AC   MF_01865;
DC   Protein; auto
TR   HAMAP; MF_01865; -; 1; level=0
XX
Names: MTTase_RimO
XX
ID   RIMO
DE   RecName: Full=Ribosomal protein uS12 methylthiotransferase RimO;
DE            Short=uS12 MTTase;
DE            Short=uS12 methylthiotransferase;
DE            EC=2.8.4.4;
DE   AltName: Full=Ribosomal protein uS12 (aspartate-C(3))-methylthiotransferase;
DE   AltName: Full=Ribosome maturation factor RimO;
GN   Name=rimO;
XX
CC   -!- FUNCTION: Catalyzes the methylthiolation of an aspartic acid residue of
CC       ribosomal protein uS12.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[sulfur carrier]-SH + AH2 + L-aspartate(89)-[ribosomal protein
CC         uS12]-hydrogen + 2 S-adenosyl-L-methionine = 3-methylsulfanyl-L-
CC         aspartate(89)-[ribosomal protein uS12]-hydrogen + 5'-deoxyadenosine +
CC         [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:37087, Rhea:RHEA-COMP:10460, Rhea:RHEA-
CC         COMP:10461, Rhea:RHEA-COMP:14737, Rhea:RHEA-COMP:14739,
CC         ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:17319,
CC         ChEBI:CHEBI:17499, ChEBI:CHEBI:29917, ChEBI:CHEBI:29961,
CC         ChEBI:CHEBI:57844, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:64428, ChEBI:CHEBI:73599; EC=2.8.4.4;
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC       Note=Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3
CC       cysteines and an exchangeable S-adenosyl-L-methionine.;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the methylthiotransferase family. RimO
CC       subfamily.
XX
DR   PROSITE; PS50926; TRAM; 0-1; trigger=yes
DR   PROSITE; PS01278; MTTASE_RADICAL; 1; trigger=no
DR   PROSITE; PS51449; MTTASE_N; 1; trigger=yes
DR   PROSITE; PS51918; RADICAL_SAM; 1; trigger=yes
DR   Pfam; PF04055; Radical_SAM; 1; trigger=no
DR   Pfam; PF01938; TRAM; 0-1; trigger=no
DR   Pfam; PF00919; UPF0004; 1; trigger=no
DR   NCBIfam; TIGR01125; TIGR01125; 1; trigger=no
DR   NCBIfam; TIGR00089; TIGR00089; 1; trigger=no
XX
KW   4Fe-4S
KW   Cytoplasm
KW   Iron
KW   Iron-sulfur
KW   Metal-binding
KW   S-adenosyl-L-methionine
KW   Transferase
XX
GO   GO:0016740; F:transferase activity
GO   GO:0051539; F:4 iron, 4 sulfur cluster binding
GO   GO:0018339; P:peptidyl-L-beta-methylthioaspartic acid biosynthetic process from peptidyl-aspartic acid
GO   GO:0005737; C:cytoplasm
XX
FT   From: RIMO_ECOLI (P0AEI4)
FT   BINDING         17
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT   Group: 1; Condition: C
FT   BINDING         53
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT   Group: 1; Condition: C
FT   BINDING         82
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT   Group: 1; Condition: C
FT   BINDING         150
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT   Group: 2; Condition: C
FT   BINDING         154
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT   Group: 2; Condition: C
FT   BINDING         157
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT   Group: 2; Condition: C
XX
Size: 401-545;
Related: None;
Template: P0AEI4;
Scope:
 Bacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.20 2023/06/01
//