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P06531

- TRPG_EMENI

UniProt

P06531 - TRPG_EMENI

Protein

Multifunctional tryptophan biosynthesis protein

Gene

trpC

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 3 (19 Oct 2011)
      Previous versions | rss
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    Functioni

    Trifunctional enzyme bearing the Gln amidotransferase (GATase) domain of anthranilate synthase, indole-glycerolphosphate synthase, and phosphoribosylanthranilate isomerase activities.

    Catalytic activityi

    N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate.
    1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate = 1-C-(3-indolyl)-glycerol 3-phosphate + CO2 + H2O.
    Chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei104 – 1041For GATase activityBy similarity
    Active sitei199 – 1991For GATase activityBy similarity
    Active sitei201 – 2011For GATase activityBy similarity

    GO - Molecular functioni

    1. anthranilate synthase activity Source: UniProtKB-EC
    2. glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity Source: ASPGD
    3. indole-3-glycerol-phosphate synthase activity Source: ASPGD
    4. phosphoribosylanthranilate isomerase activity Source: ASPGD
    5. transferase activity Source: UniProtKB-KW

    GO - Biological processi

    1. cleistothecium development Source: ASPGD
    2. glutamine metabolic process Source: UniProtKB-KW
    3. oxidation-reduction process Source: GOC
    4. para-aminobenzoic acid biosynthetic process Source: ASPGD
    5. tryptophan biosynthetic process Source: ASPGD

    Keywords - Molecular functioni

    Decarboxylase, Isomerase, Lyase, Transferase

    Keywords - Biological processi

    Amino-acid biosynthesis, Aromatic amino acid biosynthesis, Tryptophan biosynthesis

    Enzyme and pathway databases

    UniPathwayiUPA00035; UER00040.
    UPA00035; UER00042.
    UPA00035; UER00043.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Multifunctional tryptophan biosynthesis protein
    Including the following 3 domains:
    Anthranilate synthase component 2 (EC:4.1.3.27)
    Short name:
    AS
    Alternative name(s):
    Anthranilate synthase, glutamine amidotransferase component
    Indole-3-glycerol phosphate synthase (EC:4.1.1.48)
    Short name:
    IGPS
    N-(5'-phosphoribosyl)anthranilate isomerase (EC:5.3.1.24)
    Short name:
    PRAI
    Gene namesi
    Name:trpC
    ORF Names:AN0648
    OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
    Taxonomic identifieri227321 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000000560: Chromosome VIII

    Subcellular locationi

    GO - Cellular componenti

    1. anthranilate synthase complex Source: ASPGD

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 768768Multifunctional tryptophan biosynthesis proteinPRO_0000056859Add
    BLAST

    Expressioni

    Inductioni

    By tryptophan starvation.

    Structurei

    3D structure databases

    ProteinModelPortaliP06531.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini25 – 225201Glutamine amidotransferase type-1Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni252 – 516265Indole-3-glycerol phosphate synthaseAdd
    BLAST
    Regioni532 – 768237N-(5'-phosphoribosyl)anthranilate isomeraseAdd
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Glutamine amidotransferase

    Phylogenomic databases

    eggNOGiCOG0134.
    HOGENOMiHOG000280459.
    OrthoDBiEOG78WM1Q.

    Family and domain databases

    Gene3Di3.20.20.70. 3 hits.
    3.40.50.880. 1 hit.
    HAMAPiMF_00135. PRAI.
    InterProiIPR013785. Aldolase_TIM.
    IPR016302. Anthranilate_synth_II.
    IPR029062. Class_I_gatase-like.
    IPR017926. GATASE.
    IPR013798. Indole-3-glycerol_P_synth.
    IPR001468. Indole-3-GlycerolPSynthase_CS.
    IPR001240. PRAI_dom.
    IPR011060. RibuloseP-bd_barrel.
    IPR006221. TrpG/PapA_dom.
    [Graphical view]
    PfamiPF00117. GATase. 1 hit.
    PF00218. IGPS. 1 hit.
    PF00697. PRAI. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001382. TrpG-trpC-trpF. 1 hit.
    SUPFAMiSSF51366. SSF51366. 3 hits.
    SSF52317. SSF52317. 1 hit.
    TIGRFAMsiTIGR00566. trpG_papA. 1 hit.
    PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
    PS00614. IGPS. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P06531-1 [UniParc]FASTAAdd to Basket

    « Hide

    MADTALVDHS PHHPTKAPRL ETASNVILID NYDSFTWNVY QYLVLEGATV    50
    TVIRNDEISL EELIAKKPTQ LVVSPGPGHP KSDAGISNAA IQYFAGKIPI 100
    FGVCMGQQCI IHSFGGKVDV TGEILHGKTS VLKHDGRGAY EGLPPSVIIT 150
    RYHSLAGTHS TIPECLEVSS FAQLGEDADK TVIMGVRHKQ FAVEGVQFHP 200
    ESILTEHGQT MFRNFLKLTA GTWEGNGKDV AQGGNFTAAA PNPPKATKKV 250
    SILEKIYDHR RAAVAKQKTI PSQRPSDLQA AYELSVAPPQ ISFPDRLRQS 300
    AYPLSLMAEI KRASPSKGLI AEHACAPAQA RQYAKAGASV ISVLTEPEWF 350
    KGSIDDLRAV RASLEGLTNR PAILRKEFIF DEYQILEARL AGADTVLLIV 400
    KMLDTELLTR LYLYSQSLGM EPLVEVNTPD EMKIAVDLGA QVIGVNNRDL 450
    TSFEVDLGTT SRLMDQVPES TIVCALSGIS GPKDVEAYKK DGVKAILVGE 500
    ALMRAPDTAA FVAELLGGQS KKLPLQSRNS PLVKICGTRT EEGARAAIEA 550
    GADLIGIILV EGRKRTVPDD VALQISKVVK STPRPTPYPT EVPQGDTDAT 600
    SVDYFDHSAT TLRHPTRALL VGVFLNQPLS YVLAQQQKLG LDVVQLHGSE 650
    PLEWSRLIPV PVIRKFGLDE FGIARRAYHT LPLLDSGAGG SGELLDQMRV 700
    KQILKSDDGL RVILAGGLDP LNVTEIIKQL DESGYKIVGV DVSSGVETNG 750
    VQDLDKIRSF VQAAKSAF 768
    Length:768
    Mass (Da):83,127
    Last modified:October 19, 2011 - v3
    Checksum:iFEFE1374DF86151D
    GO

    Sequence cautioni

    The sequence CBF89063.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence EAA65153.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti111 – 1111I → H in CAA26232. (PubMed:3158796)Curated
    Sequence conflicti249 – 2491K → Q in CAA26232. (PubMed:3158796)Curated
    Sequence conflicti396 – 3983VLL → SYV in CAA26232. (PubMed:3158796)Curated
    Sequence conflicti396 – 3983VLL → SYV(PubMed:6324178)Curated
    Sequence conflicti410 – 4156RLYLYS → QTLSLF in CAA26232. (PubMed:3158796)Curated
    Sequence conflicti410 – 4101R → Q(PubMed:6324178)Curated
    Sequence conflicti473 – 48210VCALSGISGP → RLCTMRYFWT in CAA26232. (PubMed:3158796)Curated
    Sequence conflicti681 – 6811L → V in CAA26232. (PubMed:3158796)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X02390 Genomic DNA. Translation: CAA26232.1.
    AACD01000009 Genomic DNA. Translation: EAA65153.1. Sequence problems.
    U24705 Genomic DNA. Translation: AAB60292.1.
    BN001308 Genomic DNA. Translation: CBF89063.1. Different initiation.
    PIRiS04518.
    S07305.
    RefSeqiXP_658252.1. XM_653160.1.

    Genome annotation databases

    EnsemblFungiiCADANIAT00002028; CADANIAP00002028; CADANIAG00002028.
    GeneIDi2876427.
    KEGGiani:AN0648.2.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X02390 Genomic DNA. Translation: CAA26232.1 .
    AACD01000009 Genomic DNA. Translation: EAA65153.1 . Sequence problems.
    U24705 Genomic DNA. Translation: AAB60292.1 .
    BN001308 Genomic DNA. Translation: CBF89063.1 . Different initiation.
    PIRi S04518.
    S07305.
    RefSeqi XP_658252.1. XM_653160.1.

    3D structure databases

    ProteinModelPortali P06531.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADANIAT00002028 ; CADANIAP00002028 ; CADANIAG00002028 .
    GeneIDi 2876427.
    KEGGi ani:AN0648.2.

    Phylogenomic databases

    eggNOGi COG0134.
    HOGENOMi HOG000280459.
    OrthoDBi EOG78WM1Q.

    Enzyme and pathway databases

    UniPathwayi UPA00035 ; UER00040 .
    UPA00035 ; UER00042 .
    UPA00035 ; UER00043 .

    Family and domain databases

    Gene3Di 3.20.20.70. 3 hits.
    3.40.50.880. 1 hit.
    HAMAPi MF_00135. PRAI.
    InterProi IPR013785. Aldolase_TIM.
    IPR016302. Anthranilate_synth_II.
    IPR029062. Class_I_gatase-like.
    IPR017926. GATASE.
    IPR013798. Indole-3-glycerol_P_synth.
    IPR001468. Indole-3-GlycerolPSynthase_CS.
    IPR001240. PRAI_dom.
    IPR011060. RibuloseP-bd_barrel.
    IPR006221. TrpG/PapA_dom.
    [Graphical view ]
    Pfami PF00117. GATase. 1 hit.
    PF00218. IGPS. 1 hit.
    PF00697. PRAI. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001382. TrpG-trpC-trpF. 1 hit.
    SUPFAMi SSF51366. SSF51366. 3 hits.
    SSF52317. SSF52317. 1 hit.
    TIGRFAMsi TIGR00566. trpG_papA. 1 hit.
    PROSITEi PS51273. GATASE_TYPE_1. 1 hit.
    PS00614. IGPS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of the Aspergillus niger trpC gene: structural relationship with analogous genes of other organisms."
      Kos T., Kuijvenhoven A., Hessing H.G.M., Pouwels P.H., van den Hondel C.A.M.J.J.
      Curr. Genet. 13:137-144(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Primary structure of the trpC gene from Aspergillus nidulans."
      Mullaney E.J., Hamer J.E., Roberti K.A., Yelton M.M., Timberlake W.E.
      Mol. Gen. Genet. 199:37-45(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 7-768.
      Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
    4. "The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
      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.
      Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENOME REANNOTATION.
      Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
    5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 377-410.
    6. Genser K.F.
      Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 719-768.

    Entry informationi

    Entry nameiTRPG_EMENI
    AccessioniPrimary (citable) accession number: P06531
    Secondary accession number(s): C8VS06, Q5BFN2, Q92224
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: October 19, 2011
    Last modified: October 1, 2014
    This is version 126 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3