AC   MF_03049;
DC   Protein; auto
TR   HAMAP; MF_03049; -; 1; level=0
XX
Names: MOCS3_Uba4
XX
case <OC:Vertebrata> or <OC:Viridiplantae>
ID   MOCS3
DE   RecName: Full=Adenylyltransferase and sulfurtransferase MOCS3;
DE   AltName: Full=Molybdenum cofactor synthesis protein 3;
DE   Includes:
DE     RecName: Full=Molybdopterin-synthase adenylyltransferase;
DE              EC=2.7.7.80;
DE     AltName: Full=Adenylyltransferase MOCS3;
DE     AltName: Full=Sulfur carrier protein MOCS2A adenylyltransferase;
DE   Includes:
DE     RecName: Full=Molybdopterin-synthase sulfurtransferase;
DE              EC=2.8.1.11;
DE     AltName: Full=Sulfurtransferase MOCS3;
DE     AltName: Full=Sulfur carrier protein MOCS2A sulfurtransferase;
else case <OC:Pezizomycotina>
ID   UBA4
DE   RecName: Full=Adenylyltransferase and sulfurtransferase uba4;
DE   AltName: Full=Ubiquitin-like protein activator 4;
DE   AltName: Full=Common component for nitrate reductase and xanthine dehydrogenase protein F;
DE   Includes:
DE     RecName: Full=Molybdopterin-synthase adenylyltransferase;
DE              EC=2.7.7.80;
DE     AltName: Full=Adenylyltransferase uba4;
DE     AltName: Full=Sulfur carrier protein MOCS2A adenylyltransferase;
DE   Includes:
DE     RecName: Full=Molybdopterin-synthase sulfurtransferase;
DE              EC=2.8.1.11;
DE     AltName: Full=Sulfurtransferase uba4;
DE     AltName: Full=Sulfur carrier protein MOCS2A sulfurtransferase;
else case <OC:Fungi>
ID   UBA4
DE   RecName: Full=Adenylyltransferase and sulfurtransferase <gene_name>;
DE   AltName: Full=Ubiquitin-like protein activator 4;
DE   Includes:
DE     RecName: Full=Adenylyltransferase <gene_name>;
DE              EC=2.7.7.-;
DE   Includes:
DE     RecName: Full=Sulfurtransferase <gene_name>;
DE              EC=2.8.1.-;
else
ID   UBA4
DE   RecName: Full=Adenylyltransferase and sulfurtransferase MOCS3 homolog;
DE   AltName: Full=Ubiquitin-like protein activator 4 homolog;
DE   AltName: Full=UBA4 homolog;
DE   Includes:
DE     RecName: Full=Adenylyltransferase;
DE              EC=2.7.7.-;
DE   Includes:
DE     RecName: Full=Sulfurtransferase;
DE              EC=2.8.1.-;
end case
case <OC:Vertebrata>
GN   Name=MOCS3; Synonyms=UBA4;
else case <OC:Caenorhabditis>
GN   Name=moc-3; Synonyms=uba-4;
else case <OC:Viridiplantae>
GN   Name=MOCS3; Synonyms=CNX5, UBA4;
else case <OC:Pezizomycotina>
GN   Name=uba4; Synonyms=cnxF;
else case <OC:Fungi>
GN   Name=UBA4;
else case <OC:Drosophilidae>
GN   Name=Uba4;
end case
XX
case <OC:Vertebrata> or <OC:Viridiplantae>
CC   -!- FUNCTION: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA
CC       wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also
CC       essential during biosynthesis of the molybdenum cofactor. Acts by
CC       mediating the C-terminal thiocarboxylation of sulfur carriers @gn(URM1)
CC       and MOCS2A. Its N-terminus first activates @gn(URM1) and MOCS2A as
CC       acyl-adenylates (-COAMP), then the persulfide sulfur on the catalytic
CC       cysteine is transferred to @gn(URM1) and MOCS2A to form
CC       thiocarboxylation (-COSH) of their C-terminus. The reaction probably
CC       involves hydrogen sulfide that is generated from the persulfide
CC       intermediate and that acts as nucleophile towards @gn(URM1) and MOCS2A.
CC       Subsequently, a transient disulfide bond is formed. Does not use
CC       thiosulfate as sulfur donor; @gn(NFS1) probably acting as a sulfur
CC       donor for thiocarboxylation reactions.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[molybdopterin-synthase sulfur-carrier protein]-C-terminal
CC         Gly-Gly + ATP + H(+) = [molybdopterin-synthase sulfur-carrier
CC         protein]-C-terminal Gly-Gly-AMP + diphosphate; Xref=Rhea:RHEA:43616,
CC         Rhea:RHEA-COMP:12159, Rhea:RHEA-COMP:12202, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:90618,
CC         ChEBI:CHEBI:90778; EC=2.7.7.80;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[molybdopterin-synthase sulfur-carrier protein]-C-terminal
CC         Gly-Gly-AMP + AH2 + S-sulfanyl-L-cysteinyl-[cysteine desulfurase] =
CC         [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-NH-
CC         CH2-C(O)SH + A + AMP + H(+) + L-cysteinyl-[cysteine desulfurase];
CC         Xref=Rhea:RHEA:48612, Rhea:RHEA-COMP:12157, Rhea:RHEA-COMP:12158,
CC         Rhea:RHEA-COMP:12159, Rhea:RHEA-COMP:12160, ChEBI:CHEBI:13193,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17499, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:61963, ChEBI:CHEBI:90618, ChEBI:CHEBI:90619,
CC         ChEBI:CHEBI:456215; EC=2.8.1.11;
CC   -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
else case <OC:Pezizomycotina>
CC   -!- FUNCTION: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA
CC       wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also
CC       essential during biosynthesis of the molybdenum cofactor. Acts by
CC       mediating the C-terminal thiocarboxylation of sulfur carriers urm1 and
CC       MOCS2A. Its N-terminus first activates urm1 and MOCS2A as acyl-
CC       adenylates (-COAMP), then the persulfide sulfur on the catalytic
CC       cysteine is transferred to urm1 and MOCS2A to form thiocarboxylation (-
CC       COSH) of their C-terminus. The reaction probably involves hydrogen
CC       sulfide that is generated from the persulfide intermediate and that
CC       acts as nucleophile towards urm1 and MOCS2A. Subsequently, a transient
CC       disulfide bond is formed. Does not use thiosulfate as sulfur donor;
CC       nfs1 probably acting as a sulfur donor for thiocarboxylation reactions.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[molybdopterin-synthase sulfur-carrier protein]-C-terminal
CC         Gly-Gly + ATP + H(+) = [molybdopterin-synthase sulfur-carrier
CC         protein]-C-terminal Gly-Gly-AMP + diphosphate; Xref=Rhea:RHEA:43616,
CC         Rhea:RHEA-COMP:12159, Rhea:RHEA-COMP:12202, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:90618,
CC         ChEBI:CHEBI:90778; EC=2.7.7.80;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[molybdopterin-synthase sulfur-carrier protein]-C-terminal
CC         Gly-Gly-AMP + AH2 + S-sulfanyl-L-cysteinyl-[cysteine desulfurase] =
CC         [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-NH-
CC         CH2-C(O)SH + A + AMP + H(+) + L-cysteinyl-[cysteine desulfurase];
CC         Xref=Rhea:RHEA:48612, Rhea:RHEA-COMP:12157, Rhea:RHEA-COMP:12158,
CC         Rhea:RHEA-COMP:12159, Rhea:RHEA-COMP:12160, ChEBI:CHEBI:13193,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17499, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:61963, ChEBI:CHEBI:90618, ChEBI:CHEBI:90619,
CC         ChEBI:CHEBI:456215; EC=2.8.1.11;
CC   -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
else case <OC:Fungi>
CC   -!- FUNCTION: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA
CC       wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Acts
CC       by mediating the C-terminal thiocarboxylation of sulfur carrier
CC       @gn(URM1). Its N-terminus first activates @gn(URM1) as acyl-adenylate
CC       (-COAMP), then the persulfide sulfur on the catalytic cysteine is
CC       transferred to @gn(URM1) to form thiocarboxylation (-COSH) of its C-
CC       terminus. The reaction probably involves hydrogen sulfide that is
CC       generated from the persulfide intermediate and that acts as nucleophile
CC       towards @gn(URM1). Subsequently, a transient disulfide bond is formed.
CC       Does not use thiosulfate as sulfur donor; @gn(NFS1) probably acting as
CC       a sulfur donor for thiocarboxylation reactions. Prior mcm(5) tRNA
CC       modification by the elongator complex is required for 2-thiolation. May
CC       also be involved in protein urmylation.
else
CC   -!- FUNCTION: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA
CC       wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Acts
CC       by mediating the C-terminal thiocarboxylation of the sulfur carrier
CC       URM1. Its N-terminus first activates URM1 as acyl-adenylate (-COAMP),
CC       then the persulfide sulfur on the catalytic cysteine is transferred to
CC       URM1 to form thiocarboxylation (-COSH) of its C-terminus. The reaction
CC       probably involves hydrogen sulfide that is generated from the
CC       persulfide intermediate and that acts as nucleophile towards URM1.
CC       Subsequently, a transient disulfide bond is formed. Does not use
CC       thiosulfate as sulfur donor; NFS1 probably acting as a sulfur donor for
CC       thiocarboxylation reactions.
end case
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Note=Binds 1 zinc ion per subunit.;
CC   -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC       biosynthesis.
case <OC:Mammalia>
CC   -!- SUBUNIT: Interacts with NFS1.
end case
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the HesA/MoeB/ThiF
CC       family. UBA4 subfamily.
XX
DR   PROSITE; PS50206; RHODANESE_3; 1; trigger=yes
DR   Pfam; PF05237; MoeZ_MoeB; 1; trigger=no
DR   Pfam; PF00581; Rhodanese; 1; trigger=no
DR   Pfam; PF00899; ThiF; 1; trigger=no
XX
KW   ATP-binding
KW   Cytoplasm
KW   Metal-binding
KW   Multifunctional enzyme
KW   Nucleotide-binding
KW   Transferase
KW   tRNA processing
KW   Zinc
case <OC:Metazoa> or <OC:Viridiplantae> or <OC:Pezizomycotina>
KW   Molybdenum cofactor biosynthesis
else case <OC:Fungi>
KW   Ubl conjugation pathway
end case
case <OC:Vertebrata>
KW   Disulfide bond
end case
XX
GO   GO:0016779; F:nucleotidyltransferase activity
GO   GO:0016783; F:sulfurtransferase activity
GO   GO:0002098; P:tRNA wobble uridine modification
GO   GO:0034227; P:tRNA thio-modification
GO   GO:0005737; C:cytoplasm
case <OC:Metazoa> or <OC:Viridiplantae> or <OC:Pezizomycotina>
GO   GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process
else case <OC:Fungi>
GO   GO:0032447; P:protein urmylation
end case
XX
FT   From: MOCS3_HUMAN (O95396)
FT   BINDING         120..124
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: x-N-[LMF]-[HAQ]-R
FT   BINDING         181..182
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: [DN]-x
FT   ACT_SITE        239
FT                   /note="Glycyl thioester intermediate; for
FT                   adenylyltransferase activity"
FT   Condition: C
FT   ACT_SITE        412
FT                   /note="Cysteine persulfide intermediate; for
FT                   sulfurtransferase activity"
FT   Condition: C
FT   BINDING         222
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Condition: C
FT   BINDING         225
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Condition: C
FT   BINDING         297
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Condition: C
FT   BINDING         300
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Condition: C
FT   BINDING         92
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: G
FT   BINDING         113
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: D
FT   BINDING         137
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: K
case <OC:Vertebrata>
FT   DISULFID        316..324
FT                   /note="Alternate"
FT   Condition: C-x*-C
end case
XX
Size: 396-529;
Related: None;
Template: O95396; P38820; O59954;
Scope:
 Eukaryota
Fusion:
 Nter: None
 Cter: None
Duplicate: in DROPS, MAIZE
Plasmid: None
Comments: None
XX
# Revision 1.16 2022/11/19
//