TRPG_EMENI
ID TRPG_EMENI Reviewed; 768 AA.
AC P06531; C8VS06; Q5BFN2; Q92224;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 3.
DT 03-AUG-2022, entry version 166.
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=trpC; ORFNames=AN0648;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2836085; DOI=10.1007/bf00365648;
RA Kos T., Kuijvenhoven A., Hessing H.G.M., Pouwels P.H.,
RA van den Hondel C.A.M.J.J.;
RT "Nucleotide sequence of the Aspergillus niger trpC gene: structural
RT relationship with analogous genes of other organisms.";
RL Curr. Genet. 13:137-144(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3158796; DOI=10.1007/bf00327506;
RA Mullaney E.J., Hamer J.E., Roberti K.A., Yelton M.M., Timberlake W.E.;
RT "Primary structure of the trpC gene from Aspergillus nidulans.";
RL Mol. Gen. Genet. 199:37-45(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 7-768.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 377-410.
RX PubMed=6324178; DOI=10.1073/pnas.80.24.7576;
RA Yelton M.M., Hamer J.E., de Souza E.R., Mullaney E.J., Timberlake W.E.;
RT "Developmental regulation of the Aspergillus nidulans trpC gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:7576-7580(1983).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 719-768.
RA Genser K.F.;
RL Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
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.
CC -!- INDUCTION: By tryptophan starvation.
CC -!- SEQUENCE CAUTION:
CC Sequence=CBF89063.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=EAA65153.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X02390; CAA26232.1; -; Genomic_DNA.
DR EMBL; AACD01000009; EAA65153.1; ALT_SEQ; Genomic_DNA.
DR EMBL; U24705; AAB60292.1; -; Genomic_DNA.
DR EMBL; BN001308; CBF89063.1; ALT_INIT; Genomic_DNA.
DR PIR; S04518; S04518.
DR PIR; S07305; S07305.
DR RefSeq; XP_658252.1; XM_653160.1.
DR AlphaFoldDB; P06531; -.
DR SMR; P06531; -.
DR STRING; 162425.CADANIAP00002028; -.
DR MEROPS; C26.959; -.
DR EnsemblFungi; EAA65153; EAA65153; AN0648.2.
DR GeneID; 2876427; -.
DR KEGG; ani:AN0648.2; -.
DR eggNOG; KOG0026; Eukaryota.
DR eggNOG; KOG4201; Eukaryota.
DR eggNOG; KOG4202; Eukaryota.
DR HOGENOM; CLU_3106319_0_0_1; -.
DR InParanoid; P06531; -.
DR OrthoDB; 535224at2759; -.
DR UniPathway; UPA00035; UER00040.
DR UniPathway; UPA00035; UER00042.
DR UniPathway; UPA00035; UER00043.
DR Proteomes; UP000000560; Chromosome VIII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
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 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..768
FT /note="Multifunctional tryptophan biosynthesis protein"
FT /id="PRO_0000056859"
FT DOMAIN 25..225
FT /note="Glutamine amidotransferase type-1"
FT REGION 252..516
FT /note="Indole-3-glycerol phosphate synthase"
FT REGION 532..768
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 199
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 201
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 111
FT /note="I -> H (in Ref. 2; CAA26232)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="K -> Q (in Ref. 2; CAA26232)"
FT /evidence="ECO:0000305"
FT CONFLICT 396..398
FT /note="VLL -> SYV (in Ref. 2; CAA26232 and 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 410..415
FT /note="RLYLYS -> QTLSLF (in Ref. 2; CAA26232)"
FT /evidence="ECO:0000305"
FT CONFLICT 410
FT /note="R -> Q (in Ref. 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 473..482
FT /note="VCALSGISGP -> RLCTMRYFWT (in Ref. 2; CAA26232)"
FT /evidence="ECO:0000305"
FT CONFLICT 681
FT /note="L -> V (in Ref. 2; CAA26232)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 768 AA; 83127 MW; FEFE1374DF86151D CRC64;
MADTALVDHS PHHPTKAPRL ETASNVILID NYDSFTWNVY QYLVLEGATV TVIRNDEISL
EELIAKKPTQ LVVSPGPGHP KSDAGISNAA IQYFAGKIPI FGVCMGQQCI IHSFGGKVDV
TGEILHGKTS VLKHDGRGAY EGLPPSVIIT RYHSLAGTHS TIPECLEVSS FAQLGEDADK
TVIMGVRHKQ FAVEGVQFHP ESILTEHGQT MFRNFLKLTA GTWEGNGKDV AQGGNFTAAA
PNPPKATKKV SILEKIYDHR RAAVAKQKTI PSQRPSDLQA AYELSVAPPQ ISFPDRLRQS
AYPLSLMAEI KRASPSKGLI AEHACAPAQA RQYAKAGASV ISVLTEPEWF KGSIDDLRAV
RASLEGLTNR PAILRKEFIF DEYQILEARL AGADTVLLIV KMLDTELLTR LYLYSQSLGM
EPLVEVNTPD EMKIAVDLGA QVIGVNNRDL TSFEVDLGTT SRLMDQVPES TIVCALSGIS
GPKDVEAYKK DGVKAILVGE ALMRAPDTAA FVAELLGGQS KKLPLQSRNS PLVKICGTRT
EEGARAAIEA GADLIGIILV EGRKRTVPDD VALQISKVVK STPRPTPYPT EVPQGDTDAT
SVDYFDHSAT TLRHPTRALL VGVFLNQPLS YVLAQQQKLG LDVVQLHGSE PLEWSRLIPV
PVIRKFGLDE FGIARRAYHT LPLLDSGAGG SGELLDQMRV KQILKSDDGL RVILAGGLDP
LNVTEIIKQL DESGYKIVGV DVSSGVETNG VQDLDKIRSF VQAAKSAF
