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P08536 (MET3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sulfate adenylyltransferase

EC=2.7.7.4
Alternative name(s):
ATP-sulfurylase
Methionine-requiring protein 3
Sulfate adenylate transferase
Short name=SAT
Gene names
Name:MET3
Ordered Locus Names:YJR010W
ORF Names:J1436
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length511 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. HAMAP-Rule MF_03106

Catalytic activity

ATP + sulfate = diphosphate + adenylyl sulfate. HAMAP-Rule MF_03106

Pathway

Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 1/3. HAMAP-Rule MF_03106

Subunit structure

Homohexamer. Dimer of trimers. Ref.11 Ref.12

Subcellular location

Cytoplasm Ref.7.

Induction

Expression depends on the formation of the MET4-MET28-MET31 and MET4-MET28-MET32 complexes on its 5' upstream region. Ref.6

Domain

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. Ref.11 Ref.12

Miscellaneous

Present with 1510 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the sulfate adenylyltransferase family.

Biophysicochemical properties

Kinetic parameters:

KM=0.65 mM for Sulfate Ref.12

KM=0.082 mM for ATP

Sequence caution

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 511511Sulfate adenylyltransferase HAMAP-Rule MF_03106
PRO_0000105954

Regions

Nucleotide binding194 – 1985ATP HAMAP-Rule MF_03106
Nucleotide binding289 – 2935ATP HAMAP-Rule MF_03106
Region1 – 167167N-terminal HAMAP-Rule MF_03106
Region168 – 393226Catalytic HAMAP-Rule MF_03106
Region394 – 511118Required for oligomerization; adenylyl-sulfate kinase-like HAMAP-Rule MF_03106

Sites

Active site1961 Ref.11 Ref.12
Active site1971 Ref.11 Ref.12
Active site1981 Ref.11 Ref.12
Binding site2041Substrate
Binding site3311ATP; via amide nitrogen
Binding site3551Substrate
Binding site3561Substrate; via carbonyl oxygen
Site2011Transition state stabilizer
Site2041Transition state stabilizer
Site3281Induces change in substrate recognition on ATP binding

Experimental info

Sequence conflict2211I → T in AAU09752. Ref.5

Secondary structure

........................................................................................... 511
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P08536 [UniParc].

Last modified February 21, 2006. Version 2.
Checksum: A1E7B994A9C24DFD

FASTA51157,725
        10         20         30         40         50         60 
MPAPHGGILQ DLIARDALKK NELLSEAQSS DILVWNLTPR QLCDIELILN GGFSPLTGFL 

        70         80         90        100        110        120 
NENDYSSVVT DSRLADGTLW TIPITLDVDE AFANQIKPDT RIALFQDDEI PIAILTVQDV 

       130        140        150        160        170        180 
YKPNKTIEAE KVFRGDPEHP AISYLFNVAG DYYVGGSLEA IQLPQHYDYP GLRKTPAQLR 

       190        200        210        220        230        240 
LEFQSRQWDR VVAFQTRNPM HRAHRELTVR AAREANAKVL IHPVVGLTKP GDIDHHTRVR 

       250        260        270        280        290        300 
VYQEIIKRYP NGIAFLSLLP LAMRMSGDRE AVWHAIIRKN YGASHFIVGR DHAGPGKNSK 

       310        320        330        340        350        360 
GVDFYGPYDA QELVESYKHE LDIEVVPFRM VTYLPDEDRY APIDQIDTTK TRTLNISGTE 

       370        380        390        400        410        420 
LRRRLRVGGE IPEWFSYPEV VKILRESNPP RPKQGFSIVL GNSLTVSREQ LSIALLSTFL 

       430        440        450        460        470        480 
QFGGGRYYKI FEHNNKTELL SLIQDFIGSG SGLIIPNQWE DDKDSVVGKQ NVYLLDTSSS 

       490        500        510 
ADIQLESADE PISHIVQKVV LFLEDNGFFV F 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
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]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[8]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS55198.
RefSeqNP_012543.3. NM_001181668.3.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP08536.
SMRP08536. Positions 1-511.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33766. 14 interactions.
DIPDIP-4303N.
IntActP08536. 6 interactions.
MINTMINT-552009.
STRING4932.YJR010W.

Proteomic databases

MaxQBP08536.
PaxDbP08536.
PeptideAtlasP08536.
PRIDEP08536.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYJR010W; YJR010W; YJR010W.
GeneID853466.
KEGGsce:YJR010W.

Organism-specific databases

CYGDYJR010w.
SGDS000003771. MET3.

Phylogenomic databases

eggNOGCOG2046.
HOGENOMHOG000069044.
KOK00958.
OMAPAVKYLF.
OrthoDBEOG7MWH5T.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-362.
YEAST:YJR010W-MONOMER.
UniPathwayUPA00140; UER00204.

Gene expression databases

GenevestigatorP08536.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
3.40.50.620. 1 hit.
HAMAPMF_03106. Sulf_adenylyltr_euk.
InterProIPR025980. 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]
PfamPF01747. ATP-sulfurylase. 1 hit.
PF14306. PUA_2. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
SSF88697. SSF88697. 1 hit.
TIGRFAMsTIGR00339. sopT. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP08536.
NextBio974056.

Entry information

Entry nameMET3_YEAST
AccessionPrimary (citable) accession number: P08536
Secondary accession number(s): D6VWI5, Q66R66
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: February 21, 2006
Last modified: May 14, 2014
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome X

Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways