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P32263

- P5CR_YEAST

UniProt

P32263 - P5CR_YEAST

Protein

Pyrroline-5-carboxylate reductase

Gene

PRO3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 1 (01 Oct 1993)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    L-proline + NAD(P)+ = 1-pyrroline-5-carboxylate + NAD(P)H.

    Pathwayi

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. pyrroline-5-carboxylate reductase activity Source: SGD

    GO - Biological processi

    1. L-proline biosynthetic process Source: UniProtKB-UniPathway
    2. proline biosynthetic process Source: SGD

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Amino-acid biosynthesis, Proline biosynthesis

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-11544.
    YEAST:YER023W-MONOMER.
    UniPathwayiUPA00098; UER00361.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pyrroline-5-carboxylate reductase (EC:1.5.1.2)
    Short name:
    P5C reductase
    Short name:
    P5CR
    Gene namesi
    Name:PRO3
    Synonyms:ORE2
    Ordered Locus Names:YER023W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome V

    Organism-specific databases

    CYGDiYER023w.
    SGDiS000000825. PRO3.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: SGD

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 286286Pyrroline-5-carboxylate reductasePRO_0000187328Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei246 – 2461Phosphothreonine1 Publication
    Modified residuei279 – 2791Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP32263.
    PaxDbiP32263.
    PeptideAtlasiP32263.

    Expressioni

    Gene expression databases

    GenevestigatoriP32263.

    Interactioni

    Subunit structurei

    Homotetramer.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself4EBI-13885,EBI-13885

    Protein-protein interaction databases

    BioGridi36757. 32 interactions.
    DIPiDIP-1529N.
    IntActiP32263. 11 interactions.
    MINTiMINT-411759.
    STRINGi4932.YER023W.

    Structurei

    3D structure databases

    ProteinModelPortaliP32263.
    SMRiP32263. Positions 5-282.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0345.
    GeneTreeiENSGT00390000007443.
    HOGENOMiHOG000230247.
    KOiK00286.
    OMAiCCKPQQA.
    OrthoDBiEOG76DV3T.

    Family and domain databases

    Gene3Di1.10.3730.10. 1 hit.
    3.40.50.720. 1 hit.
    HAMAPiMF_01925. P5C_reductase.
    InterProiIPR008927. 6-PGluconate_DH_C-like.
    IPR016040. NAD(P)-bd_dom.
    IPR029036. P5CR_dimer.
    IPR028939. ProC_N.
    IPR000304. Pyrroline-COOH_reductase.
    [Graphical view]
    PANTHERiPTHR11645. PTHR11645. 1 hit.
    PfamiPF03807. F420_oxidored. 1 hit.
    PF14748. P5CR_dimer. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000193. Pyrrol-5-carb_rd. 1 hit.
    SUPFAMiSSF48179. SSF48179. 1 hit.
    TIGRFAMsiTIGR00112. proC. 1 hit.
    PROSITEiPS00521. P5CR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P32263-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTYTLAILGC GVMGQALLSA IYNAPKAADE TAAAFYPSKI ITCNHDEPSA    50
    QQVTDLVETF DESPNGIKVE STYGHNVSAV EEASVVLLGT KPFLAEEVLN 100
    GVKSVIGGKL LISLAAGWTI DQLSQYTSTV CRVMTNTPAK YGYGCAVVSY 150
    SADVSKEQKP LVNELISQVG KYVELPEKNM DAATALVGSG PAFVLLMLES 200
    LMESGLKLGI PLQESKECAM KVLEGTVKMV EKSGAHPSVL KHQVCTPGGT 250
    TIAGLCVMEE KGVKSGIING VEEAARVASQ LGQKKK 286
    Length:286
    Mass (Da):30,132
    Last modified:October 1, 1993 - v1
    Checksum:iAEB71D93B46D08B3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M57886 Genomic DNA. Translation: AAA34905.1.
    X57338 Genomic DNA. Translation: CAA40614.1.
    U18778 Genomic DNA. Translation: AAB64556.1.
    BK006939 Genomic DNA. Translation: DAA07676.1.
    PIRiS25293.
    RefSeqiNP_010940.3. NM_001178914.3.

    Genome annotation databases

    EnsemblFungiiYER023W; YER023W; YER023W.
    GeneIDi856744.
    KEGGisce:YER023W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M57886 Genomic DNA. Translation: AAA34905.1 .
    X57338 Genomic DNA. Translation: CAA40614.1 .
    U18778 Genomic DNA. Translation: AAB64556.1 .
    BK006939 Genomic DNA. Translation: DAA07676.1 .
    PIRi S25293.
    RefSeqi NP_010940.3. NM_001178914.3.

    3D structure databases

    ProteinModelPortali P32263.
    SMRi P32263. Positions 5-282.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 36757. 32 interactions.
    DIPi DIP-1529N.
    IntActi P32263. 11 interactions.
    MINTi MINT-411759.
    STRINGi 4932.YER023W.

    Proteomic databases

    MaxQBi P32263.
    PaxDbi P32263.
    PeptideAtlasi P32263.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YER023W ; YER023W ; YER023W .
    GeneIDi 856744.
    KEGGi sce:YER023W.

    Organism-specific databases

    CYGDi YER023w.
    SGDi S000000825. PRO3.

    Phylogenomic databases

    eggNOGi COG0345.
    GeneTreei ENSGT00390000007443.
    HOGENOMi HOG000230247.
    KOi K00286.
    OMAi CCKPQQA.
    OrthoDBi EOG76DV3T.

    Enzyme and pathway databases

    UniPathwayi UPA00098 ; UER00361 .
    BioCyci MetaCyc:MONOMER-11544.
    YEAST:YER023W-MONOMER.

    Miscellaneous databases

    NextBioi 982882.
    PROi P32263.

    Gene expression databases

    Genevestigatori P32263.

    Family and domain databases

    Gene3Di 1.10.3730.10. 1 hit.
    3.40.50.720. 1 hit.
    HAMAPi MF_01925. P5C_reductase.
    InterProi IPR008927. 6-PGluconate_DH_C-like.
    IPR016040. NAD(P)-bd_dom.
    IPR029036. P5CR_dimer.
    IPR028939. ProC_N.
    IPR000304. Pyrroline-COOH_reductase.
    [Graphical view ]
    PANTHERi PTHR11645. PTHR11645. 1 hit.
    Pfami PF03807. F420_oxidored. 1 hit.
    PF14748. P5CR_dimer. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000193. Pyrrol-5-carb_rd. 1 hit.
    SUPFAMi SSF48179. SSF48179. 1 hit.
    TIGRFAMsi TIGR00112. proC. 1 hit.
    PROSITEi PS00521. P5CR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Proline biosynthesis in Saccharomyces cerevisiae: analysis of the PRO3 gene, which encodes delta 1-pyrroline-5-carboxylate reductase."
      Brandriss M.C., Falvey D.A.
      J. Bacteriol. 174:3782-3788(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Erratum
      Brandriss M.C., Falvey D.A.
      J. Bacteriol. 174:5176-5176(1992) [PubMed] [Europe PMC] [Abstract]
    3. "ore2, a mutation affecting proline biosynthesis in the yeast Saccharomyces cerevisiae, leads to a cdc phenotype."
      Neuville P., Aigle M.
      Mol. Gen. Genet. 234:193-200(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    7. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-246 AND SER-279, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
      Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
      Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiP5CR_YEAST
    AccessioniPrimary (citable) accession number: P32263
    Secondary accession number(s): D3DLS2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: October 1, 1993
    Last modified: October 1, 2014
    This is version 130 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 43500 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 V
      Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

    External Data

    Dasty 3