Top Level Name

  ⌊ Superfamily (core) Radical SAM

    ⌊ Subgroup BATS domain containing

  ⌊ HydE/PylB-like

     ⌊ Family 3-methylornithine synthase (PylB-like)

  ⌊ FunctionalDomain methylornithine synthase-like protein (ID 419133)

Superfamily Assignment Evidence Code(s) ISS
Family Assignment Evidence Code ISS
This entry was last updated onJune 10, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Methanosarcina barkeri Taxon ID: 2208 21322024 AAL40868.1 (Genbank)

Uniprot

Protein NameAccessionEC Number Identifier
n/a Q8NKQ5 Q8NKQ5_METBA (TrEMBL)

Sequence

Length of Enzyme (full-length): 346 | Length of Functional Domain: 346

1       10        20        30        40        50        60

MALDEFDSLGDKVIEGYQLTDNDLRTLLSLESEENLERLYSAARKVRDHYFGNRDFLNCF
IYFSTYCKNQCSFCYYNCRNEINRYRLTMEEIKETCKTLKGVGFHMVDLTMGEDPYYYED
PNRFVELVQLVKEDLGLSIMISPGLMDNATLLKAREKGANFLALYQETYDTELYRKLRVG
QSFDGRVNARRFAKKQGYCVEDGILTGVGNDIESTILSLRGMSTNDPDMVRVMTFLPQEG
TPLEGFRDKSNLSELKIISVLRLMFPKRLIPASLDLEGIDGMVLRLNAGANIVTSILPPD
SQLEGVANYDRGLKERDRDIKSVIQRLEIMGMKPARQADFEAVLGC
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
67 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
71 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
74 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
67 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
71 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
74 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
Family CAR This EFD conserves 13/13 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
60 Phe (F) side chain Van der Waals binding of substrate substrate binding -- binding ISS PubMed:22095926
67 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS PubMed:22095926
71 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS PubMed:22095926
74 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS PubMed:22095926
108 Asp (D) side chain Binds substrate substrate binding -- binding ISS PubMed:22095926
142 Ser (S) side chain Binds substrate substrate binding -- binding ISS PubMed:22095926
165 Tyr (Y) side chain Binds substrate substrate binding -- binding ISS PubMed:22095926
167 Glu (E) side chain Binds AdoMet cofactor binding -- binding ISS PubMed:22095926
186 Arg (R) side chain Binds AdoMet cofactor binding -- binding ISS PubMed:22095926
231 Arg (R) side chain Binds substrate substrate binding -- binding ISS PubMed:22095926
233 Met (M) side chain Van der Waals binding of substrate substrate binding -- binding ISS PubMed:22095926
273 Ser (S) side chain Binds substrate substrate binding -- binding ISS PubMed:22095926
275 Asp (D) side chain Binds substrate substrate binding -- binding ISS PubMed:22095926

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
3T7V Crystal Structure Of Methylornithine Synthase (Pylb) Methylornithine Synthase Pylb 2 1.5 Iron/Sulfur Cluster
(2 more ⇓) 		CSA • PDB • PDBSum
Percent identity and alignment length from the BLAST match of the Functional Domain sequence to the PDB sequence.
"Yes" indicates that a GI associated with this Functional Domain was mapped to the PDB ID via UniProtKB.

Curation History
Time Change Annotation Old Value New Value
May 14, 2014, 3:08 a.m. update curation agent holliday setDomainBoundaries.py
update domain end position 344 346
update domain start position 5 1
July 15, 2014, 6:18 a.m. update curation agent setDomainBoundaries.py holliday
update family assignment evidence code CFM,ISS ISS
Sept. 15, 2014, 5:17 a.m. update subgroup - BATS domain containing
Oct. 16, 2014, 6:45 a.m. update curation agent holliday setDomainBoundaries.py
May 11, 2015, 1:49 p.m. update curation agent setDomainBoundaries.py holliday
update curation agent holliday setDomainBoundaries.py
update name Methylornithine synthase (PylB) methylornithine synthase-like protein
Dec. 17, 2015, 5:52 a.m. update curation agent setDomainBoundaries.py holliday
update subgroup BATS domain containing HydE/PylB-like
Jan. 18, 2016, 5:46 a.m. update curation agent holliday setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.