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HAMAP rule MF_03106

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General rule information [?]

Accession MF_03106
Dates 14-AUG-2009 (Created)
1-JUN-2023 (Last updated, Version 12)
Name Sulf_adenylyltr_euk
Scope
Eukaryota; Fungi
Templates P08536 (MET3_YEAST); Q12650 (MET3_PENCH): [Recover all]
Triggered by

Propagated annotation [?]


Identifier, protein and gene names [?]

Identifier
MET3
case <OC:Saccharomyces>
Protein name
RecName: Full=Sulfate adenylyltransferase;
EC 2.7.7.4;
AltName: Full=ATP-sulfurylase;
AltName: Full=Methionine-requiring protein 3;
AltName: Full=Sulfate adenylate transferase;
Short=SAT;
else
Protein name
RecName: Full=Sulfate adenylyltransferase;
EC 2.7.7.4;
AltName: Full=ATP-sulfurylase;
AltName: Full=Sulfate adenylate transferase;
Short=SAT;
end case
Gene name
MET3

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.
Catalytic activity RHEA:18133: ATP + H(+) + sulfate = adenosine 5'-phosphosulfate + diphosphate
EC 2.7.7.4
Pathway Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 1/3.
Subunit Homohexamer. Dimer of trimers.
Subcellular location Cytoplasm.
case <IPRO:IPR002891>
Activity regulation Allosterically inhibited by 3'-phosphoadenosine 5'-phosphosulfate (PAPS).
Domain 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.
Similarity In the N-terminal section; belongs to the sulfate adenylyltransferase family.
In the C-terminal section; belongs to the APS kinase family.
else
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.
Similarity Belongs to the sulfate adenylyltransferase family.
end case

Keywords [?]

Cytoplasm
Amino-acid biosynthesis
ATP-binding
Cysteine biosynthesis
Methionine biosynthesis
Nucleotide-binding
Nucleotidyltransferase
Transferase
case <IPRO:IPR002891>
Allosteric enzyme
end case
case <OC:Saccharomyces>
Phosphoprotein
end case

Gene Ontology [?]

GO:0004781; Molecular function: sulfate adenylyltransferase (ATP) activity.
GO:0000103; Biological process: sulfate assimilation.
GO:0005737; Cellular component: cytoplasm.

Cross-references [?]

Pfam PF01747; ATP-sulfurylase; 1;
PF01583; APS_kinase; 0-1;
NCBIfam TIGR00339; sopT; 1;
TIGR00455; apsK; 0-1;

Features [?]

From: MET3_YEAST (P08536)
Key     From     To       Description   Tag   Condition   FTGroup
BINDING     195     198       /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616     Q-T-R-N  
BINDING     289     292       /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616     G-R-D-H  
ACT_SITE     196     196             T  
ACT_SITE     197     197             R  
ACT_SITE     198     198             N  
BINDING     195     195       /ligand="sulfate" /ligand_id="ChEBI:CHEBI:16189     Q  
BINDING     197     197       /ligand="sulfate" /ligand_id="ChEBI:CHEBI:16189     R  
BINDING     293     293       /ligand="sulfate" /ligand_id="ChEBI:CHEBI:16189     A  
BINDING     331     331       /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616     [MILV]  
SITE     201     201       Transition state stabilizer     H  
SITE     204     204       Transition state stabilizer     H  
SITE     328     328       Induces change in substrate recognition on ATP binding     F  
REGION     Nter     167       N-terminal        
REGION     168     393       Catalytic        
case not <IPRO:IPR002891>
REGION     394     Cter       Required for oligomerization; adenylyl-sulfate kinase-like        
else
From: MET3_PENCH (Q12650)
REGION     394     Cter       Allosteric regulation domain; adenylyl-sulfate kinase-like        
BINDING     433     436       /ligand="3'-phosphoadenylyl sulfate" /ligand_id="ChEBI:CHEBI:58339" /ligand_note="allosteric inhibitor     [DE]-x(2)-R  
BINDING     476     477       /ligand="3'-phosphoadenylyl sulfate" /ligand_id="ChEBI:CHEBI:58339" /ligand_note="allosteric inhibitor     [IT]-A  
BINDING     450     450       /ligand="3'-phosphoadenylyl sulfate" /ligand_id="ChEBI:CHEBI:58339" /ligand_note="allosteric inhibitor     R  
BINDING     514     514       /ligand="3'-phosphoadenylyl sulfate" /ligand_id="ChEBI:CHEBI:58339" /ligand_note="allosteric inhibitor     [RK]  
end case

Additional information [?]

Size range 490-581 amino acids
Related rules None
Fusion None


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