Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P40857

- PHS1_YEAST

UniProt

P40857 - PHS1_YEAST

Protein

Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase PHS1

Gene

PHS1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Responsible for the dehydration step in very long-chain fatty acid (VLCFA) synthesis.2 Publications

    Catalytic activityi

    A very-long-chain (3R)-3-hydroxyacyl-CoA = a very-long-chain trans-2,3-dehydroacyl-CoA + H2O.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei149 – 14911 Publication
    Active sitei156 – 15611 Publication

    GO - Molecular functioni

    1. 3-hydroxyacyl-CoA dehydratase activity Source: SGD
    2. enoyl-CoA hydratase activity Source: SGD

    GO - Biological processi

    1. fatty acid elongation Source: SGD
    2. sphingolipid biosynthetic process Source: SGD
    3. vacuolar transport Source: SGD

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-17327.
    YEAST:G3O-31552-MONOMER.
    YEAST:MONOMER3O-85.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase PHS1 (EC:4.2.1.134)
    Alternative name(s):
    3-hydroxyacyl-CoA dehydratase PHS1
    Short name:
    HACD
    PTPLA homolog involved in sphingolipid biosynthesis protein 1
    Gene namesi
    Name:PHS1
    Ordered Locus Names:YJL097W
    ORF Names:J0902
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome X

    Organism-specific databases

    CYGDiYJL097w.
    SGDiS000003633. PHS1.

    Subcellular locationi

    GO - Cellular componenti

    1. fungal-type vacuole Source: SGD
    2. integral component of endoplasmic reticulum membrane Source: SGD
    3. vacuolar membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane, Vacuole

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi149 – 1491Y → A: No catalytic activity. 1 Publication
    Mutagenesisi156 – 1561E → A: No catalytic activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 217217Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase PHS1PRO_0000203047Add
    BLAST

    Proteomic databases

    PaxDbiP40857.

    Expressioni

    Gene expression databases

    GenevestigatoriP40857.

    Interactioni

    Protein-protein interaction databases

    BioGridi33660. 27 interactions.
    DIPiDIP-2104N.
    IntActiP40857. 31 interactions.
    MINTiMINT-534987.
    STRINGi4932.YJL097W.

    Structurei

    3D structure databases

    ProteinModelPortaliP40857.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1111CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini30 – 4718LumenalSequence AnalysisAdd
    BLAST
    Topological domaini67 – 7610CytoplasmicSequence Analysis
    Topological domaini95 – 995LumenalSequence Analysis
    Topological domaini118 – 14225CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini161 – 17818LumenalSequence AnalysisAdd
    BLAST
    Topological domaini197 – 21721CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei12 – 2918HelicalSequence AnalysisAdd
    BLAST
    Transmembranei48 – 6619HelicalSequence AnalysisAdd
    BLAST
    Transmembranei77 – 9418HelicalSequence AnalysisAdd
    BLAST
    Transmembranei100 – 11718HelicalSequence AnalysisAdd
    BLAST
    Transmembranei143 – 16018HelicalSequence AnalysisAdd
    BLAST
    Transmembranei179 – 19618HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi214 – 2174Endoplasmic reticulum retention signal

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG5198.
    GeneTreeiENSGT00530000062962.
    HOGENOMiHOG000190538.
    KOiK10703.
    OMAiGEFTKWT.
    OrthoDBiEOG7NKKXC.

    Family and domain databases

    InterProiIPR007482. Tyr_Pase-like_PTPLA.
    [Graphical view]
    PANTHERiPTHR11035. PTHR11035. 1 hit.
    PfamiPF04387. PTPLA. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P40857-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSKKLASPLS FLPLYNLLSA VGWSYLLYLV ISLYPKVGQP AFFYQTKNVA    50
    TLVQCGAIIE IINSFLGVVR SPLLTTVAQV SSRLLVVLGI FQLLPNTSGV 100
    QSVVYISLLL AWSITEIVRY LYYFFMLVFK NGAPKILILL RYNLFWILYP 150
    TGVASELRII YCALNAAESQ YSLLYKRILI AAMLAYIPGF PMLFLHMVAQ 200
    RKKVMKSLRS SFGKKLI 217
    Length:217
    Mass (Da):24,511
    Last modified:February 1, 1995 - v1
    Checksum:i5C87BC9563FB83AA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X77923 Genomic DNA. Translation: CAA54893.1.
    Z49372 Genomic DNA. Translation: CAA89391.1.
    AY557855 Genomic DNA. Translation: AAS56181.1.
    BK006943 Genomic DNA. Translation: DAA08703.1.
    PIRiS50296.
    RefSeqiNP_012438.1. NM_001181530.1.

    Genome annotation databases

    EnsemblFungiiYJL097W; YJL097W; YJL097W.
    GeneIDi853348.
    KEGGisce:YJL097W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X77923 Genomic DNA. Translation: CAA54893.1 .
    Z49372 Genomic DNA. Translation: CAA89391.1 .
    AY557855 Genomic DNA. Translation: AAS56181.1 .
    BK006943 Genomic DNA. Translation: DAA08703.1 .
    PIRi S50296.
    RefSeqi NP_012438.1. NM_001181530.1.

    3D structure databases

    ProteinModelPortali P40857.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 33660. 27 interactions.
    DIPi DIP-2104N.
    IntActi P40857. 31 interactions.
    MINTi MINT-534987.
    STRINGi 4932.YJL097W.

    Proteomic databases

    PaxDbi P40857.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YJL097W ; YJL097W ; YJL097W .
    GeneIDi 853348.
    KEGGi sce:YJL097W.

    Organism-specific databases

    CYGDi YJL097w.
    SGDi S000003633. PHS1.

    Phylogenomic databases

    eggNOGi COG5198.
    GeneTreei ENSGT00530000062962.
    HOGENOMi HOG000190538.
    KOi K10703.
    OMAi GEFTKWT.
    OrthoDBi EOG7NKKXC.

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-17327.
    YEAST:G3O-31552-MONOMER.
    YEAST:MONOMER3O-85.

    Miscellaneous databases

    NextBioi 973747.

    Gene expression databases

    Genevestigatori P40857.

    Family and domain databases

    InterProi IPR007482. Tyr_Pase-like_PTPLA.
    [Graphical view ]
    PANTHERi PTHR11035. PTHR11035. 1 hit.
    Pfami PF04387. PTPLA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence and function analysis of a 9.74 kb fragment of Saccharomyces cerevisiae chromosome X including the BCK1 gene."
      Miosga T., Boles E., Schaaff-Gerstenschlaeger I., Schmitt S., Zimmermann F.K.
      Yeast 10:1481-1488(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
      Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K.
      , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
      EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    6. "A global topology map of the Saccharomyces cerevisiae membrane proteome."
      Kim H., Melen K., Oesterberg M., von Heijne G.
      Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
      Strain: ATCC 208353 / W303-1A.
    7. "A molecular caliper mechanism for determining very long-chain fatty acid length."
      Denic V., Weissman J.S.
      Cell 130:663-677(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY.
    8. "Membrane topology and essential amino acid residues of Phs1, a 3-hydroxyacyl-CoA dehydratase involved in very long-chain fatty acid elongation."
      Kihara A., Sakuraba H., Ikeda M., Denpoh A., Igarashi Y.
      J. Biol. Chem. 283:11199-11209(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, MUTAGENESIS OF TYR-149 AND GLU-156, ACTIVE SITE, CATALYTIC ACTIVITY.

    Entry informationi

    Entry nameiPHS1_YEAST
    AccessioniPrimary (citable) accession number: P40857
    Secondary accession number(s): D6VW87
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 105 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3