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Protein

Sulfate adenylyltransferase

Gene

met3

Organism
Penicillium chrysogenum (Penicillium notatum)
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

Enzyme regulationi

Allosterically inhibited by 3'-phosphoadenosine 5'-phosphosulfate (PAPS).

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
  3. no protein annotated in this organism
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 sitei198 – 1981
Active sitei199 – 1991
Active sitei200 – 2001
Sitei203 – 2031Transition state stabilizerUniRule annotation
Binding sitei206 – 2061SubstrateUniRule annotation1 Publication
Sitei206 – 2061Transition state stabilizerUniRule annotation
Sitei330 – 3301Induces change in substrate recognition on ATP bindingUniRule annotation
Binding sitei333 – 3331ATP; via amide nitrogen
Binding sitei356 – 3561SubstrateUniRule annotation1 Publication
Binding sitei357 – 3571Substrate; via carbonyl oxygenUniRule annotation1 Publication
Binding sitei433 – 4331APS
Binding sitei436 – 4361PAPS
Binding sitei450 – 4501PAPS
Binding sitei514 – 5141PAPS

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi196 – 2005ATP
Nucleotide bindingi291 – 2955ATP

GO - Molecular functioni

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

BRENDAi2.7.7.4. 4606.
SABIO-RKQ12650.
UniPathwayiUPA00140; UER00204.

Names & Taxonomyi

Protein namesi
Recommended name:
Sulfate adenylyltransferaseUniRule annotation (EC:2.7.7.4UniRule annotation)
Alternative name(s):
ATP-sulfurylaseUniRule annotation
Sulfate adenylate transferaseUniRule annotation
Short name:
SATUniRule annotation
Gene namesi
Name:met3
Synonyms:APS
OrganismiPenicillium chrysogenum (Penicillium notatum)
Taxonomic identifieri5076 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaePenicilliumPenicillium chrysogenum complex

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 572572Sulfate adenylyltransferasePRO_0000105951Add
BLAST

Proteomic databases

PRIDEiQ12650.

Interactioni

Subunit structurei

Homohexamer. Dimer of trimers.UniRule annotation2 Publications

Protein-protein interaction databases

STRINGi500485.XP_002563294.1.

Structurei

Secondary structure

1
572
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi13 – 164Combined sources
Helixi18 – 203Combined sources
Helixi21 – 288Combined sources
Beta strandi33 – 364Combined sources
Helixi38 – 4811Combined sources
Turni51 – 544Combined sources
Helixi61 – 7010Combined sources
Helixi89 – 946Combined sources
Beta strandi102 – 1076Combined sources
Turni108 – 1103Combined sources
Beta strandi113 – 1208Combined sources
Helixi127 – 1337Combined sources
Helixi142 – 1498Combined sources
Beta strandi153 – 1553Combined sources
Beta strandi158 – 1625Combined sources
Helixi172 – 1743Combined sources
Helixi178 – 18710Combined sources
Beta strandi192 – 1965Combined sources
Helixi204 – 21613Combined sources
Beta strandi220 – 2234Combined sources
Helixi235 – 24713Combined sources
Helixi248 – 2503Combined sources
Beta strandi255 – 2584Combined sources
Helixi269 – 28315Combined sources
Beta strandi286 – 2905Combined sources
Turni292 – 2954Combined sources
Beta strandi305 – 3073Combined sources
Helixi311 – 32313Combined sources
Beta strandi326 – 3294Combined sources
Beta strandi333 – 3364Combined sources
Turni337 – 3404Combined sources
Beta strandi345 – 3484Combined sources
Beta strandi350 – 3523Combined sources
Helixi359 – 36810Combined sources
Turni373 – 3753Combined sources
Helixi378 – 3858Combined sources
Turni391 – 3933Combined sources
Beta strandi396 – 4016Combined sources
Helixi408 – 42215Combined sources
Beta strandi427 – 4315Combined sources
Helixi432 – 4387Combined sources
Helixi447 – 46620Combined sources
Beta strandi470 – 4745Combined sources
Helixi480 – 49112Combined sources
Beta strandi494 – 5018Combined sources
Helixi505 – 5117Combined sources
Helixi516 – 5216Combined sources
Beta strandi524 – 5274Combined sources
Turni529 – 5313Combined sources
Beta strandi542 – 5454Combined sources
Turni547 – 5493Combined sources
Helixi552 – 56514Combined sources
Turni566 – 5694Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1I2DX-ray2.81A/B/C1-572[»]
1M8PX-ray2.60A/B/C1-572[»]
ProteinModelPortaliQ12650.
SMRiQ12650. Positions 1-572.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ12650.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 169169N-terminalAdd
BLAST
Regioni170 – 393224CatalyticAdd
BLAST
Regioni394 – 572179Allosteric regulation domain; adenylyl-sulfate kinase-likeAdd
BLAST

Domaini

The adenylyl-sulfate kinase (APS kinase) is non-functional. It is involved in allosteric regulation by PAPS. PAPS binding induces a large rotational rearrangement of domains lowering the substrate affinity of the enzyme.

Sequence similaritiesi

In the N-terminal section; belongs to the sulfate adenylyltransferase family.UniRule annotation
In the C-terminal section; belongs to the APS kinase family.UniRule annotation

Phylogenomic databases

eggNOGiKOG0636. Eukaryota.
COG2046. LUCA.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
3.40.50.620. 1 hit.
HAMAPiMF_03106. Sulf_adenylyltr_euk.
InterProiIPR002891. APS_kinase.
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]
PfamiPF01747. ATP-sulfurylase. 1 hit.
PF14306. PUA_2. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
SSF88697. SSF88697. 1 hit.
TIGRFAMsiTIGR00455. apsK. 1 hit.
TIGR00339. sopT. 1 hit.

Sequencei

Sequence statusi: Complete.

Q12650-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANAPHGGVL KDLLARDAPR QAELAAEAES LPAVTLTERQ LCDLELIMNG
60 70 80 90 100
GFSPLEGFMN QADYDRVCED NRLADGNVFS MPITLDASQE VIDEKKLQAA
110 120 130 140 150
SRITLRDFRD DRNLAILTID DIYRPDKTKE AKLVFGGDPE HPAIVYLNNT
160 170 180 190 200
VKEFYIGGKI EAVNKLNHYD YVALRYTPAE LRVHFDKLGW SRVVAFQTRN
210 220 230 240 250
PMHRAHRELT VRAARSRQAN VLIHPVVGLT KPGDIDHFTR VRAYQALLPR
260 270 280 290 300
YPNGMAVLGL LGLAMRMGGP REAIWHAIIR KNHGATHFIV GRDHAGPGSN
310 320 330 340 350
SKGEDFYGPY DAQHAVEKYK DELGIEVVEF QMVTYLPDTD EYRPVDQVPA
360 370 380 390 400
GVKTLNISGT ELRRRLRSAH IPEWFSYPEV VKILRESNPP RATQGFTIFL
410 420 430 440 450
TGYMNSGKDA IARALQVTLN QQGGRSVSLL LGDTVRHELS SELGFTREDR
460 470 480 490 500
HTNIQRIAFV ATELTRAGAA VIAAPIAPYE ESRKFARDAV SQAGSFFLVH
510 520 530 540 550
VATPLEHCEQ SDKRGIYAAA RRGEIKGFTG VDDPYETPEK ADLVVDFSKQ
560 570
SVRSIVHEII LVLESQGFLE RQ
Length:572
Mass (Da):63,917
Last modified:November 1, 1996 - v1
Checksum:i4C921D76FD1988E1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U07353 mRNA. Translation: AAA20839.1.
PIRiA59274. A53651.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U07353 mRNA. Translation: AAA20839.1.
PIRiA59274. A53651.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1I2DX-ray2.81A/B/C1-572[»]
1M8PX-ray2.60A/B/C1-572[»]
ProteinModelPortaliQ12650.
SMRiQ12650. Positions 1-572.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi500485.XP_002563294.1.

Proteomic databases

PRIDEiQ12650.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG0636. Eukaryota.
COG2046. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00140; UER00204.
BRENDAi2.7.7.4. 4606.
SABIO-RKQ12650.

Miscellaneous databases

EvolutionaryTraceiQ12650.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
3.40.50.620. 1 hit.
HAMAPiMF_03106. Sulf_adenylyltr_euk.
InterProiIPR002891. APS_kinase.
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]
PfamiPF01747. ATP-sulfurylase. 1 hit.
PF14306. PUA_2. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
SSF88697. SSF88697. 1 hit.
TIGRFAMsiTIGR00455. apsK. 1 hit.
TIGR00339. sopT. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Cloning and sequencing of ATP sulfurylase from Penicillium chrysogenum. Identification of a likely allosteric domain."
    Foster B.A., Thomas S.M., Mahr J.A., Renosto F., Patel H.C., Segel I.H.
    J. Biol. Chem. 269:19777-19786(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Strain: ATCC 24791 / PS-75.
  2. "The 'regulatory' sulfhydryl group of Penicillium chrysogenum ATP sulfurylase. Cooperative ligand binding after SH modification; chemical and thermodynamic properties."
    Martin R.L., Daley L.A., Lovric Z., Wailes L.M., Renosto F., Segel I.H.
    J. Biol. Chem. 264:11768-11775(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 487-517.
  3. "Crystal structure of ATP sulfurylase from Penicillium chrysogenum: insights into the allosteric regulation of sulfate assimilation."
    MacRae I.J., Segel I.H., Fisher A.J.
    Biochemistry 40:6795-6804(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND ALLOSTERIC INHIBITOR.
  4. "Allosteric inhibition via R-state destabilization in ATP sulfurylase from Penicillium chrysogenum."
    MacRae I.J., Segel I.H., Fisher A.J.
    Nat. Struct. Biol. 9:945-949(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH ALLOSTERIC INHIBITOR.

Entry informationi

Entry nameiMET3_PENCH
AccessioniPrimary (citable) accession number: Q12650
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: May 11, 2016
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Allosteric enzyme, Direct protein sequencing

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

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.