Top Level Name

  ⌊ Superfamily (core) Radical SAM

    ⌊ Subgroup methylthiotransferase

     ⌊ Family ribosomal protein S12 methylthiotransferase (RimO-like)

  ⌊ FunctionalDomain Ribosomal protein S12 methylthiotransferase RimO (ID 280036)

Superfamily Assignment Evidence Code(s) ISS
Family Assignment Evidence Code CFM PubMed:19736993 PubMed:18252828 PubMed:21169565
This entry was last updated onJune 10, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Escherichia coli O157:H7 str. Sakai Taxon ID: 386585 15830169 NP_308942.1 (RefSeq)
Escherichia coli str. K-12 substr. MG1655 Taxon ID: 511145 16128803 NP_415356.1 (RefSeq) URP
Taxon ID: 543 445971512 WP_000049367.1 (RefSeq)
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Uniprot

Protein NameAccessionEC Number Identifier
Ribosomal protein S12 methylthiotransferase RimO {ECO:0000255|HAMAP-Rule:MF_01865} A7ZJQ2 RIMO_ECO24 (Swiss-Prot)
Ribosomal protein S12 methylthiotransferase RimO {ECO:0000255|HAMAP-Rule:MF_01865} B7LCB8 RIMO_ECO55 (Swiss-Prot)
Ribosomal protein S12 methylthiotransferase RimO {ECO:0000255|HAMAP-Rule:MF_01865} P0AEI5 RIMO_ECO57 (Swiss-Prot)
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Sequence

Length of Enzyme (full-length): 441 | Length of Functional Domain: 439

1       10        20        30        40        50        60

MSKVTPQPKIGFVSLGCPKNLVDSERILTELRTEGYDVVPSYDDADMVIVNTCGFIDSAV
QESLEAIGEALNENGKVIVTGCLGAKEDQIREVHPKVLEITGPHSYEQVLEHVHHYVPKP
KHNPFLSLVPEQGVKLTPRHYAYLKISEGCNHRCTFCIIPSMRGDLVSRPIGEVLSEAKR
LVDAGVKEILVISQDTSAYGVDVKHRTGFHNGEPVKTSMVSLCEQLSKLGIWTRLHYVYP
YPHVDDVIPLMAEGKILPYLDIPLQHASPRILKLMKRPGSVDRQLARIKQWREICPELTL
RSTFIVGFPGETEEDFQMLLDFLKEARLDRVGCFKYSPVEGADANALPDQVPEEVKEERW
NRFMQLQQQISAERLQEKVGREILVIIDEVDEEGAIGRSMADAPEIDGAVYLNGETNVKP
GDILRVKVEHADEYDLWGSRV
This shows the full-length sequence of the enzyme. The region of the functional domain is highlighted in black letters, while the residual residues are shown in grey. The Superfamily domain, when present, is shown using underlining. In many cases the functional domain is the full-length sequence.
Conserved catalytic residues (as determined by automated alignment to family, subgroup, or superfamily HMMs) are shown with teal highlighting . Conserved catalytic residues which do not matched the Conserved Alignment Residue are shown with maroon highlighting . Information regarding their function can be found in the Conserved Residues section below.
FASTA formatted full-length sequence.
BLAST this sequence against SFLD.
Scan SFLD-HMMs with this sequence.

Conserved Residues
Superfamily CAR This EFD conserves 3/3 Superfamily-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
150 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
154 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
157 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
Subgroup CAR This EFD conserves 3/3 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
150 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
154 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
157 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
Family CAR This EFD conserves 6/6 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
17 Cys (C) side chain Binds [4Fe-4S] cluster cofactor binding -- binding ISS
53 Cys (C) side chain Binds [4Fe-4S] cluster cofactor binding -- binding ISS
82 Cys (C) side chain Binds [4Fe-4S] cluster cofactor binding -- binding ISS
150 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
154 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
157 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS

Catalyzed Reaction

[ribosomal protein S12] (aspartate89-C3)-methylthiotransferase

+ + 2 + + +
L-aspartate residue
29961		 Sulfur donor
80867		 S-adenosyl-L-methionine zwitterion
59789		 3-methylthioaspartate residue
73599		 S-adenosyl-L-homocysteine zwitterion
57856		 5'-deoxyadenosine
17319		 L-methionine zwitterion
57844

EC: 2.8.4.4 | IntEnz: 2.8.4.4 | Kegg: 2.8.4.4 | BioCyc: 2.8.4.4 | BRENDA: 2.8.4.4

Curation History
Time Change Annotation Old Value New Value
May 14, 2014, 3 a.m. update curation agent holliday setDomainBoundaries.py
update domain start position 1 2
May 11, 2015, 8:43 a.m. update curation agent setDomainBoundaries.py holliday
update curation agent holliday setDomainBoundaries.py
update family assignment evidence code CFM,ISS CFM
Oct. 15, 2016, 3:51 a.m. update domain start position 2 3
EC number assigned by UniProtKB accession ID.