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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_SCHPO              Reviewed;         759 AA.
Q92370; Q9UUF5;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
27-APR-2001, sequence version 2.
25-APR-2018, entry version 140.
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=trp1; ORFNames=SPBC1539.09c;
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
Schizosaccharomycetes; Schizosaccharomycetales;
Schizosaccharomycetaceae; Schizosaccharomyces.
NCBI_TaxID=284812;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=972 / ATCC 24843;
David C., Couzin N., Lauquin G.J.-M.;
Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=972 / ATCC 24843;
PubMed=11859360; DOI=10.1038/nature724;
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
-!- 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.
-----------------------------------------------------------------------
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EMBL; Y09137; CAA70348.1; -; mRNA.
EMBL; CU329671; CAB51341.1; -; Genomic_DNA.
PIR; T39468; T39468.
PIR; T46566; T46566.
RefSeq; NP_596823.1; NM_001023843.1.
ProteinModelPortal; Q92370; -.
SMR; Q92370; -.
BioGrid; 276517; 2.
STRING; 4896.SPBC1539.09c.1; -.
MEROPS; C26.A25; -.
iPTMnet; Q92370; -.
MaxQB; Q92370; -.
PaxDb; Q92370; -.
PRIDE; Q92370; -.
EnsemblFungi; SPBC1539.09c.1; SPBC1539.09c.1:pep; SPBC1539.09c.
GeneID; 2539973; -.
KEGG; spo:SPBC1539.09c; -.
EuPathDB; FungiDB:SPBC1539.09c; -.
PomBase; SPBC1539.09c; trp1.
HOGENOM; HOG000280459; -.
InParanoid; Q92370; -.
KO; K13501; -.
OMA; WFKGSIE; -.
OrthoDB; EOG092C1PKC; -.
PhylomeDB; Q92370; -.
UniPathway; UPA00035; UER00040.
UniPathway; UPA00035; UER00042.
UniPathway; UPA00035; UER00043.
PRO; PR:Q92370; -.
Proteomes; UP000002485; Chromosome II.
GO; GO:0005950; C:anthranilate synthase complex; ISO:PomBase.
GO; GO:0005829; C:cytosol; HDA:PomBase.
GO; GO:0004049; F:anthranilate synthase activity; IMP:PomBase.
GO; GO:0033984; F:indole-3-glycerol-phosphate lyase activity; IMP:PomBase.
GO; GO:0004425; F:indole-3-glycerol-phosphate synthase activity; IEA:UniProtKB-EC.
GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IMP:PomBase.
GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
GO; GO:0000162; P:tryptophan biosynthetic process; IMP:PomBase.
CDD; cd00331; IGPS; 1.
CDD; cd00405; PRAI; 1.
Gene3D; 3.20.20.70; -; 2.
Gene3D; 3.40.50.880; -; 1.
HAMAP; MF_00134_B; IGPS_B; 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 1 759 Multifunctional tryptophan biosynthesis
protein.
/FTId=PRO_0000056865.
DOMAIN 27 223 Glutamine amidotransferase type-1.
REGION 80 82 Glutamine binding.
{ECO:0000250|UniProtKB:P00900}.
REGION 158 159 Glutamine binding.
{ECO:0000250|UniProtKB:P00900}.
REGION 257 519 Indole-3-glycerol phosphate synthase.
REGION 536 759 N-(5'-phosphoribosyl)anthranilate
isomerase.
ACT_SITE 108 108 Nucleophile; for GATase activity.
{ECO:0000250|UniProtKB:P00900}.
ACT_SITE 197 197 For GATase activity. {ECO:0000250}.
ACT_SITE 199 199 For GATase activity. {ECO:0000250}.
BINDING 112 112 Glutamine.
{ECO:0000250|UniProtKB:P00900}.
CONFLICT 387 387 Q -> E (in Ref. 1; CAA70348).
{ECO:0000305}.
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


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