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HAMAP rule MF_03049

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General rule information [?]

PURL https://purl.expasy.org/hamap/rule/MF_03049
Accession MF_03049
Dates 19-AUG-2013 (Created)
29-OCT-2024 (Last updated, Version 19)
Name MOCS3_Uba4
Scope(s) Eukaryota
Template(s) O95396; P38820; O59954; [ Recover all ]
Triggered by HAMAP; MF_03049 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

case <OC:Vertebrata> or <OC:Viridiplantae>
Identifier MOCS3
Protein name RecName: Full=Adenylyltransferase and sulfurtransferase MOCS3;
AltName: Full=Molybdenum cofactor synthesis protein 3;
                 Includes:
RecName: Full=Molybdopterin-synthase adenylyltransferase;
                 EC=2.7.7.80;
AltName: Full=Adenylyltransferase MOCS3;
AltName: Full=Sulfur carrier protein MOCS2A adenylyltransferase;
                 Includes:
RecName: Full=Molybdopterin-synthase sulfurtransferase;
                 EC=2.8.1.11;
AltName: Full=Sulfurtransferase MOCS3;
AltName: Full=Sulfur carrier protein MOCS2A sulfurtransferase;
else case <OC:Pezizomycotina>
Identifier UBA4
Protein name RecName: Full=Adenylyltransferase and sulfurtransferase uba4;
AltName: Full=Ubiquitin-like protein activator 4;
AltName: Full=Common component for nitrate reductase and xanthine dehydrogenase protein F;
                 Includes:
RecName: Full=Molybdopterin-synthase adenylyltransferase;
                 EC=2.7.7.80;
AltName: Full=Adenylyltransferase uba4;
AltName: Full=Sulfur carrier protein MOCS2A adenylyltransferase;
                 Includes:
RecName: Full=Molybdopterin-synthase sulfurtransferase;
                 EC=2.8.1.11;
AltName: Full=Sulfurtransferase uba4;
AltName: Full=Sulfur carrier protein MOCS2A sulfurtransferase;
else case <OC:Fungi>
Identifier UBA4
Protein name RecName: Full=Adenylyltransferase and sulfurtransferase ;
AltName: Full=Ubiquitin-like protein activator 4;
                 Includes:
RecName: Full=Adenylyltransferase ;
                 EC=2.7.7.-;
                 Includes:
RecName: Full=Sulfurtransferase ;
                 EC=2.8.1.-;
else
Identifier UBA4
Protein name RecName: Full=Adenylyltransferase and sulfurtransferase MOCS3 homolog;
AltName: Full=Ubiquitin-like protein activator 4 homolog;
AltName: Full=UBA4 homolog;
                 Includes:
RecName: Full=Adenylyltransferase;
                 EC=2.7.7.-;
                 Includes:
RecName: Full=Sulfurtransferase;
                 EC=2.8.1.-;
end case
case <OC:Vertebrata>
Gene name Name=MOCS3; Synonyms=UBA4;
else case <OC:Caenorhabditis>
Gene name Name=moc-3; Synonyms=uba-4;
else case <OC:Viridiplantae>
Gene name Name=MOCS3; Synonyms=CNX5, UBA4;
else case <OC:Pezizomycotina>
Gene name Name=uba4; Synonyms=cnxF;
else case <OC:Fungi>
Gene name Name=UBA4;
else case <OC:Drosophilidae>
Gene name Name=Uba4;
end case

Comments [?]

case <OC:Vertebrata> or <OC:Viridiplantae>
FUNCTIONPlays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers @gn(URM1) and MOCS2A. Its N-terminus first activates @gn(URM1) and MOCS2A as acyl-adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to @gn(URM1) and MOCS2A to form thiocarboxylation (-COSH) of their C-terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as nucleophile towards @gn(URM1) and MOCS2A. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor; @gn(NFS1) probably acting as a sulfur donor for thiocarboxylation reactions.
CATALYTIC ACTIVITY Reaction=[molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly + ATP + H(+) = [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly-AMP + diphosphate; Xref=Rhea:RHEA:43616, Rhea:RHEA-COMP:12159, Rhea:RHEA-COMP:12202, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:90618, ChEBI:CHEBI:90778; EC=2.7.7.80;
CATALYTIC ACTIVITY Reaction=[molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly-AMP + S-sulfanyl-L-cysteinyl-[cysteine desulfurase] + AH2 = [molybdopterin-synthase sulfur-carrier protein]-C-terminal-Gly- aminoethanethioate + L-cysteinyl-[cysteine desulfurase] + A + AMP + 2 H(+); Xref=Rhea:RHEA:48612, Rhea:RHEA-COMP:12157, Rhea:RHEA- COMP:12158, Rhea:RHEA-COMP:12159, Rhea:RHEA-COMP:19907, ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:17499, ChEBI:CHEBI:29950, ChEBI:CHEBI:61963, ChEBI:CHEBI:90618, ChEBI:CHEBI:232372, ChEBI:CHEBI:456215; EC=2.8.1.11;
PATHWAYCofactor biosynthesis; molybdopterin biosynthesis.
else case <OC:Pezizomycotina>
FUNCTIONPlays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers urm1 and MOCS2A. Its N-terminus first activates urm1 and MOCS2A as acyl- adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to urm1 and MOCS2A to form thiocarboxylation (- COSH) of their C-terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as nucleophile towards urm1 and MOCS2A. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor; nfs1 probably acting as a sulfur donor for thiocarboxylation reactions.
CATALYTIC ACTIVITY Reaction=[molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly + ATP + H(+) = [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly-AMP + diphosphate; Xref=Rhea:RHEA:43616, Rhea:RHEA-COMP:12159, Rhea:RHEA-COMP:12202, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:90618, ChEBI:CHEBI:90778; EC=2.7.7.80;
CATALYTIC ACTIVITY Reaction=[molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly-AMP + S-sulfanyl-L-cysteinyl-[cysteine desulfurase] + AH2 = [molybdopterin-synthase sulfur-carrier protein]-C-terminal-Gly- aminoethanethioate + L-cysteinyl-[cysteine desulfurase] + A + AMP + 2 H(+); Xref=Rhea:RHEA:48612, Rhea:RHEA-COMP:12157, Rhea:RHEA- COMP:12158, Rhea:RHEA-COMP:12159, Rhea:RHEA-COMP:19907, ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:17499, ChEBI:CHEBI:29950, ChEBI:CHEBI:61963, ChEBI:CHEBI:90618, ChEBI:CHEBI:232372, ChEBI:CHEBI:456215; EC=2.8.1.11;
PATHWAYCofactor biosynthesis; molybdopterin biosynthesis.
else case <OC:Fungi>
FUNCTIONPlays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Acts by mediating the C-terminal thiocarboxylation of sulfur carrier @gn(URM1). Its N-terminus first activates @gn(URM1) as acyl-adenylate (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to @gn(URM1) to form thiocarboxylation (-COSH) of its C- terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as nucleophile towards @gn(URM1). Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor; @gn(NFS1) probably acting as a sulfur donor for thiocarboxylation reactions. Prior mcm(5) tRNA modification by the elongator complex is required for 2-thiolation. May also be involved in protein urmylation.
else
FUNCTIONPlays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Acts by mediating the C-terminal thiocarboxylation of the sulfur carrier URM1. Its N-terminus first activates URM1 as acyl-adenylate (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to URM1 to form thiocarboxylation (-COSH) of its C-terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as nucleophile towards URM1. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor; NFS1 probably acting as a sulfur donor for thiocarboxylation reactions.
end case
COFACTOR Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 zinc ion per subunit.;
PATHWAYtRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis.
case <OC:Mammalia>
SUBUNITInteracts with NFS1.
end case
SUBCELLULAR LOCATIONCytoplasm.
SIMILARITYIn the N-terminal section; belongs to the HesA/MoeB/ThiF family. UBA4 subfamily.

Keywords [?]

ATP-binding
Cytoplasm
Metal-binding
Multifunctional enzyme
Nucleotide-binding
Transferase
tRNA processing
Zinc
case <OC:Metazoa> or <OC:Viridiplantae> or <OC:Pezizomycotina>
Molybdenum cofactor biosynthesis
else case <OC:Fungi>
Ubl conjugation pathway
end case
case <OC:Vertebrata>
Disulfide bond
end case

Gene Ontology [?]

GO:0016779; Molecular function:nucleotidyltransferase activity
GO:0016783; Molecular function:sulfurtransferase activity
GO:0002098; Biological process:tRNA wobble uridine modification
GO:0034227; Biological process:tRNA thio-modification
GO:0005737; Cellular component:cytoplasm
case <OCellular component:Metazoa> or <OC:Viridiplantae> or <OC:Pezizomycotina>
GO:0006777; Biological process:Mo-molybdopterin cofactor biosynthetic process
else case <OCellular component:Fungi>
GO:0032447; Biological process:protein urmylation
end case

Cross-references [?]

PROSITE PS50206; RHODANESE_3; 1;
Pfam PF05237; MoeZ_MoeB; 1;
Pfam PF00581; Rhodanese; 1;
Pfam PF00899; ThiF; 1;

Features [?]

From: MOCS3_HUMAN (O95396)
Key From To Description Tag Condition FTGroup
BINDING 120 124 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"		 x-N-[LMF]-[HAQ]-R
BINDING 181 182 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"		 [DN]-x
ACT_SITE 239 239 /note="Glycyl thioester intermediate; for adenylyltransferase activity" C
ACT_SITE 412 412 /note="Cysteine persulfide intermediate; for sulfurtransferase activity" C
BINDING 222 222 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"		 C
BINDING 225 225 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"		 C
BINDING 297 297 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"		 C
BINDING 300 300 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"		 C
BINDING 92 92 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"		 G
BINDING 113 113 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"		 D
BINDING 137 137 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"		 K
case <OC:Vertebrata>
DISULFID 316 324 /note="Alternate" C-x*-C
end case

Additional information [?]

Size range 396-529 amino acids
Related rules None
Fusion Nter: None Cter: None



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