TRPE_SCHPO
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 03-AUG-2022, entry version 134.
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 (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX 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., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA 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 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 SER-488, AND
RP IDENTIFICATION BY 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:
CC Reaction=chorismate + L-glutamine = anthranilate + H(+) + L-glutamate +
CC pyruvate; Xref=Rhea:RHEA:21732, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16567, ChEBI:CHEBI:29748, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:58359; EC=4.1.3.27;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P00897};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P00897};
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.
CC {ECO:0000250}.
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 family.
CC {ECO:0000305}.
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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; NM_001023314.2.
DR AlphaFoldDB; O94582; -.
DR SMR; O94582; -.
DR BioGRID; 275423; 4.
DR STRING; 4896.SPCC1442.09.1; -.
DR iPTMnet; O94582; -.
DR MaxQB; O94582; -.
DR PaxDb; O94582; -.
DR PRIDE; O94582; -.
DR EnsemblFungi; SPCC1442.09.1; SPCC1442.09.1:pep; SPCC1442.09.
DR GeneID; 2538842; -.
DR KEGG; spo:SPCC1442.09; -.
DR PomBase; SPCC1442.09; trp3.
DR VEuPathDB; FungiDB:SPCC1442.09; -.
DR eggNOG; KOG1223; Eukaryota.
DR HOGENOM; CLU_006493_9_3_1; -.
DR InParanoid; O94582; -.
DR OMA; GCVGYLD; -.
DR PhylomeDB; O94582; -.
DR UniPathway; UPA00035; UER00040.
DR PRO; PR:O94582; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005950; C:anthranilate synthase complex; ISO:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0004049; F:anthranilate synthase activity; ISO:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000162; P:tryptophan biosynthetic process; EXP:PomBase.
DR Gene3D; 3.60.120.10; -; 1.
DR InterPro; IPR005801; ADC_synthase.
DR InterPro; IPR019999; Anth_synth_I-like.
DR InterPro; IPR006805; Anth_synth_I_N.
DR InterPro; IPR005256; Anth_synth_I_PabB.
DR InterPro; IPR015890; Chorismate_C.
DR PANTHER; PTHR11236; PTHR11236; 1.
DR Pfam; PF04715; Anth_synt_I_N; 1.
DR Pfam; PF00425; Chorismate_bind; 1.
DR PRINTS; PR00095; ANTSNTHASEI.
DR SUPFAM; SSF56322; SSF56322; 1.
DR TIGRFAMs; TIGR00564; trpE_most; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW Magnesium; Metal-binding; Phosphoprotein; Reference proteome;
KW Tryptophan biosynthesis.
FT CHAIN 1..489
FT /note="Probable anthranilate synthase component 1"
FT /id="PRO_0000154133"
FT BINDING 54
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 262..264
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 297..298
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 324
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 412
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 433
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 447..449
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 449
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT BINDING 462
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00897"
FT MOD_RES 390
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 392
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 488
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 144
FT /note="D -> N (in Ref. 2; BAA13917)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="K -> Q (in Ref. 2; BAA13917)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="Y -> F (in Ref. 2; BAA13917)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="K -> E (in Ref. 2; BAA13917)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="K -> Q (in Ref. 2; BAA13917)"
FT /evidence="ECO:0000305"
FT CONFLICT 351
FT /note="M -> R (in Ref. 2; BAA13917)"
FT /evidence="ECO:0000305"
FT CONFLICT 402
FT /note="Y -> N (in Ref. 2; BAA13917)"
FT /evidence="ECO:0000305"
FT CONFLICT 411
FT /note="I -> R (in Ref. 2; BAA13917)"
FT /evidence="ECO:0000305"
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
