AC   MF_03106;
DC   Protein; auto
TR   HAMAP; MF_03106; -; 1; level=0
XX
Names: Sulf_adenylyltr_euk
XX
ID   MET3
case <OC:Saccharomyces>
DE   RecName: Full=Sulfate adenylyltransferase;
DE            EC=2.7.7.4;
DE   AltName: Full=ATP-sulfurylase;
DE   AltName: Full=Methionine-requiring protein 3;
DE   AltName: Full=Sulfate adenylate transferase;
DE            Short=SAT;
else
DE   RecName: Full=Sulfate adenylyltransferase;
DE            EC=2.7.7.4;
DE   AltName: Full=ATP-sulfurylase;
DE   AltName: Full=Sulfate adenylate transferase;
DE            Short=SAT;
end case
GN   Name=MET3;
XX
CC   -!- FUNCTION: Catalyzes the first intracellular reaction of sulfate
CC       assimilation, forming adenosine-5'-phosphosulfate (APS) from inorganic
CC       sulfate and ATP. Plays an important role in sulfate activation as a
CC       component of the biosynthesis pathway of sulfur-containing amino acids.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H(+) + sulfate = adenosine 5'-phosphosulfate +
CC         diphosphate; Xref=Rhea:RHEA:18133, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16189, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58243; EC=2.7.7.4;
CC   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC       sulfate: step 1/3.
CC   -!- SUBUNIT: Homohexamer. Dimer of trimers.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
case <IPRO:IPR002891>
CC   -!- ACTIVITY REGULATION: Allosterically inhibited by 3'-phosphoadenosine
CC       5'-phosphosulfate (PAPS).
CC   -!- DOMAIN: The adenylyl-sulfate kinase (APS kinase) is non-functional. It
CC       is involved in allosteric regulation by PAPS. PAPS binding induces a
CC       large rotational rearrangement of domains lowering the substrate
CC       affinity of the enzyme.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the sulfate
CC       adenylyltransferase family.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the APS kinase
CC       family.
else
CC   -!- DOMAIN: The oligomerization domain is distantly related to APS kinases,
CC       but it is not functional and does not bind APS. It is required for
CC       oligomerization of the enzyme, although the oligomerization state has
CC       no effect on the catalytic activity of the enzyme.
CC   -!- SIMILARITY: Belongs to the sulfate adenylyltransferase family.
end case
XX
DR   Pfam; PF01747; ATP-sulfurylase; 1; trigger=no
DR   Pfam; PF01583; APS_kinase; 0-1; trigger=no
DR   NCBIfam; TIGR00339; sopT; 1; trigger=no
DR   NCBIfam; TIGR00455; apsK; 0-1; trigger=no
XX
KW   Cytoplasm
KW   Amino-acid biosynthesis
KW   ATP-binding
KW   Cysteine biosynthesis
KW   Methionine biosynthesis
KW   Nucleotide-binding
KW   Nucleotidyltransferase
KW   Transferase
case <IPRO:IPR002891>
KW   Allosteric enzyme
end case
case <OC:Saccharomyces>
KW   Phosphoprotein
end case
XX
GO   GO:0004781; F:sulfate adenylyltransferase (ATP) activity
GO   GO:0000103; P:sulfate assimilation
GO   GO:0005737; C:cytoplasm
XX
FT   From: MET3_YEAST (P08536)
FT   BINDING         195..198
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: Q-T-R-N
FT   BINDING         289..292
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: G-R-D-H
FT   ACT_SITE        196
FT   Condition: T
FT   ACT_SITE        197
FT   Condition: R
FT   ACT_SITE        198
FT   Condition: N
FT   BINDING         195
FT                   /ligand="sulfate"
FT                   /ligand_id="ChEBI:CHEBI:16189"
FT   Condition: Q
FT   BINDING         197
FT                   /ligand="sulfate"
FT                   /ligand_id="ChEBI:CHEBI:16189"
FT   Condition: R
FT   BINDING         293
FT                   /ligand="sulfate"
FT                   /ligand_id="ChEBI:CHEBI:16189"
FT   Condition: A
FT   BINDING         331
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: [MILV]
FT   SITE            201
FT                   /note="Transition state stabilizer"
FT   Condition: H
FT   SITE            204
FT                   /note="Transition state stabilizer"
FT   Condition: H
FT   SITE            328
FT                   /note="Induces change in substrate recognition on ATP
FT                   binding"
FT   Condition: F
FT   REGION          Nter..167
FT                   /note="N-terminal"
FT   REGION          168..393
FT                   /note="Catalytic"
case not <IPRO:IPR002891>
FT   REGION          394..Cter
FT                   /note="Required for oligomerization; adenylyl-sulfate
FT                   kinase-like"
else
FT   From: MET3_PENCH (Q12650)
FT   REGION          394..Cter
FT                   /note="Allosteric regulation domain; adenylyl-sulfate
FT                   kinase-like"
FT   BINDING         433..436
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /ligand_note="allosteric inhibitor"
FT   Condition: [DE]-x(2)-R
FT   BINDING         476..477
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /ligand_note="allosteric inhibitor"
FT   Condition: [IT]-A
FT   BINDING         450
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /ligand_note="allosteric inhibitor"
FT   Condition: R
FT   BINDING         514
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /ligand_note="allosteric inhibitor"
FT   Condition: [RK]
end case
XX
Size: 490-581;
Related: None;
Template: P08536; Q12650;
Scope:
 Eukaryota; Fungi
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.12 2023/06/01
//