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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), Sulfate adenylyltransferase (met3)
  2. Adenylyl-sulfate kinase, Adenylyl-sulfate kinase (EN45_032050)
  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)DescriptionActionsGraphical viewLength
Active sitei1981
Active sitei1991
Active sitei2001
Sitei203Transition state stabilizerUniRule annotation1
Binding sitei206SubstrateUniRule annotation1 Publication1
Sitei206Transition state stabilizerUniRule annotation1
Sitei330Induces change in substrate recognition on ATP bindingUniRule annotation1
Binding sitei333ATP; via amide nitrogen1
Binding sitei356SubstrateUniRule annotation1 Publication1
Binding sitei357Substrate; via carbonyl oxygenUniRule annotation1 Publication1
Binding sitei433APS1
Binding sitei436PAPS1
Binding sitei450PAPS1
Binding sitei514PAPS1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi196 – 200ATP5
Nucleotide bindingi291 – 295ATP5

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)DescriptionActionsGraphical viewLength
ChainiPRO_00001059511 – 572Sulfate adenylyltransferaseAdd BLAST572

Proteomic databases

PRIDEiQ12650.

Interactioni

Subunit structurei

Homohexamer. Dimer of trimers.UniRule annotation2 Publications

Protein-protein interaction databases

STRINGi500485.XP_002563294.1.

Structurei

Secondary structure

1572
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi13 – 16Combined sources4
Helixi18 – 20Combined sources3
Helixi21 – 28Combined sources8
Beta strandi33 – 36Combined sources4
Helixi38 – 48Combined sources11
Turni51 – 54Combined sources4
Helixi61 – 70Combined sources10
Helixi89 – 94Combined sources6
Beta strandi102 – 107Combined sources6
Turni108 – 110Combined sources3
Beta strandi113 – 120Combined sources8
Helixi127 – 133Combined sources7
Helixi142 – 149Combined sources8
Beta strandi153 – 155Combined sources3
Beta strandi158 – 162Combined sources5
Helixi172 – 174Combined sources3
Helixi178 – 187Combined sources10
Beta strandi192 – 196Combined sources5
Helixi204 – 216Combined sources13
Beta strandi220 – 223Combined sources4
Helixi235 – 247Combined sources13
Helixi248 – 250Combined sources3
Beta strandi255 – 258Combined sources4
Helixi269 – 283Combined sources15
Beta strandi286 – 290Combined sources5
Turni292 – 295Combined sources4
Beta strandi305 – 307Combined sources3
Helixi311 – 323Combined sources13
Beta strandi326 – 329Combined sources4
Beta strandi333 – 336Combined sources4
Turni337 – 340Combined sources4
Beta strandi345 – 348Combined sources4
Beta strandi350 – 352Combined sources3
Helixi359 – 368Combined sources10
Turni373 – 375Combined sources3
Helixi378 – 385Combined sources8
Turni391 – 393Combined sources3
Beta strandi396 – 401Combined sources6
Helixi408 – 422Combined sources15
Beta strandi427 – 431Combined sources5
Helixi432 – 438Combined sources7
Helixi447 – 466Combined sources20
Beta strandi470 – 474Combined sources5
Helixi480 – 491Combined sources12
Beta strandi494 – 501Combined sources8
Helixi505 – 511Combined sources7
Helixi516 – 521Combined sources6
Beta strandi524 – 527Combined sources4
Turni529 – 531Combined sources3
Beta strandi542 – 545Combined sources4
Turni547 – 549Combined sources3
Helixi552 – 565Combined sources14
Turni566 – 569Combined sources4

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ12650.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 169N-terminalAdd BLAST169
Regioni170 – 393CatalyticAdd BLAST224
Regioni394 – 572Allosteric regulation domain; adenylyl-sulfate kinase-likeAdd BLAST179

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

CDDicd02027. APSK. 1 hit.
cd00517. ATPS. 1 hit.
Gene3Di3.40.50.300. 1 hit.
3.40.50.620. 1 hit.
HAMAPiMF_03106. Sulf_adenylyltr_euk. 1 hit.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1I2DX-ray2.81A/B/C1-572[»]
1M8PX-ray2.60A/B/C1-572[»]
ProteinModelPortaliQ12650.
SMRiQ12650.
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

CDDicd02027. APSK. 1 hit.
cd00517. ATPS. 1 hit.
Gene3Di3.40.50.300. 1 hit.
3.40.50.620. 1 hit.
HAMAPiMF_03106. Sulf_adenylyltr_euk. 1 hit.
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...

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: November 2, 2016
This is version 103 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.