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P08536

- MET3_YEAST

UniProt

P08536 - MET3_YEAST

Protein

Sulfate adenylyltransferase

Gene

MET3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 2 (21 Feb 2006)
      Previous versions | rss
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    Functioni

    Catalyzes the first intracellular reaction of sulfate assimilation, forming adenosine-5'-phosphosulfate (APS) from inorganic sulfate and ATP. Plays an important role in sulfate activation as a component of the biosynthesis pathway of sulfur-containing amino acids.

    Catalytic activityi

    ATP + sulfate = diphosphate + adenylyl sulfate.UniRule annotation

    Kineticsi

    1. KM=0.65 mM for Sulfate1 Publication
    2. KM=0.082 mM for ATP1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei196 – 1961
    Active sitei197 – 1971
    Active sitei198 – 1981
    Sitei201 – 2011Transition state stabilizer
    Binding sitei204 – 2041Substrate
    Sitei204 – 2041Transition state stabilizer
    Sitei328 – 3281Induces change in substrate recognition on ATP binding
    Binding sitei331 – 3311ATP; via amide nitrogen
    Binding sitei355 – 3551Substrate
    Binding sitei356 – 3561Substrate; via carbonyl oxygen

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi194 – 1985ATP
    Nucleotide bindingi289 – 2935ATP

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. sulfate adenylyltransferase (ATP) activity Source: SGD

    GO - Biological processi

    1. cysteine biosynthetic process Source: UniProtKB-KW
    2. hydrogen sulfide biosynthetic process Source: UniProtKB-UniPathway
    3. methionine biosynthetic process Source: UniProtKB-KW
    4. sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin) Source: SGD
    5. sulfur amino acid metabolic process Source: SGD

    Keywords - Molecular functioni

    Nucleotidyltransferase, Transferase

    Keywords - Biological processi

    Amino-acid biosynthesis, Cysteine biosynthesis, Methionine biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-362.
    YEAST:YJR010W-MONOMER.
    UniPathwayiUPA00140; UER00204.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sulfate adenylyltransferaseUniRule annotation (EC:2.7.7.4UniRule annotation)
    Alternative name(s):
    ATP-sulfurylaseUniRule annotation
    Methionine-requiring protein 3UniRule annotation
    Sulfate adenylate transferaseUniRule annotation
    Short name:
    SATUniRule annotation
    Gene namesi
    Name:MET3UniRule annotation
    Ordered Locus Names:YJR010W
    ORF Names:J1436
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome X

    Organism-specific databases

    CYGDiYJR010w.
    SGDiS000003771. MET3.

    Subcellular locationi

    Cytoplasm 1 PublicationUniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 511511Sulfate adenylyltransferasePRO_0000105954Add
    BLAST

    Proteomic databases

    MaxQBiP08536.
    PaxDbiP08536.
    PeptideAtlasiP08536.
    PRIDEiP08536.

    Expressioni

    Inductioni

    Expression depends on the formation of the MET4-MET28-MET31 and MET4-MET28-MET32 complexes on its 5' upstream region.1 Publication

    Gene expression databases

    GenevestigatoriP08536.

    Interactioni

    Subunit structurei

    Homohexamer. Dimer of trimers.2 PublicationsUniRule annotation

    Protein-protein interaction databases

    BioGridi33766. 14 interactions.
    DIPiDIP-4303N.
    IntActiP08536. 6 interactions.
    MINTiMINT-552009.
    STRINGi4932.YJR010W.

    Structurei

    Secondary structure

    1
    511
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi12 – 154
    Helixi17 – 193
    Helixi20 – 278
    Beta strandi32 – 365
    Helixi39 – 4911
    Turni51 – 555
    Helixi62 – 7110
    Beta strandi86 – 883
    Helixi90 – 945
    Beta strandi101 – 1066
    Turni107 – 1093
    Beta strandi110 – 12112
    Helixi125 – 1339
    Helixi140 – 1478
    Beta strandi151 – 16111
    Turni170 – 1723
    Helixi176 – 18510
    Beta strandi191 – 1944
    Helixi202 – 21413
    Beta strandi218 – 2214
    Helixi235 – 24511
    Helixi246 – 2483
    Beta strandi254 – 2563
    Helixi267 – 28014
    Beta strandi284 – 2885
    Turni290 – 2934
    Beta strandi303 – 3053
    Helixi309 – 32113
    Beta strandi324 – 3274
    Beta strandi331 – 3344
    Helixi335 – 3373
    Beta strandi339 – 3424
    Turni343 – 3453
    Beta strandi348 – 3503
    Helixi358 – 3669
    Turni373 – 3753
    Helixi378 – 3847
    Helixi391 – 3933
    Beta strandi396 – 4005
    Helixi408 – 41912
    Beta strandi428 – 4303
    Helixi437 – 4404
    Helixi443 – 4486
    Beta strandi452 – 4576
    Helixi461 – 4666
    Beta strandi472 – 4787
    Beta strandi482 – 4843
    Helixi492 – 50514

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1G8FX-ray1.95A1-511[»]
    1G8GX-ray2.60A/B1-511[»]
    1G8HX-ray2.80A/B1-511[»]
    1J70X-ray2.30A/B/C1-511[»]
    1JECX-ray2.50A2-511[»]
    1JEDX-ray2.95A/B2-511[»]
    1JEEX-ray2.80A/B2-511[»]
    1R6XX-ray1.40A2-393[»]
    ProteinModelPortaliP08536.
    SMRiP08536. Positions 1-511.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP08536.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 167167N-terminalAdd
    BLAST
    Regioni168 – 393226CatalyticAdd
    BLAST
    Regioni394 – 511118Required for oligomerization; adenylyl-sulfate kinase-likeAdd
    BLAST

    Domaini

    The oligomerization domain is distantly related to APS kinases, but it is not functional and does not bind APS. It is required for oligomerization of the enzyme, although the oligomerization state has no effect on the catalytic activity of the enzyme.2 PublicationsUniRule annotation

    Sequence similaritiesi

    Belongs to the sulfate adenylyltransferase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG2046.
    HOGENOMiHOG000069044.
    KOiK00958.
    OMAiPAVKYLF.
    OrthoDBiEOG7MWH5T.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    3.40.50.620. 1 hit.
    HAMAPiMF_03106. Sulf_adenylyltr_euk.
    InterProiIPR025980. ATP-Sase_PUA-like_dom.
    IPR027417. P-loop_NTPase.
    IPR015947. PUA-like_domain.
    IPR014729. Rossmann-like_a/b/a_fold.
    IPR027535. Sulf_adenylyltr_euk.
    IPR024951. Sulfurylase_cat_dom.
    IPR002650. Sulphate_adenylyltransferase.
    [Graphical view]
    PfamiPF01747. ATP-sulfurylase. 1 hit.
    PF14306. PUA_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    SSF88697. SSF88697. 1 hit.
    TIGRFAMsiTIGR00339. sopT. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P08536-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPAPHGGILQ DLIARDALKK NELLSEAQSS DILVWNLTPR QLCDIELILN    50
    GGFSPLTGFL NENDYSSVVT DSRLADGTLW TIPITLDVDE AFANQIKPDT 100
    RIALFQDDEI PIAILTVQDV YKPNKTIEAE KVFRGDPEHP AISYLFNVAG 150
    DYYVGGSLEA IQLPQHYDYP GLRKTPAQLR LEFQSRQWDR VVAFQTRNPM 200
    HRAHRELTVR AAREANAKVL IHPVVGLTKP GDIDHHTRVR VYQEIIKRYP 250
    NGIAFLSLLP LAMRMSGDRE AVWHAIIRKN YGASHFIVGR DHAGPGKNSK 300
    GVDFYGPYDA QELVESYKHE LDIEVVPFRM VTYLPDEDRY APIDQIDTTK 350
    TRTLNISGTE LRRRLRVGGE IPEWFSYPEV VKILRESNPP RPKQGFSIVL 400
    GNSLTVSREQ LSIALLSTFL QFGGGRYYKI FEHNNKTELL SLIQDFIGSG 450
    SGLIIPNQWE DDKDSVVGKQ NVYLLDTSSS ADIQLESADE PISHIVQKVV 500
    LFLEDNGFFV F 511
    Length:511
    Mass (Da):57,725
    Last modified:February 21, 2006 - v2
    Checksum:iA1E7B994A9C24DFD
    GO

    Sequence cautioni

    The sequence CAA29702.1 differs from that shown. Reason: Frameshift at position 492.
    The sequence CAA42726.1 differs from that shown. Reason: Frameshift at position 492.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti221 – 2211I → T in AAU09752. (PubMed:17322287)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X06413 Genomic DNA. Translation: CAA29702.1. Frameshift.
    X60157 Genomic DNA. Translation: CAA42726.1. Frameshift.
    X87611 Genomic DNA. Translation: CAA60932.1.
    Z49510 Genomic DNA. Translation: CAA89532.1.
    AY723835 Genomic DNA. Translation: AAU09752.1.
    BK006943 Genomic DNA. Translation: DAA08801.1.
    PIRiS55198.
    RefSeqiNP_012543.3. NM_001181668.3.

    Genome annotation databases

    EnsemblFungiiYJR010W; YJR010W; YJR010W.
    GeneIDi853466.
    KEGGisce:YJR010W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X06413 Genomic DNA. Translation: CAA29702.1 . Frameshift.
    X60157 Genomic DNA. Translation: CAA42726.1 . Frameshift.
    X87611 Genomic DNA. Translation: CAA60932.1 .
    Z49510 Genomic DNA. Translation: CAA89532.1 .
    AY723835 Genomic DNA. Translation: AAU09752.1 .
    BK006943 Genomic DNA. Translation: DAA08801.1 .
    PIRi S55198.
    RefSeqi NP_012543.3. NM_001181668.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1G8F X-ray 1.95 A 1-511 [» ]
    1G8G X-ray 2.60 A/B 1-511 [» ]
    1G8H X-ray 2.80 A/B 1-511 [» ]
    1J70 X-ray 2.30 A/B/C 1-511 [» ]
    1JEC X-ray 2.50 A 2-511 [» ]
    1JED X-ray 2.95 A/B 2-511 [» ]
    1JEE X-ray 2.80 A/B 2-511 [» ]
    1R6X X-ray 1.40 A 2-393 [» ]
    ProteinModelPortali P08536.
    SMRi P08536. Positions 1-511.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 33766. 14 interactions.
    DIPi DIP-4303N.
    IntActi P08536. 6 interactions.
    MINTi MINT-552009.
    STRINGi 4932.YJR010W.

    Proteomic databases

    MaxQBi P08536.
    PaxDbi P08536.
    PeptideAtlasi P08536.
    PRIDEi P08536.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YJR010W ; YJR010W ; YJR010W .
    GeneIDi 853466.
    KEGGi sce:YJR010W.

    Organism-specific databases

    CYGDi YJR010w.
    SGDi S000003771. MET3.

    Phylogenomic databases

    eggNOGi COG2046.
    HOGENOMi HOG000069044.
    KOi K00958.
    OMAi PAVKYLF.
    OrthoDBi EOG7MWH5T.

    Enzyme and pathway databases

    UniPathwayi UPA00140 ; UER00204 .
    BioCyci MetaCyc:MONOMER-362.
    YEAST:YJR010W-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P08536.
    NextBioi 974056.

    Gene expression databases

    Genevestigatori P08536.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    3.40.50.620. 1 hit.
    HAMAPi MF_03106. Sulf_adenylyltr_euk.
    InterProi IPR025980. ATP-Sase_PUA-like_dom.
    IPR027417. P-loop_NTPase.
    IPR015947. PUA-like_domain.
    IPR014729. Rossmann-like_a/b/a_fold.
    IPR027535. Sulf_adenylyltr_euk.
    IPR024951. Sulfurylase_cat_dom.
    IPR002650. Sulphate_adenylyltransferase.
    [Graphical view ]
    Pfami PF01747. ATP-sulfurylase. 1 hit.
    PF14306. PUA_2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    SSF88697. SSF88697. 1 hit.
    TIGRFAMsi TIGR00339. sopT. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The Saccharomyces cerevisiae MET3 gene: nucleotide sequence and relationship of the 5' non-coding region to that of MET25."
      Cherest H., Kerjan P., Surdin-Kerjan Y.
      Mol. Gen. Genet. 210:307-313(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: FL100A.
    2. "TDH2 is linked to MET3 on chromosome X of Saccharomyces cerevisiae."
      Mountain H.A., Korch C.
      Yeast 7:873-880(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. "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.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    6. "Multiple transcriptional activation complexes tether the yeast activator Met4 to DNA."
      Blaiseau P.L., Thomas D.
      EMBO J. 17:6327-6336(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    9. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Crystal structure of ATP sulfurylase from Saccharomyces cerevisiae, a key enzyme in sulfate activation."
      Ullrich T.C., Blaesse M., Huber R.
      EMBO J. 20:316-329(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS, SUBUNIT, DOMAIN, ACTIVE SITE.
      Strain: ATCC 96604 / S288c / FY1679.
    12. "Structural and functional analysis of a truncated form of Saccharomyces cerevisiae ATP sulfurylase: C-terminal domain essential for oligomer formation but not for activity."
      Lalor D.J., Schnyder T., Saridakis V., Pilloff D.E., Dong A., Tang H., Leyh T.S., Pai E.F.
      Protein Eng. 16:1071-1079(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 2-393 IN COMPLEX WITH SUBSTRATE ANALOGS, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DOMAIN, ACTIVE SITE.

    Entry informationi

    Entry nameiMET3_YEAST
    AccessioniPrimary (citable) accession number: P08536
    Secondary accession number(s): D6VWI5, Q66R66
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: February 21, 2006
    Last modified: October 1, 2014
    This is version 145 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 1510 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3