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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 (EC 4.1.1.48) (PRAI)]

 TRPG_YEAST              Reviewed;         484 AA.
P00937; D6VWZ2;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 2.
18-JUL-2018, entry version 183.
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;
EC=4.1.1.48;
AltName: Full=PRAI;
Name=TRP3; OrderedLocusNames=YKL211C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6323449;
Zalkin H., Paluh J.L., van Cleemput M., Moye W.S., Yanofsky C.;
"Nucleotide sequence of Saccharomyces cerevisiae genes TRP2 and TRP3
encoding bifunctional anthranilate synthase: indole-3-glycerol
phosphate synthase.";
J. Biol. Chem. 259:3985-3992(1984).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=7941750; DOI=10.1002/yea.320100511;
Tzermia M., Horaitis O., Alexandraki D.;
"The complete sequencing of a 24.6 kb segment of yeast chromosome XI
identified the known loci URA1, SAC1 and TRP3, and revealed 6 new open
reading frames including homologues to the threonine dehydratases,
membrane transporters, hydantoinases and the phospholipase A2-
activating protein.";
Yeast 10:663-679(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8196765; DOI=10.1038/369371a0;
Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M.,
Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C.,
Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G.,
Zimmermann J., Haasemann M., Becker I., Mewes H.-W.;
"Complete DNA sequence of yeast chromosome XI.";
Nature 369:371-378(1994).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-280.
Aebi M., Furter R., Prantl F., Niederberger P., Huetter R.;
"Structure and function of the TRP3 gene of Saccharomyces cerevisiae:
analysis of transcription, promoter sequence, and sequence coding for
a glutamine amidotransferase.";
Curr. Genet. 8:165-172(1984).
[6]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
-!- CATALYTIC ACTIVITY: Chorismate + L-glutamine = anthranilate +
pyruvate + L-glutamate.
-!- CATALYTIC ACTIVITY: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-
phosphate = 1-C-(3-indolyl)-glycerol 3-phosphate + CO(2) + H(2)O.
-!- 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 4/5.
-!- SUBUNIT: Tetramer of two components I and two components II.
-!- INTERACTION:
P00899:TRP2; NbExp=6; IntAct=EBI-19585, EBI-19575;
-!- INDUCTION: By tryptophan starvation.
-!- MISCELLANEOUS: Component I catalyzes the formation of anthranilate
using ammonia rather than glutamine, whereas component II provides
glutamine amidotransferase activity.
-!- MISCELLANEOUS: Yeast component II C-terminal half also has indole-
3-glycerol phosphate synthase activity.
-!- MISCELLANEOUS: Present with 13400 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-----------------------------------------------------------------------
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EMBL; K01386; AAA35176.1; -; Genomic_DNA.
EMBL; X75951; CAA53562.1; -; Genomic_DNA.
EMBL; Z28211; CAA82056.1; -; Genomic_DNA.
EMBL; M36300; AAA34450.1; -; Genomic_DNA.
EMBL; BK006944; DAA08958.1; -; Genomic_DNA.
PIR; S38049; NNBY2.
RefSeq; NP_012711.1; NM_001179776.1.
ProteinModelPortal; P00937; -.
SMR; P00937; -.
BioGrid; 33954; 90.
ComplexPortal; CPX-1850; Anthranilate synthase complex.
DIP; DIP-543N; -.
IntAct; P00937; 39.
MINT; P00937; -.
STRING; 4932.YKL211C; -.
MEROPS; C26.959; -.
iPTMnet; P00937; -.
MaxQB; P00937; -.
PaxDb; P00937; -.
PRIDE; P00937; -.
EnsemblFungi; YKL211C; YKL211C; YKL211C.
GeneID; 853669; -.
KEGG; sce:YKL211C; -.
EuPathDB; FungiDB:YKL211C; -.
SGD; S000001694; TRP3.
GeneTree; ENSGT00620000088738; -.
HOGENOM; HOG000280459; -.
InParanoid; P00937; -.
KO; K01656; -.
OMA; WFKGSIE; -.
OrthoDB; EOG092C1PKC; -.
BioCyc; YEAST:YKL211C-MONOMER; -.
UniPathway; UPA00035; UER00040.
UniPathway; UPA00035; UER00043.
PRO; PR:P00937; -.
Proteomes; UP000002311; Chromosome XI.
GO; GO:0005950; C:anthranilate synthase complex; IPI:SGD.
GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-EC.
GO; GO:0004425; F:indole-3-glycerol-phosphate synthase activity; IMP:SGD.
GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
GO; GO:0000162; P:tryptophan biosynthetic process; IMP:SGD.
CDD; cd00331; IGPS; 1.
Gene3D; 3.20.20.70; -; 1.
Gene3D; 3.40.50.880; -; 1.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR029062; Class_I_gatase-like.
InterPro; IPR017926; GATASE.
InterPro; IPR013798; Indole-3-glycerol_P_synth.
InterPro; IPR001468; Indole-3-GlycerolPSynthase_CS.
InterPro; IPR011060; RibuloseP-bd_barrel.
InterPro; IPR006221; TrpG/PapA_dom.
Pfam; PF00117; GATase; 1.
Pfam; PF00218; IGPS; 1.
SUPFAM; SSF51366; SSF51366; 1.
SUPFAM; SSF52317; SSF52317; 1.
TIGRFAMs; TIGR00566; trpG_papA; 1.
PROSITE; PS51273; GATASE_TYPE_1; 1.
PROSITE; PS00614; IGPS; 1.
1: Evidence at protein level;
Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
Complete proteome; Glutamine amidotransferase; Lyase;
Multifunctional enzyme; Phosphoprotein; Reference proteome;
Tryptophan biosynthesis.
CHAIN 1 484 Multifunctional tryptophan biosynthesis
protein.
/FTId=PRO_0000056866.
DOMAIN 13 207 Glutamine amidotransferase type-1.
{ECO:0000255|PROSITE-ProRule:PRU00605}.
REGION 64 66 Glutamine binding.
{ECO:0000250|UniProtKB:P00900}.
REGION 142 143 Glutamine binding.
{ECO:0000250|UniProtKB:P00900}.
REGION 215 484 Indole-3-glycerol phosphate synthase.
ACT_SITE 92 92 Nucleophile; for GATase activity.
{ECO:0000255|PROSITE-ProRule:PRU00605}.
ACT_SITE 181 181 For GATase activity.
{ECO:0000255|PROSITE-ProRule:PRU00605}.
ACT_SITE 183 183 For GATase activity.
{ECO:0000255|PROSITE-ProRule:PRU00605}.
BINDING 96 96 Glutamine.
{ECO:0000250|UniProtKB:P00900}.
MOD_RES 2 2 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
CONFLICT 32 32 C -> S (in Ref. 5; AAA34450).
{ECO:0000305}.
CONFLICT 63 65 PGP -> LGL (in Ref. 5; AAA34450).
{ECO:0000305}.
CONFLICT 129 129 K -> R (in Ref. 1; AAA35176).
{ECO:0000305}.
CONFLICT 170 170 H -> Y (in Ref. 5; AAA34450).
{ECO:0000305}.
CONFLICT 236 236 G -> S (in Ref. 5; AAA34450).
{ECO:0000305}.
SEQUENCE 484 AA; 53489 MW; 34EF65E829279C1F CRC64;
MSVHAATNPI NKHVVLIDNY DSFTWNVYEY LCQEGAKVSV YRNDAITVPE IAALNPDTLL
ISPGPGHPKT DSGISRDCIR YFTGKIPVFG ICMGQQCMFD VFGGEVAYAG EIVHGKTSPI
SHDNCGIFKN VPQGIAVTRY HSLAGTESSL PSCLKVTAST ENGIIMGVRH KKYTVEGVQF
HPESILTEEG HLMIRNILNV SGGTWEENKS SPSNSILDRI YARRKIDVNE QSKIPGFTFQ
DLQSNYDLGL APPLQDFYTV LSSSHKRAVV LAEVKRASPS KGPICLKAVA AEQALKYAEA
GASAISVLTE PHWFHGSLQD LVNVRKILDL KFPPKERPCV LRKEFIFSKY QILEARLAGA
DTVLLIVKML SQPLLKELYS YSKDLNMEPL VEVNSKEELQ RALEIGAKVV GVNNRDLHSF
NVDLNTTSNL VESIPKDVLL IALSGITTRD DAEKYKKEGV HGFLVGEALM KSTDVKKFIH
ELCE


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