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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

    Pathwayi: 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)DescriptionActionsGraphical viewLength
    Active sitei1961
    Active sitei1971
    Active sitei1981
    Sitei201Transition state stabilizer1
    Binding sitei204Substrate1
    Sitei204Transition state stabilizer1
    Sitei328Induces change in substrate recognition on ATP binding1
    Binding sitei331ATP; via amide nitrogen1
    Binding sitei355Substrate1
    Binding sitei356Substrate; via carbonyl oxygen1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi194 – 198ATP5
    Nucleotide bindingi289 – 293ATP5

    GO - Molecular functioni

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

    GO - Biological processi

    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:YJR010W-MONOMER.
    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
    Proteomesi
    • UP000002311 Componenti: Chromosome X

    Organism-specific databases

    EuPathDBiFungiDB:YJR010W.
    SGDiS000003771. MET3.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001059541 – 511Sulfate adenylyltransferaseAdd BLAST511

    Proteomic databases

    MaxQBiP08536.
    PRIDEiP08536.
    TopDownProteomicsiP08536.

    PTM databases

    iPTMnetiP08536.

    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. 16 interactors.
    DIPiDIP-4303N.
    IntActiP08536. 6 interactors.
    MINTiMINT-552009.

    Structurei

    Secondary structure

    1511
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi12 – 15Combined sources4
    Helixi17 – 19Combined sources3
    Helixi20 – 27Combined sources8
    Beta strandi32 – 36Combined sources5
    Helixi39 – 49Combined sources11
    Turni51 – 55Combined sources5
    Helixi62 – 71Combined sources10
    Beta strandi86 – 88Combined sources3
    Helixi90 – 94Combined sources5
    Beta strandi101 – 106Combined sources6
    Turni107 – 109Combined sources3
    Beta strandi110 – 121Combined sources12
    Helixi125 – 133Combined sources9
    Helixi140 – 147Combined sources8
    Beta strandi151 – 161Combined sources11
    Turni170 – 172Combined sources3
    Helixi176 – 185Combined sources10
    Beta strandi191 – 194Combined sources4
    Helixi202 – 214Combined sources13
    Beta strandi218 – 221Combined sources4
    Helixi235 – 245Combined sources11
    Helixi246 – 248Combined sources3
    Beta strandi254 – 256Combined sources3
    Helixi267 – 280Combined sources14
    Beta strandi284 – 288Combined sources5
    Turni290 – 293Combined sources4
    Beta strandi303 – 305Combined sources3
    Helixi309 – 321Combined sources13
    Beta strandi324 – 327Combined sources4
    Beta strandi331 – 334Combined sources4
    Helixi335 – 337Combined sources3
    Beta strandi339 – 342Combined sources4
    Turni343 – 345Combined sources3
    Beta strandi348 – 350Combined sources3
    Helixi358 – 366Combined sources9
    Turni373 – 375Combined sources3
    Helixi378 – 384Combined sources7
    Helixi391 – 393Combined sources3
    Beta strandi396 – 400Combined sources5
    Helixi408 – 419Combined sources12
    Beta strandi428 – 430Combined sources3
    Helixi437 – 440Combined sources4
    Helixi443 – 448Combined sources6
    Beta strandi452 – 457Combined sources6
    Helixi461 – 466Combined sources6
    Beta strandi472 – 478Combined sources7
    Beta strandi482 – 484Combined sources3
    Helixi492 – 505Combined sources14

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP08536.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni1 – 167N-terminalAdd BLAST167
    Regioni168 – 393CatalyticAdd BLAST226
    Regioni394 – 511Required for oligomerization; adenylyl-sulfate kinase-likeAdd BLAST118

    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

    HOGENOMiHOG000069044.
    InParanoidiP08536.
    KOiK00958.
    OMAiLQHMIIR.
    OrthoDBiEOG092C20R5.

    Family and domain databases

    CDDicd00517. ATPS. 1 hit.
    Gene3Di3.40.50.300. 1 hit.
    3.40.50.620. 1 hit.
    HAMAPiMF_03106. Sulf_adenylyltr_euk. 1 hit.
    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 differs from that shown. Reason: Frameshift at position 492.Curated
    The sequence CAA42726 differs from that shown. Reason: Frameshift at position 492.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti221I → T in AAU09752 (PubMed:17322287).Curated1

    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
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi33766. 16 interactors.
    DIPiDIP-4303N.
    IntActiP08536. 6 interactors.
    MINTiMINT-552009.

    PTM databases

    iPTMnetiP08536.

    Proteomic databases

    MaxQBiP08536.
    PRIDEiP08536.
    TopDownProteomicsiP08536.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    EuPathDBiFungiDB:YJR010W.
    SGDiS000003771. MET3.

    Phylogenomic databases

    HOGENOMiHOG000069044.
    InParanoidiP08536.
    KOiK00958.
    OMAiLQHMIIR.
    OrthoDBiEOG092C20R5.

    Enzyme and pathway databases

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

    Miscellaneous databases

    EvolutionaryTraceiP08536.
    PROiP08536.

    Family and domain databases

    CDDicd00517. ATPS. 1 hit.
    Gene3Di3.40.50.300. 1 hit.
    3.40.50.620. 1 hit.
    HAMAPiMF_03106. Sulf_adenylyltr_euk. 1 hit.
    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...

    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: November 30, 2016
    This is version 165 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

    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 one 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.