ID   TRPG_NEUCR              Reviewed;         762 AA.
AC   P00908; Q7RV57; U9W354;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   31-AUG-2004, sequence version 2.
DT   24-JAN-2024, entry version 175.
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=trp-1; Synonyms=trpg-trpc-trpf, tryp-1; ORFNames=NCU00200;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6221060;
RA   Schechtman M.G., Yanofsky C.;
RT   "Structure of the trifunctional trp-1 gene from Neurospora crassa and its
RT   aberrant expression in Escherichia coli.";
RL   J. Mol. Appl. Genet. 2:83-99(1983).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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=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   -!- 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   -!- 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.
CC   -!- SUBUNIT: Tetramer of two components I and two components II.
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DR   EMBL; J01252; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CM002238; ESA43300.1; -; Genomic_DNA.
DR   EMBL; CM002238; ESA43301.1; -; Genomic_DNA.
DR   PIR; A01130; NNNC2.
DR   RefSeq; XP_011393782.1; XM_011395480.1.
DR   RefSeq; XP_011393783.1; XM_011395481.1.
DR   AlphaFoldDB; P00908; -.
DR   SMR; P00908; -.
DR   STRING; 367110.P00908; -.
DR   PaxDb; 5141-EFNCRP00000000483; -.
DR   EnsemblFungi; ESA43300; ESA43300; NCU00200.
DR   EnsemblFungi; ESA43301; ESA43301; NCU00200.
DR   GeneID; 3872732; -.
DR   KEGG; ncr:NCU00200; -.
DR   VEuPathDB; FungiDB:NCU00200; -.
DR   HOGENOM; CLU_007713_2_0_1; -.
DR   InParanoid; P00908; -.
DR   OrthoDB; 294181at2759; -.
DR   UniPathway; UPA00035; UER00040.
DR   UniPathway; UPA00035; UER00042.
DR   UniPathway; UPA00035; UER00043.
DR   Proteomes; UP000001805; Chromosome 3, Linkage Group III.
DR   GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004425; F:indole-3-glycerol-phosphate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central.
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_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; 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; PTHR43418:SF4; MULTIFUNCTIONAL TRYPTOPHAN BIOSYNTHESIS PROTEIN; 1.
DR   PANTHER; PTHR43418; MULTIFUNCTIONAL TRYPTOPHAN BIOSYNTHESIS PROTEIN-RELATED; 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   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Decarboxylase;
KW   Glutamine amidotransferase; Isomerase; Lyase; Multifunctional enzyme;
KW   Reference proteome; Tryptophan biosynthesis.
FT   CHAIN           1..762
FT                   /note="Multifunctional tryptophan biosynthesis protein"
FT                   /id="PRO_0000056861"
FT   DOMAIN          25..224
FT                   /note="Glutamine amidotransferase type-1"
FT   REGION          251..515
FT                   /note="Indole-3-glycerol phosphate synthase"
FT   REGION          531..762
FT                   /note="N-(5'-phosphoribosyl)anthranilate isomerase"
FT   ACT_SITE        104
FT                   /note="Nucleophile; for GATase activity"
FT                   /evidence="ECO:0000250|UniProtKB:P00900"
FT   ACT_SITE        198
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        200
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000250"
FT   BINDING         76..78
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000250|UniProtKB:P00900"
FT   BINDING         108
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000250|UniProtKB:P00900"
FT   BINDING         154..155
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000250|UniProtKB:P00900"
FT   CONFLICT        337
FT                   /note="A -> G (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        511
FT                   /note="I -> V (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        523
FT                   /note="P -> S (in Ref. 1)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   762 AA;  82559 MW;  C058B21FF4B7C5BB CRC64;
     MSSSSVVDHS PHDSAPSPLV PTASNLILID NYDSFTWNVY QYLVLEGAKV TVFRNDQITI
     DELIAKNPTQ LVISPGPGHP GTDSGISRDA IRHFAGKIPI FGVCMGQQCI FDVYGGDVCF
     AGEILHGKTS PLRHDGKGAY AGLSQDLPVT RYHSLAGTHV TLPECLEVTS WIAKEDGSKG
     VIMGVRHKEY TIEGVQFHPE SILSAEGRGM FRNFLHMQGG TWAENERLQK AAQAQAANTK
     SDAPTPKKSN ILQKIYAHRK AAVDAQKQIP SLRPSDLQAA YNLSIAPPQI SLVDRLRNSP
     FDVALCAEIK RASPSKGVFA LDIDAPSQAR KYALAGASVI SVLTEPEWFK GSIDDLRAVR
     QVLNGMPNRP AVLRKEFIFD EYQILEARLA GADTVLLIVK MLEYELLERL YKYSLSLGME
     PLVEVQNTEE MATAIKLGAK VIGVNNRNLE SFEVDLGTTG RLRSMVPSDT FLCALSGINT
     HQDVLDCKRD GVNGILVGEA IMRAPDATQF IRELCAGLTG PVPKSAAEPL LVKICGTRSA
     EAAAEAIKAG ADLVGMIMVP GTKRCVDHET ALSISQAVHM SKKTGSTEVS SQASKSARDF
     FNINAEIIRK RGPLLVGVFM NQPLEEVLEK QHLYDLDIVQ LHGDEPLEWA NLIPVPVVRK
     FKPGQVGLAT RGYHAVPLLD SGAGSGTLLD LESVKKELEK DEQVTVLLAG GLEPSNVVET
     VKSLGPLSER VIGVDVSSGV EEGGKQSLEK IREFVKAAKS VR
//