TRPG_NEUCR
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 03-AUG-2022, entry version 170.
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; 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 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; 3.20.20.70; -; 2.
DR Gene3D; 3.40.50.880; -; 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; 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 Pfam; PF00117; GATase; 1.
DR Pfam; PF00218; IGPS; 1.
DR Pfam; PF00697; PRAI; 1.
DR PIRSF; PIRSF001382; TrpG-trpC-trpF; 1.
DR SUPFAM; SSF51366; SSF51366; 2.
DR SUPFAM; SSF52317; SSF52317; 1.
DR TIGRFAMs; TIGR00566; trpG_papA; 1.
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
