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P08536

- MET3_YEAST

UniProt

P08536 - MET3_YEAST

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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

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
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.
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-HAMAP
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

Gene expression databases

GenevestigatoriP08536.

Interactioni

Subunit structurei

Homohexamer. Dimer of trimers.2 PublicationsUniRule annotation

Protein-protein interaction databases

BioGridi33766. 15 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.2 PublicationsUniRule annotation

Sequence similaritiesi

Belongs to the sulfate adenylyltransferase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG2046.
HOGENOMiHOG000069044.
InParanoidiP08536.
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

        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 .
PIRi S55198.
RefSeqi NP_012543.3. NM_001181668.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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. 15 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.
InParanoidi P08536.
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

« 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: November 26, 2014
This is version 147 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