TRPG_SCHPO
ID TRPG_SCHPO Reviewed; 759 AA.
AC Q92370; Q9UUF5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 158.
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=trp1; ORFNames=SPBC1539.09c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=972 / ATCC 24843;
RA David C., Couzin N., Lauquin G.J.-M.;
RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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.
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DR EMBL; Y09137; CAA70348.1; -; mRNA.
DR EMBL; CU329671; CAB51341.1; -; Genomic_DNA.
DR PIR; T39468; T39468.
DR PIR; T46566; T46566.
DR RefSeq; NP_596823.1; NM_001023843.1.
DR AlphaFoldDB; Q92370; -.
DR SMR; Q92370; -.
DR BioGRID; 276517; 5.
DR STRING; 4896.SPBC1539.09c.1; -.
DR MEROPS; C26.A25; -.
DR iPTMnet; Q92370; -.
DR MaxQB; Q92370; -.
DR PaxDb; Q92370; -.
DR PRIDE; Q92370; -.
DR EnsemblFungi; SPBC1539.09c.1; SPBC1539.09c.1:pep; SPBC1539.09c.
DR GeneID; 2539973; -.
DR KEGG; spo:SPBC1539.09c; -.
DR PomBase; SPBC1539.09c; trp1.
DR VEuPathDB; FungiDB:SPBC1539.09c; -.
DR eggNOG; KOG0026; Eukaryota.
DR eggNOG; KOG4201; Eukaryota.
DR eggNOG; KOG4202; Eukaryota.
DR HOGENOM; CLU_007713_2_0_1; -.
DR InParanoid; Q92370; -.
DR OMA; CLEVSSW; -.
DR PhylomeDB; Q92370; -.
DR UniPathway; UPA00035; UER00040.
DR UniPathway; UPA00035; UER00042.
DR UniPathway; UPA00035; UER00043.
DR PRO; PR:Q92370; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005950; C:anthranilate synthase complex; ISO:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0004049; F:anthranilate synthase activity; IMP:PomBase.
DR GO; GO:0033984; F:indole-3-glycerol-phosphate lyase activity; IMP:PomBase.
DR GO; GO:0004425; F:indole-3-glycerol-phosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IMP:PomBase.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IMP:PomBase.
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_00134_B; IGPS_B; 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..759
FT /note="Multifunctional tryptophan biosynthesis protein"
FT /id="PRO_0000056865"
FT DOMAIN 27..223
FT /note="Glutamine amidotransferase type-1"
FT REGION 257..519
FT /note="Indole-3-glycerol phosphate synthase"
FT REGION 536..759
FT /note="N-(5'-phosphoribosyl)anthranilate isomerase"
FT ACT_SITE 108
FT /note="Nucleophile; for GATase activity"
FT /evidence="ECO:0000250|UniProtKB:P00900"
FT ACT_SITE 197
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 199
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT BINDING 80..82
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00900"
FT BINDING 112
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00900"
FT BINDING 158..159
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00900"
FT CONFLICT 387
FT /note="Q -> E (in Ref. 1; CAA70348)"
FT /evidence="ECO:0000305"
SQ 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
