSeq; NP_588323.1; -.
DR   HSSP; P05041; 1K0E.
DR   GeneID; 2538842; -.
DR   KEGG; spo:SPCC1442.09; -.
DR   NMPDR; fig|4896.1.peg.661; -.
DR   GeneDB_Spombe; SPCC1442.09; -.
DR   OMA; O94582; RFSILAY.
DR   BioCyc; SPOM-XXX-01:SPOM-XXX-01-000246-MON; -.
DR   BRENDA; 4.1.3.27; 653.
DR   ArrayExpress; O94582; -.
DR   GO; GO:0005829; C:cytosol; IDA:GeneDB_SPombe.
DR   GO; GO:0005634; C:nucleus; IDA:GeneDB_SPombe.
DR   GO; GO:0004049; F:anthranilate synthase activity; IEA:EC.
DR   GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR005801; ADC_synthase.
DR   InterPro; IPR006805; Anth_synth_I_N.
DR   InterPro; IPR005256; Anth_synthI.
DR   InterPro; IPR019999; Anthranilate_synth_I_C.
DR   InterPro; IPR015890; Chorismate-bd_C.
DR   Gene3D; G3DSA:3.60.120.10; TRPE_1_chor_bd; 1.
DR   PANTHER; PTHR11236; TRPE_1_chor_bd; 1.
DR   Pfam; PF04715; Anth_synt_I_N; 1.
DR   Pfam; PF00425; Chorismate_bind; 1.
DR   PRINTS; PR00095; ANTSNTHASEI.
DR   ProDom; PD000779; Anth_synth_chor; 1.
DR   TIGRFAMs; TIGR00564; trpE_most; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Complete proteome; Lyase; Phosphoprotein; Tryptophan biosynthesis.
FT   CHAIN         1    489       Probable anthranilate synthase component
FT                                1.
FT                                /FTId=PRO_0000154133.
FT   MOD_RES     390    390       Phosphoserine.
FT   MOD_RES     392    392       Phosphoserine.
FT   MOD_RES     488    488       Phosphoserine.
FT   CONFLICT    144    144       D -> N (in Ref. 2; BAA13917).
FT   CONFLICT    156    156       K -> Q (in Ref. 2; BAA13917).
FT   CONFLICT    263    263       Y -> F (in Ref. 2; BAA13917).
FT   CONFLICT    305    305       K -> E (in Ref. 2; BAA13917).
FT   CONFLICT    320    320       K -> Q (in Ref. 2; BAA13917).
FT   CONFLICT    351    351       M -> R (in Ref. 2; BAA13917).
FT   CONFLICT    402    402       Y -> N (in Ref. 2; BAA13917).
FT   CONFLICT    411    411       I -> R (in Ref. 2; BAA13917).
SQ   SEQUENCE   489 AA;  54960 MW;  442D522BA59EBA31 CRC64;
     MKIYPDLKQV QELAEKHKAN KIPIYGVIPA DMLTPSVAYL KLNQGKKYSF ILESVTQGES
     VSRYSFIGSP YRILMANGKT DPLARLEREL KEVKTAPVEG LPSFSGGAVG YVSYDCIKYF
     EPTTEMPLED TLGLPEAMFF MTDDLVAFDH AYQTVKIISH VCIQQGRPIE EAYEAAVFKI
     NMLKKKLESP EIPLPEQKKV HLGYEAKSNV GEDGYKAFVS NLKEHIFNGD IFQAVPSQRI
     ARRTDLHPFN LYRHLRTVNP SPYMFYIHCD DFDIIGASPE LLVKSEHGRI INHPIAGTVP
     RGKTKEEDEA YAKDLLASVK DRAEHVMLVD LARNDVSRVC DLDTTSVDKL MTIEKFSHVQ
     HLVSQVSGVL RPDKTRFDAF RSIFPAGTVS GSPKVRAIQL VYGLEKEKRG IYAGAVGRWG
     YEDDNMDTCI AIRTMVYKDG TVYLQAGGGI VFDSDEQDEY VETLNKLRSN VTAIEETEKL
     YAEEENSSA
//