ID   TRPG_SCHPO              Reviewed;         759 AA.
AC   Q92370; Q9UUF5;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 2.
DT   27-MAR-2024, entry version 165.
DE   RecName: Full=Multifunctional tryptophan biosynthesis protein;
DE   Includes:
DE     RecName: Full=Anthranilate synthase component 2;
DE              Short=AS;
DE              EC=4.1.3.27;
DE     AltName: Full=Anthranilate synthase, glutamine amidotransferase component;
DE   Includes:
DE     RecName: Full=Indole-3-glycerol phosphate synthase;
DE              Short=IGPS;
DE              EC=4.1.1.48;
DE   Includes:
DE     RecName: Full=N-(5'-phosphoribosyl)anthranilate isomerase;
DE              Short=PRAI;
DE              EC=5.3.1.24;
GN   Name=trp1; ORFNames=SPBC1539.09c;
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 [MRNA].
RC   STRAIN=972 / ATCC 24843;
RA   David C., Couzin N., Lauquin G.J.-M.;
RL   Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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).
CC   -!- FUNCTION: Trifunctional enzyme bearing the Gln amidotransferase
CC       (GATase) domain of anthranilate synthase, indole-glycerolphosphate
CC       synthase, and phosphoribosylanthranilate isomerase activities.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-
CC         carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate;
CC         Xref=Rhea:RHEA:21540, ChEBI:CHEBI:18277, ChEBI:CHEBI:58613;
CC         EC=5.3.1.24;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+)
CC         = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O;
CC         Xref=Rhea:RHEA:23476, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:58613, ChEBI:CHEBI:58866; EC=4.1.1.48;
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   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 1/5.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 3/5.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 4/5.
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DR   EMBL; Y09137; CAA70348.1; -; mRNA.
DR   EMBL; CU329671; CAB51341.1; -; Genomic_DNA.
DR   PIR; T39468; T39468.
DR   PIR; T46566; T46566.
DR   RefSeq; NP_596823.1; NM_001023843.1.
DR   AlphaFoldDB; Q92370; -.
DR   SMR; Q92370; -.
DR   BioGRID; 276517; 5.
DR   STRING; 284812.Q92370; -.
DR   MEROPS; C26.A25; -.
DR   iPTMnet; Q92370; -.
DR   MaxQB; Q92370; -.
DR   PaxDb; 4896-SPBC1539-09c-1; -.
DR   EnsemblFungi; SPBC1539.09c.1; SPBC1539.09c.1:pep; SPBC1539.09c.
DR   GeneID; 2539973; -.
DR   KEGG; spo:SPBC1539.09c; -.
DR   PomBase; SPBC1539.09c; trp1.
DR   VEuPathDB; FungiDB:SPBC1539.09c; -.
DR   eggNOG; KOG0026; Eukaryota.
DR   eggNOG; KOG4201; Eukaryota.
DR   eggNOG; KOG4202; Eukaryota.
DR   HOGENOM; CLU_007713_2_0_1; -.
DR   InParanoid; Q92370; -.
DR   OMA; EPIEWAN; -.
DR   PhylomeDB; Q92370; -.
DR   UniPathway; UPA00035; UER00040.
DR   UniPathway; UPA00035; UER00042.
DR   UniPathway; UPA00035; UER00043.
DR   PRO; PR:Q92370; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005950; C:anthranilate synthase complex; ISO:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0004049; F:anthranilate synthase activity; IMP:PomBase.
DR   GO; GO:0033984; F:indole-3-glycerol-phosphate lyase activity; IMP:PomBase.
DR   GO; GO:0004425; F:indole-3-glycerol-phosphate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IMP:PomBase.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0000162; P:tryptophan biosynthetic process; IMP:PomBase.
DR   CDD; cd01743; GATase1_Anthranilate_Synthase; 1.
DR   CDD; cd00331; IGPS; 1.
DR   CDD; cd00405; PRAI; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 2.
DR   HAMAP; MF_00134_B; IGPS_B; 1.
DR   HAMAP; MF_00135; PRAI; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR016302; Anthranilate_synth_II.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR017926; GATASE.
DR   InterPro; IPR045186; Indole-3-glycerol_P_synth.
DR   InterPro; IPR013798; Indole-3-glycerol_P_synth_dom.
DR   InterPro; IPR001468; Indole-3-GlycerolPSynthase_CS.
DR   InterPro; IPR001240; PRAI_dom.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   InterPro; IPR006221; TrpG/PapA_dom.
DR   NCBIfam; TIGR00566; trpG_papA; 1.
DR   PANTHER; PTHR22854:SF2; INDOLE-3-GLYCEROL-PHOSPHATE SYNTHASE; 1.
DR   PANTHER; PTHR22854; TRYPTOPHAN BIOSYNTHESIS PROTEIN; 1.
DR   Pfam; PF00117; GATase; 1.
DR   Pfam; PF00218; IGPS; 1.
DR   Pfam; PF00697; PRAI; 1.
DR   PIRSF; PIRSF001382; TrpG-trpC-trpF; 1.
DR   PRINTS; PR00097; ANTSNTHASEII.
DR   PRINTS; PR00096; GATASE.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 2.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
DR   PROSITE; PS00614; IGPS; 1.
PE   2: Evidence at transcript level;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Decarboxylase;
KW   Glutamine amidotransferase; Isomerase; Lyase; Multifunctional enzyme;
KW   Reference proteome; Tryptophan biosynthesis.
FT   CHAIN           1..759
FT                   /note="Multifunctional tryptophan biosynthesis protein"
FT                   /id="PRO_0000056865"
FT   DOMAIN          27..223
FT                   /note="Glutamine amidotransferase type-1"
FT   REGION          257..519
FT                   /note="Indole-3-glycerol phosphate synthase"
FT   REGION          536..759
FT                   /note="N-(5'-phosphoribosyl)anthranilate isomerase"
FT   ACT_SITE        108
FT                   /note="Nucleophile; for GATase activity"
FT                   /evidence="ECO:0000250|UniProtKB:P00900"
FT   ACT_SITE        197
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        199
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000250"
FT   BINDING         80..82
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000250|UniProtKB:P00900"
FT   BINDING         112
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000250|UniProtKB:P00900"
FT   BINDING         158..159
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000250|UniProtKB:P00900"
FT   CONFLICT        387
FT                   /note="Q -> E (in Ref. 1; CAA70348)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   759 AA;  83040 MW;  519E2EA55CB9B212 CRC64;
     MSEKVDVGES VKGDASENAV KEVAERPIVM IDNYDSFTWN VVQYLSNLEK RYPIMVFRND
     EITVDELEKL NPLKLVLSPG PGHPARDGGI CNEAISRFAG KIPILGVCMG LQCIFETMGG
     KVDSAGEIIH GKVSKINHDG LGFYQGIPQN ISVTRYHSLA GKISSLPDCL DVTSWTENGV
     IMGARHKKYA IEGVQYHPES ILSEYGKEYI QNFLNLTAGT WEENGIVMPT KNNAFNAAMR
     ENSNSVSSTK IRKQESILEK IHAQRLIDIA ESKRKPGLSV GDLQTYLNLN IAPPCINFYE
     RLKQSKPALM AEVKRASPSK GDIKLDANAA IQALTYAQVG ASVISVLTEP KWFKGSLNDL
     FVARKAVEHV ANRPAILRKD FIIDPYQIME ARLNGADSVL LIVAMLSREQ LESLYKFSKS
     LGMEPLVEVN CAEEMKTAIE LGAKVIGVNN RNLHSFEVDL STTSKLAEMV PDDVILAALS
     GISSPADVAH YSSQGVSAVL VGESLMRASD PAAFARELLN LSSSEISNGK KTSTPLVKVC
     GTRSLLAAKT IVESGGDLIG LIFVEKSKRK VDLSVAKEIS HFVHTTNRKH ISPKKAVTGQ
     SWFDHQYENL ASSPHPLLVG VFQNQPLEYI RSIIAEVNLD IVQLHGQEPF EWIHMLDRPV
     IKVFPLNSSE ISRPNYHIVP LIDAYVGGES GGLGKKVDWE AASFIPVSYV LAGGLTPKNV
     QDAISVSRPA VVDVSSGVET DGKQDLEKIK AFINAVKEL
//