HAMAP rule MF_03106
General rule information
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| Accession | MF_03106 |
| Dates | 14-AUG-2009 (Created)
24-MAY-2024 (Last updated, Version 13) |
| Name | Sulf_adenylyltr_euk |
| Scope(s) |
Eukaryota Fungi |
| Template(s) | P08536 (MET3_YEAST); Q12650 (MET3_PENCH); [ Recover all ] |
| Triggered by |
HAMAP; MF_03106 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| 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 | Name=MET3; |
Comments
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| 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 | Reaction=ATP + H(+) + sulfate = adenosine 5'-phosphosulfate + diphosphate; Xref=Rhea:RHEA:18133, ChEBI:CHEBI:15378, ChEBI:CHEBI:16189, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58243; 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. |
| SIMILARITY | 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
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| 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
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| GO:0004781; Molecular function:sulfate adenylyltransferase (ATP) activity |
| GO:0000103; Biological process:sulfate assimilation |
| GO:0070814; Biological process:hydrogen sulfide biosynthetic process |
| GO:0005737; Cellular component:cytoplasm |
Cross-references
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| Pfam | PF01747; ATP-sulfurylase; 1; |
| Pfam | PF01583; APS_kinase; 0-1; |
| NCBIfam | TIGR00339; sopT; 1; |
| NCBIfam | TIGR00455; apsK; 0-1; |
Features
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| 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 | /note="Transition state stabilizer" | H | ||||||||
| SITE | 204 | 204 | /note="Transition state stabilizer" | H | ||||||||
| SITE | 328 | 328 | /note="Induces change in substrate recognition on ATP binding" | F | ||||||||
| REGION | Nter | 167 | /note="N-terminal" | |||||||||
| REGION | 168 | 393 | /note="Catalytic" | |||||||||
| case not <IPRO:IPR002891> | ||||||||||||
| REGION | 394 | Cter | /note="Required for oligomerization; adenylyl-sulfate kinase-like" | |||||||||
| else | ||||||||||||
| From: MET3_PENCH (Q12650) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| REGION | 394 | Cter | /note="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
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| Size range | 490-581 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: None |