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)

P54874

- HMCS_SCHPO

UniProt

P54874 - HMCS_SCHPO

Protein

Hydroxymethylglutaryl-CoA synthase

Gene

hcs1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    This enzyme condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA, which is the substrate for HMG-CoA reductase.By similarity

    Catalytic activityi

    Acetyl-CoA + H2O + acetoacetyl-CoA = (S)-3-hydroxy-3-methylglutaryl-CoA + CoA.PROSITE-ProRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei86 – 861Proton donor/acceptorPROSITE-ProRule annotation
    Active sitei118 – 1181Acyl-thioester intermediatePROSITE-ProRule annotation
    Active sitei250 – 2501Proton donor/acceptorPROSITE-ProRule annotation

    GO - Molecular functioni

    1. hydroxymethylglutaryl-CoA synthase activity Source: PomBase

    GO - Biological processi

    1. acetyl-CoA metabolic process Source: PomBase
    2. cellular response to nitrogen starvation Source: PomBase
    3. ergosterol biosynthetic process Source: PomBase
    4. farnesyl diphosphate biosynthetic process, mevalonate pathway Source: PomBase
    5. negative regulation of G0 to G1 transition Source: PomBase

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism

    Enzyme and pathway databases

    BRENDAi2.3.3.10. 5615.
    ReactomeiREACT_188314. PPARA activates gene expression.
    REACT_188316. Activation of gene expression by SREBF (SREBP).
    REACT_223245. Synthesis of Ketone Bodies.
    UniPathwayiUPA00058; UER00102.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Hydroxymethylglutaryl-CoA synthase (EC:2.3.3.10)
    Short name:
    HMG-CoA synthase
    Alternative name(s):
    3-hydroxy-3-methylglutaryl coenzyme A synthase
    Gene namesi
    Name:hcs1
    Synonyms:hcs
    ORF Names:SPAC4F8.14c
    OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
    Taxonomic identifieri284812 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
    ProteomesiUP000002485: Chromosome I

    Organism-specific databases

    PomBaseiSPAC4F8.14c.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: PomBase
    2. endoplasmic reticulum Source: PomBase
    3. nucleus Source: PomBase

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 447447Hydroxymethylglutaryl-CoA synthasePRO_0000213757Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei398 – 3981Phosphothreonine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP54874.
    PaxDbiP54874.

    Interactioni

    Protein-protein interaction databases

    BioGridi279573. 2 interactions.
    MINTiMINT-4690976.
    STRINGi4896.SPAC4F8.14c-1.

    Structurei

    3D structure databases

    ProteinModelPortaliP54874.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the HMG-CoA synthase family.Curated

    Phylogenomic databases

    eggNOGiCOG3425.
    HOGENOMiHOG000012351.
    KOiK01641.
    OMAiPHVFQID.
    PhylomeDBiP54874.

    Family and domain databases

    Gene3Di3.40.47.10. 1 hit.
    InterProiIPR000590. HMG_CoA_synt_AS.
    IPR013746. HMG_CoA_synt_C_dom.
    IPR013528. HMG_CoA_synth_N.
    IPR010122. HMG_CoA_synthase_euk.
    IPR016039. Thiolase-like.
    IPR016038. Thiolase-like_subgr.
    [Graphical view]
    PfamiPF08540. HMG_CoA_synt_C. 1 hit.
    PF01154. HMG_CoA_synt_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF53901. SSF53901. 3 hits.
    TIGRFAMsiTIGR01833. HMG-CoA-S_euk. 1 hit.
    PROSITEiPS01226. HMG_COA_SYNTHASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P54874-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSFDRKDIGI KGLVLYTPNQ YVEQAALEAH DGVSTGKYTI GLGLTKMAFV    50
    DDREDIYSFG LTALSQLIKR YQIDISKIGR LEVGTETIID KSKSVKSVLM 100
    QLFGDNHNVE GIDCVNACYG GVNALFNTID WIESSAWDGR DGIVVAGDIA 150
    LYAKGNARPT GGAGCVALLV GPNAPIVFEP GLRGTYMQHA YDFYKPDLTS 200
    EYPYVDGHFS LECYVKALDG AYANYNVRDV AKNGKSQGLG LDRFDYCIFH 250
    APTCKQVQKA YARLLYTDSA AEPSNPELEG VRELLSTLDA KKSLTDKALE 300
    KGLMAITKER FNKRVSPSVY APTNCGNMYT ASIFSCLTAL LSRVPADELK 350
    GKRVGAYSYG SGLAASFFSF VVKGDVSEIA KKTNLVNDLD NRHCLTPTQY 400
    EEAIELRHQA HLKKNFTPKG SIERLRSGTY YLTGIDDMFR RSYSVKP 447
    Length:447
    Mass (Da):49,239
    Last modified:October 1, 1996 - v1
    Checksum:i919BDDBD9207B886
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U32187 Genomic DNA. Translation: AAB17601.1.
    CU329670 Genomic DNA. Translation: CAB11060.1.
    PIRiS61875.
    RefSeqiNP_593859.1. NM_001019288.2.

    Genome annotation databases

    EnsemblFungiiSPAC4F8.14c.1; SPAC4F8.14c.1:pep; SPAC4F8.14c.
    GeneIDi2543141.
    KEGGispo:SPAC4F8.14c.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U32187 Genomic DNA. Translation: AAB17601.1 .
    CU329670 Genomic DNA. Translation: CAB11060.1 .
    PIRi S61875.
    RefSeqi NP_593859.1. NM_001019288.2.

    3D structure databases

    ProteinModelPortali P54874.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 279573. 2 interactions.
    MINTi MINT-4690976.
    STRINGi 4896.SPAC4F8.14c-1.

    Proteomic databases

    MaxQBi P54874.
    PaxDbi P54874.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii SPAC4F8.14c.1 ; SPAC4F8.14c.1:pep ; SPAC4F8.14c .
    GeneIDi 2543141.
    KEGGi spo:SPAC4F8.14c.

    Organism-specific databases

    PomBasei SPAC4F8.14c.

    Phylogenomic databases

    eggNOGi COG3425.
    HOGENOMi HOG000012351.
    KOi K01641.
    OMAi PHVFQID.
    PhylomeDBi P54874.

    Enzyme and pathway databases

    UniPathwayi UPA00058 ; UER00102 .
    BRENDAi 2.3.3.10. 5615.
    Reactomei REACT_188314. PPARA activates gene expression.
    REACT_188316. Activation of gene expression by SREBF (SREBP).
    REACT_223245. Synthesis of Ketone Bodies.

    Miscellaneous databases

    NextBioi 20804168.

    Family and domain databases

    Gene3Di 3.40.47.10. 1 hit.
    InterProi IPR000590. HMG_CoA_synt_AS.
    IPR013746. HMG_CoA_synt_C_dom.
    IPR013528. HMG_CoA_synth_N.
    IPR010122. HMG_CoA_synthase_euk.
    IPR016039. Thiolase-like.
    IPR016038. Thiolase-like_subgr.
    [Graphical view ]
    Pfami PF08540. HMG_CoA_synt_C. 1 hit.
    PF01154. HMG_CoA_synt_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53901. SSF53901. 3 hits.
    TIGRFAMsi TIGR01833. HMG-CoA-S_euk. 1 hit.
    PROSITEi PS01226. HMG_COA_SYNTHASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and sequencing of the hcs gene, which encodes 3-hydroxy-3-methylglutaryl coenzyme A synthase of Schizosaccharomyces pombe."
      Katayama S., Adachi N., Takao K., Nakagawa T., Matsuda H., Kawamukai M.
      Yeast 11:1533-1537(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The genome sequence of Schizosaccharomyces pombe."
      Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
      , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
      Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 972 / ATCC 24843.
    3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-398, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiHMCS_SCHPO
    AccessioniPrimary (citable) accession number: P54874
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 114 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. Schizosaccharomyces pombe
      Schizosaccharomyces pombe: entries and gene names
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3