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Protein

Sulfate adenylyltransferase

Gene

MET3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

    Pathway: hydrogen sulfide biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes sulfite from sulfate.UniRule annotation
    Proteins known to be involved in the 3 steps of the subpathway in this organism are:
    1. Sulfate adenylyltransferase (MET3)
    2. Adenylyl-sulfate kinase (MET14)
    3. Phosphoadenosine phosphosulfate reductase (MET16)
    This subpathway is part of the pathway hydrogen sulfide biosynthesis, which is itself part of Sulfur metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes sulfite from sulfate, the pathway hydrogen sulfide biosynthesis and in Sulfur metabolism.

    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

    • ATP binding Source: UniProtKB-KW
    • sulfate adenylyltransferase (ATP) activity Source: SGD

    GO - Biological processi

    • cysteine biosynthetic process Source: UniProtKB-KW
    • hydrogen sulfide biosynthetic process Source: UniProtKB-UniPathway
    • methionine biosynthetic process Source: UniProtKB-KW
    • sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin) Source: SGD
    • sulfur amino acid metabolic process Source: SGD
    Complete GO annotation...

    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.
    BRENDAi2.7.7.4. 984.
    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 Componenti: Chromosome X

    Organism-specific databases

    CYGDiYJR010w.
    EuPathDBiFungiDB:YJR010W.
    SGDiS000003771. MET3.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    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

    Interactioni

    Subunit structurei

    Homohexamer. Dimer of trimers.UniRule annotation2 Publications

    Protein-protein interaction databases

    BioGridi33766. 17 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 – 154Combined sources
    Helixi17 – 193Combined sources
    Helixi20 – 278Combined sources
    Beta strandi32 – 365Combined sources
    Helixi39 – 4911Combined sources
    Turni51 – 555Combined sources
    Helixi62 – 7110Combined sources
    Beta strandi86 – 883Combined sources
    Helixi90 – 945Combined sources
    Beta strandi101 – 1066Combined sources
    Turni107 – 1093Combined sources
    Beta strandi110 – 12112Combined sources
    Helixi125 – 1339Combined sources
    Helixi140 – 1478Combined sources
    Beta strandi151 – 16111Combined sources
    Turni170 – 1723Combined sources
    Helixi176 – 18510Combined sources
    Beta strandi191 – 1944Combined sources
    Helixi202 – 21413Combined sources
    Beta strandi218 – 2214Combined sources
    Helixi235 – 24511Combined sources
    Helixi246 – 2483Combined sources
    Beta strandi254 – 2563Combined sources
    Helixi267 – 28014Combined sources
    Beta strandi284 – 2885Combined sources
    Turni290 – 2934Combined sources
    Beta strandi303 – 3053Combined sources
    Helixi309 – 32113Combined sources
    Beta strandi324 – 3274Combined sources
    Beta strandi331 – 3344Combined sources
    Helixi335 – 3373Combined sources
    Beta strandi339 – 3424Combined sources
    Turni343 – 3453Combined sources
    Beta strandi348 – 3503Combined sources
    Helixi358 – 3669Combined sources
    Turni373 – 3753Combined sources
    Helixi378 – 3847Combined sources
    Helixi391 – 3933Combined sources
    Beta strandi396 – 4005Combined sources
    Helixi408 – 41912Combined sources
    Beta strandi428 – 4303Combined sources
    Helixi437 – 4404Combined sources
    Helixi443 – 4486Combined sources
    Beta strandi452 – 4576Combined sources
    Helixi461 – 4666Combined sources
    Beta strandi472 – 4787Combined sources
    Beta strandi482 – 4843Combined sources
    Helixi492 – 50514Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    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.UniRule annotation2 Publications

    Sequence similaritiesi

    Belongs to the sulfate adenylyltransferase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG2046.
    HOGENOMiHOG000069044.
    InParanoidiP08536.
    KOiK00958.
    OMAiEHEFLQA.
    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

            10         20         30         40         50
    MPAPHGGILQ DLIARDALKK NELLSEAQSS DILVWNLTPR QLCDIELILN
    60 70 80 90 100
    GGFSPLTGFL NENDYSSVVT DSRLADGTLW TIPITLDVDE AFANQIKPDT
    110 120 130 140 150
    RIALFQDDEI PIAILTVQDV YKPNKTIEAE KVFRGDPEHP AISYLFNVAG
    160 170 180 190 200
    DYYVGGSLEA IQLPQHYDYP GLRKTPAQLR LEFQSRQWDR VVAFQTRNPM
    210 220 230 240 250
    HRAHRELTVR AAREANAKVL IHPVVGLTKP GDIDHHTRVR VYQEIIKRYP
    260 270 280 290 300
    NGIAFLSLLP LAMRMSGDRE AVWHAIIRKN YGASHFIVGR DHAGPGKNSK
    310 320 330 340 350
    GVDFYGPYDA QELVESYKHE LDIEVVPFRM VTYLPDEDRY APIDQIDTTK
    360 370 380 390 400
    TRTLNISGTE LRRRLRVGGE IPEWFSYPEV VKILRESNPP RPKQGFSIVL
    410 420 430 440 450
    GNSLTVSREQ LSIALLSTFL QFGGGRYYKI FEHNNKTELL SLIQDFIGSG
    460 470 480 490 500
    SGLIIPNQWE DDKDSVVGKQ NVYLLDTSSS ADIQLESADE PISHIVQKVV
    510
    LFLEDNGFFV F
    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. Curated
    The sequence CAA42726.1 differs from that shown. Reason: Frameshift at position 492. Curated

    Experimental Info

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

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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:
    EMBLi
    GenBanki
    DDBJi
    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.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    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...

    Protein-protein interaction databases

    BioGridi33766. 17 interactions.
    DIPiDIP-4303N.
    IntActiP08536. 6 interactions.
    MINTiMINT-552009.
    STRINGi4932.YJR010W.

    Proteomic databases

    MaxQBiP08536.
    PaxDbiP08536.
    PeptideAtlasiP08536.
    PRIDEiP08536.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    CYGDiYJR010w.
    EuPathDBiFungiDB:YJR010W.
    SGDiS000003771. MET3.

    Phylogenomic databases

    eggNOGiCOG2046.
    HOGENOMiHOG000069044.
    InParanoidiP08536.
    KOiK00958.
    OMAiEHEFLQA.
    OrthoDBiEOG7MWH5T.

    Enzyme and pathway databases

    UniPathwayiUPA00140; UER00204.
    BioCyciMetaCyc:MONOMER-362.
    YEAST:YJR010W-MONOMER.
    BRENDAi2.7.7.4. 984.

    Miscellaneous databases

    EvolutionaryTraceiP08536.
    NextBioi974056.
    PROiP08536.

    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.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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: June 24, 2015
    This is version 152 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.