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Multifunctional tryptophan biosynthesis protein [Includes: Anthranilate synthase component 2 (AS) (EC 4.1.3.27) (Anthranilate synthase, glutamine amidotransferase component); Indole-3-glycerol phosphate synthase (IGPS) (EC 4.1.1.48); N-(5'-phosphoribosyl)anthranilate isomerase (PRAI) (EC 5.3.1.24)]

 TRPG_EMENI              Reviewed;         768 AA.
P06531; C8VS06; Q5BFN2; Q92224;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
19-OCT-2011, sequence version 3.
23-MAY-2018, entry version 146.
RecName: Full=Multifunctional tryptophan biosynthesis protein;
Includes:
RecName: Full=Anthranilate synthase component 2;
Short=AS;
EC=4.1.3.27;
AltName: Full=Anthranilate synthase, glutamine amidotransferase component;
Includes:
RecName: Full=Indole-3-glycerol phosphate synthase;
Short=IGPS;
EC=4.1.1.48;
Includes:
RecName: Full=N-(5'-phosphoribosyl)anthranilate isomerase;
Short=PRAI;
EC=5.3.1.24;
Name=trpC; ORFNames=AN0648;
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL
194 / M139) (Aspergillus nidulans).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
NCBI_TaxID=227321;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2836085; DOI=10.1007/BF00365648;
Kos T., Kuijvenhoven A., Hessing H.G.M., Pouwels P.H.,
van den Hondel C.A.M.J.J.;
"Nucleotide sequence of the Aspergillus niger trpC gene: structural
relationship with analogous genes of other organisms.";
Curr. Genet. 13:137-144(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3158796; DOI=10.1007/BF00327506;
Mullaney E.J., Hamer J.E., Roberti K.A., Yelton M.M., Timberlake W.E.;
"Primary structure of the trpC gene from Aspergillus nidulans.";
Mol. Gen. Genet. 199:37-45(1985).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 7-768.
STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
PubMed=16372000; DOI=10.1038/nature04341;
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R.,
Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J.,
Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J.,
Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
"Sequencing of Aspergillus nidulans and comparative analysis with A.
fumigatus and A. oryzae.";
Nature 438:1105-1115(2005).
[4]
GENOME REANNOTATION.
STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P.,
von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E.,
Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G.,
de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K.,
Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S.,
Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E.,
Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A.,
Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P.,
Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R.,
Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I.,
Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B.,
van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N.,
Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J.,
de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W.,
Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.;
"The 2008 update of the Aspergillus nidulans genome annotation: a
community effort.";
Fungal Genet. Biol. 46:S2-13(2009).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 377-410.
PubMed=6324178; DOI=10.1073/pnas.80.24.7576;
Yelton M.M., Hamer J.E., de Souza E.R., Mullaney E.J.,
Timberlake W.E.;
"Developmental regulation of the Aspergillus nidulans trpC gene.";
Proc. Natl. Acad. Sci. U.S.A. 80:7576-7580(1983).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 719-768.
Genser K.F.;
Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Trifunctional enzyme bearing the Gln amidotransferase
(GATase) domain of anthranilate synthase, indole-glycerolphosphate
synthase, and phosphoribosylanthranilate isomerase activities.
-!- CATALYTIC ACTIVITY: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-
(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate.
-!- CATALYTIC ACTIVITY: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-
phosphate = 1-C-(3-indolyl)-glycerol 3-phosphate + CO(2) + H(2)O.
-!- CATALYTIC ACTIVITY: Chorismate + L-glutamine = anthranilate +
pyruvate + L-glutamate.
-!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
tryptophan from chorismate: step 1/5.
-!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
tryptophan from chorismate: step 3/5.
-!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
tryptophan from chorismate: step 4/5.
-!- INDUCTION: By tryptophan starvation.
-!- SEQUENCE CAUTION:
Sequence=CBF89063.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=EAA65153.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; X02390; CAA26232.1; -; Genomic_DNA.
EMBL; AACD01000009; EAA65153.1; ALT_SEQ; Genomic_DNA.
EMBL; U24705; AAB60292.1; -; Genomic_DNA.
EMBL; BN001308; CBF89063.1; ALT_INIT; Genomic_DNA.
PIR; S04518; S04518.
PIR; S07305; S07305.
RefSeq; XP_658252.1; XM_653160.1.
ProteinModelPortal; P06531; -.
SMR; P06531; -.
STRING; 162425.CADANIAP00002028; -.
MEROPS; C26.959; -.
PRIDE; P06531; -.
EnsemblFungi; CADANIAT00002028; CADANIAP00002028; CADANIAG00002028.
EnsemblFungi; EAA65153; EAA65153; AN0648.2.
GeneID; 2876427; -.
KEGG; ani:AN0648.2; -.
HOGENOM; HOG000280459; -.
InParanoid; P06531; -.
OrthoDB; EOG092C1PKC; -.
UniPathway; UPA00035; UER00040.
UniPathway; UPA00035; UER00042.
UniPathway; UPA00035; UER00043.
Proteomes; UP000000560; Chromosome VIII.
Proteomes; UP000005890; Unassembled WGS sequence.
GO; GO:0005950; C:anthranilate synthase complex; IBA:GO_Central.
GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-EC.
GO; GO:0004425; F:indole-3-glycerol-phosphate synthase activity; IEA:UniProtKB-EC.
GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IEA:UniProtKB-EC.
GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central.
CDD; cd00331; IGPS; 1.
CDD; cd00405; PRAI; 1.
Gene3D; 3.20.20.70; -; 3.
Gene3D; 3.40.50.880; -; 1.
HAMAP; MF_00135; PRAI; 1.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR016302; Anthranilate_synth_II.
InterPro; IPR029062; Class_I_gatase-like.
InterPro; IPR017926; GATASE.
InterPro; IPR013798; Indole-3-glycerol_P_synth.
InterPro; IPR001468; Indole-3-GlycerolPSynthase_CS.
InterPro; IPR001240; PRAI.
InterPro; IPR011060; RibuloseP-bd_barrel.
InterPro; IPR006221; TrpG/PapA_dom.
Pfam; PF00117; GATase; 1.
Pfam; PF00218; IGPS; 1.
Pfam; PF00697; PRAI; 1.
PIRSF; PIRSF001382; TrpG-trpC-trpF; 1.
SUPFAM; SSF51366; SSF51366; 3.
SUPFAM; SSF52317; SSF52317; 1.
TIGRFAMs; TIGR00566; trpG_papA; 1.
PROSITE; PS51273; GATASE_TYPE_1; 1.
PROSITE; PS00614; IGPS; 1.
2: Evidence at transcript level;
Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
Complete proteome; Decarboxylase; Glutamine amidotransferase;
Isomerase; Lyase; Multifunctional enzyme; Reference proteome;
Tryptophan biosynthesis.
CHAIN 1 768 Multifunctional tryptophan biosynthesis
protein.
/FTId=PRO_0000056859.
DOMAIN 25 225 Glutamine amidotransferase type-1.
REGION 76 78 Glutamine binding.
{ECO:0000250|UniProtKB:P00900}.
REGION 154 155 Glutamine binding.
{ECO:0000250|UniProtKB:P00900}.
REGION 252 516 Indole-3-glycerol phosphate synthase.
REGION 532 768 N-(5'-phosphoribosyl)anthranilate
isomerase.
ACT_SITE 104 104 Nucleophile; for GATase activity.
{ECO:0000250|UniProtKB:P00900}.
ACT_SITE 199 199 For GATase activity. {ECO:0000250}.
ACT_SITE 201 201 For GATase activity. {ECO:0000250}.
BINDING 108 108 Glutamine.
{ECO:0000250|UniProtKB:P00900}.
CONFLICT 111 111 I -> H (in Ref. 2; CAA26232).
{ECO:0000305}.
CONFLICT 249 249 K -> Q (in Ref. 2; CAA26232).
{ECO:0000305}.
CONFLICT 396 398 VLL -> SYV (in Ref. 2; CAA26232 and 5).
{ECO:0000305}.
CONFLICT 410 415 RLYLYS -> QTLSLF (in Ref. 2; CAA26232).
{ECO:0000305}.
CONFLICT 410 410 R -> Q (in Ref. 5). {ECO:0000305}.
CONFLICT 473 482 VCALSGISGP -> RLCTMRYFWT (in Ref. 2;
CAA26232). {ECO:0000305}.
CONFLICT 681 681 L -> V (in Ref. 2; CAA26232).
{ECO:0000305}.
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


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