P08536 (MET3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	511 AA.
Sequence status	Complete.
Protein existence	Evidence 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. HAMAP-Rule MF_03106
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.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Cysteine biosynthesis Methionine biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Nucleotidyltransferase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cysteine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW hydrogen sulfide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway methionine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin) Inferred from mutant phenotype PubMed 197388. Source: SGD sulfur amino acid metabolic process Inferred from mutant phenotype PubMed 1101032. Source: SGD
Cellular_component	mitochondrion Inferred from direct assay PubMed 14576278PubMed 16823961. Source: SGD
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW sulfate adenylyltransferase (ATP) activity Inferred from direct assay PubMed 10092498. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 511

511

Sulfate adenylyltransferase HAMAP-Rule MF_03106

PRO_0000105954

Regions

Nucleotide binding

194 – 198

5

ATP HAMAP-Rule MF_03106

Nucleotide binding

289 – 293

5

ATP HAMAP-Rule MF_03106

Region

1 – 167

167

N-terminal HAMAP-Rule MF_03106

Region

168 – 393

226

Catalytic HAMAP-Rule MF_03106

Region

394 – 511

118

Required for oligomerization; adenylyl-sulfate kinase-like HAMAP-Rule MF_03106

Sites

Active site

196

1

Ref.11 Ref.12

Active site

197

1

Ref.11 Ref.12

Active site

198

1

Ref.11 Ref.12

Binding site

204

1

Substrate

Binding site

331

1

ATP; via amide nitrogen

Binding site

355

1

Substrate

Binding site

356

1

Substrate; via carbonyl oxygen

Site

201

1

Transition state stabilizer

Site

204

1

Transition state stabilizer

Site

328

1

Induces change in substrate recognition on ATP binding

Amino acid modifications

Modified residue

126

1

Phosphothreonine Ref.9

Modified residue

359

1

Phosphothreonine Ref.10

Experimental info

Sequence conflict

221

1

I → T in AAU09752. Ref.5

Secondary structure

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511

Helix Strand Turn

Details...

Helix

12 – 15

4

Helix

17 – 19

3

Helix

20 – 27

8

Beta strand

32 – 36

5

Helix

39 – 49

11

Turn

51 – 55

5

Helix

62 – 71

10

Beta strand

86 – 88

3

Helix

90 – 94

5

Beta strand

101 – 106

6

Turn

107 – 109

3

Beta strand

110 – 121

12

Helix

125 – 133

9

Helix

140 – 147

8

Beta strand

151 – 161

11

Turn

170 – 172

3

Helix

176 – 185

10

Beta strand

191 – 194

4

Helix

202 – 214

13

Beta strand

218 – 221

4

Helix

235 – 245

11

Helix

246 – 248

3

Beta strand

254 – 256

3

Helix

267 – 280

14

Beta strand

284 – 288

5

Turn

290 – 293

4

Beta strand

303 – 305

3

Helix

309 – 321

13

Beta strand

324 – 327

4

Beta strand

331 – 334

4

Helix

335 – 337

3

Beta strand

339 – 342

4

Turn

343 – 345

3

Beta strand

348 – 350

3

Helix

358 – 366

9

Turn

373 – 375

3

Helix

378 – 384

7

Helix

391 – 393

3

Beta strand

396 – 400

5

Helix

408 – 419

12

Beta strand

428 – 430

3

Helix

437 – 440

4

Helix

443 – 448

6

Beta strand

452 – 457

6

Helix

461 – 466

6

Beta strand

472 – 478

7

Beta strand

482 – 484

3

Helix

492 – 505

14

Sequences

	Sequence		Length	Mass (Da)
	P08536 [UniParc]. Last modified February 21, 2006. Version 2. Checksum: A1E7B994A9C24DFD	FASTA	511	57,725
	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

References

	« Hide 'large scale' referencesShow '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. , 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 96604 / S288c / FY1679.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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. , 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]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-126, MASS SPECTROMETRY. Strain: YAL6B.
[10]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-359, MASS SPECTROMETRY.
[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.

PIR

S55198.

RefSeq

NP_012543.3. NM_001181668.3.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P08536.

SMR

P08536. Positions 1-511.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-4303N.

IntAct

P08536. 6 interactions.

MINT

MINT-552009.

STRING

4932.YJR010W.

Proteomic databases

PaxDb

P08536.

PeptideAtlas

P08536.

PRIDE

P08536.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YJR010W; YJR010W; YJR010W.

GeneID

853466.

KEGG

sce:YJR010W.
sce:YJR012C.

Organism-specific databases

CYGD

YJR010w.

SGD

S000003771. MET3.

Phylogenomic databases

eggNOG

COG2046.

HOGENOM

HOG000069044.

KO

K00958.

OMA

RIRWAYL.

OrthoDB

EOG4B8NNH.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-362.

UniPathway

UPA00140; UER00204.

Gene expression databases

Genevestigator

P08536.

GermOnline

YJR010W. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

3.40.50.620. 1 hit.

HAMAP

MF_03106. Sulf_adenylyltr_euk.

InterPro

IPR025980. ATP-Sase_PUA-like_dom.
IPR015947. PUA-like_domain.
IPR014729. Rossmann-like_a/b/a_fold.
IPR024951. Sulfurylase_cat_dom.
IPR002650. Sulphate_adenylyltransferase.
[Graphical view]

Pfam

PF01747. ATP-sulfurylase. 1 hit.
PF14306. PUA_2. 1 hit.
[Graphical view]

SUPFAM

SSF88697. PUA-like. 1 hit.

TIGRFAMs

TIGR00339. sopT. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P08536.

NextBio

974056.

Entry information

Entry name

MET3_YEAST

Accession

Primary (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:	April 3, 2013
This is version 135 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program