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P00912

- TRPF_YEAST

UniProt

P00912 - TRPF_YEAST

Protein

N-(5'-phosphoribosyl)anthranilate isomerase

Gene

TRP1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 2 (21 Dec 2004)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate.

    Pathwayi

    GO - Molecular functioni

    1. phosphoribosylanthranilate isomerase activity Source: SGD

    GO - Biological processi

    1. tryptophan biosynthetic process Source: SGD

    Keywords - Molecular functioni

    Isomerase

    Keywords - Biological processi

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

    Enzyme and pathway databases

    BioCyciYEAST:YDR007W-MONOMER.
    UniPathwayiUPA00035; UER00042.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    N-(5'-phosphoribosyl)anthranilate isomerase (EC:5.3.1.24)
    Short name:
    PRAI
    Gene namesi
    Name:TRP1
    Ordered Locus Names:YDR007W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IV

    Organism-specific databases

    CYGDiYDR007w.
    SGDiS000002414. TRP1.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 224224N-(5'-phosphoribosyl)anthranilate isomerasePRO_0000154337Add
    BLAST

    Proteomic databases

    MaxQBiP00912.
    PaxDbiP00912.

    Expressioni

    Gene expression databases

    GenevestigatoriP00912.

    Interactioni

    Protein-protein interaction databases

    BioGridi32060. 35 interactions.
    DIPiDIP-2671N.
    IntActiP00912. 1 interaction.
    MINTiMINT-509744.

    Structurei

    3D structure databases

    ProteinModelPortaliP00912.
    SMRiP00912. Positions 14-215.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the TrpF family.Curated

    Phylogenomic databases

    eggNOGiCOG0135.
    KOiK01817.
    OMAiKRNIDIN.
    OrthoDBiEOG76MKM7.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_00135. PRAI.
    InterProiIPR013785. Aldolase_TIM.
    IPR001240. PRAI_dom.
    IPR011060. RibuloseP-bd_barrel.
    [Graphical view]
    PfamiPF00697. PRAI. 1 hit.
    [Graphical view]
    SUPFAMiSSF51366. SSF51366. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P00912-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSVINFTGSS GPLVKVCGLQ STEAAECALD SDADLLGIIC VPNRKRTIDP    50
    VIARKISSLV KAYKNSSGTP KYLVGVFRNQ PKEDVLALVN DYGIDIVQLH 100
    GDESWQEYQE FLGLPVIKRL VFPKDCNILL SAASQKPHSF IPLFDSEAGG 150
    TGELLDWNSI SDWVGRQESP ESLHFMLAGG LTPENVGDAL RLNGVIGVDV 200
    SGGVETNGVK DSNKIANFVK NAKK 224
    Length:224
    Mass (Da):24,144
    Last modified:December 21, 2004 - v2
    Checksum:i03353B85F24FA09D
    GO

    Sequence cautioni

    The sequence AAA80674.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAA88067.1 differs from that shown. Reason: Erroneous termination at position 67. Translated as Ser. This mutation is only found in the substrain S288c / AB972. The S288c reference strain does not contain this mutation.
    The sequence CAA88068.1 differs from that shown. Reason: Erroneous termination at position 67. Translated as Ser. This mutation is only found in the substrain S288c / AB972. The S288c reference strain does not contain this mutation.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti48 – 481I → V in strain: CLIB 556 haplotype Ha2 and CLIB 630 haplotype Ha2. 1 Publication
    Natural varianti172 – 1721S → R in strain: CLIB 556 haplotype Ha1. 1 Publication
    Natural varianti212 – 2121S → F in strain: CLIB 95, CLIB 382, CLIB 388, CLIB 556 haplotype Ha2, CLIB 630, K1, R12, R13, YIIc12 haplotype Ha2 and YIIc17 haplotype Ha1. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V01341 Genomic DNA. Translation: CAA24634.1.
    M74015 Genomic DNA. Translation: AAA72097.1.
    U37458 Genomic DNA. Translation: AAA80674.1. Different initiation.
    AJ585667 Genomic DNA. Translation: CAE52187.1.
    AJ585668 Genomic DNA. Translation: CAE52188.1.
    AJ585669 Genomic DNA. Translation: CAE52189.1.
    AJ585670 Genomic DNA. Translation: CAE52190.1.
    AJ585671 Genomic DNA. Translation: CAE52191.1.
    AJ585672 Genomic DNA. Translation: CAE52192.1.
    AJ585673 Genomic DNA. Translation: CAE52193.1.
    AJ585674 Genomic DNA. Translation: CAE52194.1.
    AJ585675 Genomic DNA. Translation: CAE52195.1.
    AJ585676 Genomic DNA. Translation: CAE52196.1.
    AJ585677 Genomic DNA. Translation: CAE52197.1.
    AJ585678 Genomic DNA. Translation: CAE52198.1.
    AJ585679 Genomic DNA. Translation: CAE52199.1.
    AJ585680 Genomic DNA. Translation: CAE52200.1.
    AJ585681 Genomic DNA. Translation: CAE52201.1.
    AJ585682 Genomic DNA. Translation: CAE52202.1.
    AJ585683 Genomic DNA. Translation: CAE52203.1.
    AJ585684 Genomic DNA. Translation: CAE52204.1.
    AJ585685 Genomic DNA. Translation: CAE52205.1.
    Z48008 Genomic DNA. Translation: CAA88067.1. Sequence problems.
    Z48008 Genomic DNA. Translation: CAA88068.1. Sequence problems.
    M30386 Genomic DNA. Translation: AAA18406.1.
    BK006938 Genomic DNA. Translation: DAA11855.1.
    PIRiA01135. ISBYN.
    RefSeqiNP_010290.3. NM_001180315.3.

    Genome annotation databases

    EnsemblFungiiYDR007W; YDR007W; YDR007W.
    GeneIDi851570.
    KEGGisce:YDR007W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V01341 Genomic DNA. Translation: CAA24634.1 .
    M74015 Genomic DNA. Translation: AAA72097.1 .
    U37458 Genomic DNA. Translation: AAA80674.1 . Different initiation.
    AJ585667 Genomic DNA. Translation: CAE52187.1 .
    AJ585668 Genomic DNA. Translation: CAE52188.1 .
    AJ585669 Genomic DNA. Translation: CAE52189.1 .
    AJ585670 Genomic DNA. Translation: CAE52190.1 .
    AJ585671 Genomic DNA. Translation: CAE52191.1 .
    AJ585672 Genomic DNA. Translation: CAE52192.1 .
    AJ585673 Genomic DNA. Translation: CAE52193.1 .
    AJ585674 Genomic DNA. Translation: CAE52194.1 .
    AJ585675 Genomic DNA. Translation: CAE52195.1 .
    AJ585676 Genomic DNA. Translation: CAE52196.1 .
    AJ585677 Genomic DNA. Translation: CAE52197.1 .
    AJ585678 Genomic DNA. Translation: CAE52198.1 .
    AJ585679 Genomic DNA. Translation: CAE52199.1 .
    AJ585680 Genomic DNA. Translation: CAE52200.1 .
    AJ585681 Genomic DNA. Translation: CAE52201.1 .
    AJ585682 Genomic DNA. Translation: CAE52202.1 .
    AJ585683 Genomic DNA. Translation: CAE52203.1 .
    AJ585684 Genomic DNA. Translation: CAE52204.1 .
    AJ585685 Genomic DNA. Translation: CAE52205.1 .
    Z48008 Genomic DNA. Translation: CAA88067.1 . Sequence problems.
    Z48008 Genomic DNA. Translation: CAA88068.1 . Sequence problems.
    M30386 Genomic DNA. Translation: AAA18406.1 .
    BK006938 Genomic DNA. Translation: DAA11855.1 .
    PIRi A01135. ISBYN.
    RefSeqi NP_010290.3. NM_001180315.3.

    3D structure databases

    ProteinModelPortali P00912.
    SMRi P00912. Positions 14-215.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32060. 35 interactions.
    DIPi DIP-2671N.
    IntActi P00912. 1 interaction.
    MINTi MINT-509744.

    Proteomic databases

    MaxQBi P00912.
    PaxDbi P00912.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YDR007W ; YDR007W ; YDR007W .
    GeneIDi 851570.
    KEGGi sce:YDR007W.

    Organism-specific databases

    CYGDi YDR007w.
    SGDi S000002414. TRP1.

    Phylogenomic databases

    eggNOGi COG0135.
    KOi K01817.
    OMAi KRNIDIN.
    OrthoDBi EOG76MKM7.

    Enzyme and pathway databases

    UniPathwayi UPA00035 ; UER00042 .
    BioCyci YEAST:YDR007W-MONOMER.

    Miscellaneous databases

    NextBioi 969022.

    Gene expression databases

    Genevestigatori P00912.

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    HAMAPi MF_00135. PRAI.
    InterProi IPR013785. Aldolase_TIM.
    IPR001240. PRAI_dom.
    IPR011060. RibuloseP-bd_barrel.
    [Graphical view ]
    Pfami PF00697. PRAI. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51366. SSF51366. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Sequence of a yeast DNA fragment containing a chromosomal replicator and the TRP1 gene."
      Tschumper G., Carbon J.
      Gene 10:157-166(1980) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "A series of yeast shuttle vectors for expression of cDNAs and other DNA sequences."
      Brunelli J.P., Pall M.L.
      Yeast 9:1299-1308(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. Lieberman B.
      Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Differential evolution of the Saccharomyces cerevisiae DUP240 paralogs and implication of recombination in phylogeny."
      Leh-Louis V., Wirth B., Despons L., Wain-Hobson S., Potier S., Souciet J.-L.
      Nucleic Acids Res. 32:2069-2078(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-48; ARG-172 AND PHE-212.
      Strain: ATCC 204508 / S288c, CLIB 219, CLIB 382, CLIB 388, CLIB 410, CLIB 413, CLIB 556, CLIB 630, CLIB 95, K1, R12, R13, Sigma 1278B, YIIc12 and YIIc17.
    5. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
      Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
      , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
      Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    6. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    7. "Bent DNA at a yeast autonomously replicating sequence."
      Snyder M., Buchman A.R., Davis R.W.
      Nature 324:87-89(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 206-224.
    8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiTRPF_YEAST
    AccessioniPrimary (citable) accession number: P00912
    Secondary accession number(s): D6VRZ5
    , Q03448, Q12131, Q70DA4, Q70DA7, Q70DB2, Q7LHE0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: December 21, 2004
    Last modified: October 1, 2014
    This is version 124 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 1850 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome IV
      Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

    External Data

    Dasty 3