Top Level Name

  ⌊ Superfamily (core) Radical SAM

    ⌊ Subgroup BATS domain containing

  ⌊ HydE/PylB-like

     ⌊ Family 3-methylornithine synthase (PylB-like)

  ⌊ FunctionalDomain 3-methylornithine synthase (PylB) (ID 419136)

Superfamily Assignment Evidence Code(s) ISS PubMed:22095926 PubMed:21455182
Family Assignment Evidence Code CFM PubMed:22095926 PubMed:21455182
This entry was last updated onJune 10, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Methanosarcina barkeri Taxon ID: 2208 499625130 WP_011305864.1 (RefSeq)
Methanosarcina barkeri str. Wiesmoor Taxon ID: 1434109 805398896 AKB49416.1 (Genbank) URP
Methanosarcina barkeri str. Fusaro Taxon ID: 269797 72395541 AAZ69814.1 (Genbank) URP
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Uniprot

Protein NameAccessionEC Number Identifier
3-methylornithine synthase Q46E78 5.4.99.58 PYLB_METBF (Swiss-Prot)
n/a A0A0E3LKF2 A0A0E3LKF2_METBA (TrEMBL)

Sequence

Length of Enzyme (full-length): 350 | Length of Functional Domain: 348

1       10        20        30        40        50        60

MIQKMALDEFDSLGDKVIEGYQLTDNDLRTLLSLESKEGLERLYSAARKVRDHYFGNRVF
LNCFIYFSTYCKNQCSFCYYNCRNEINRYRLTMEEIKETCKTLKGAGFHMVDLTMGEDPY
YYEDPNRFVELVQIVKEELGLPIMISPGLMDNATLLKAREKGANFLALYQETYDTELYRK
LRVGQSFDGRVNARRFAKQQGYCVEDGILTGVGNDIESTILSLRGMSTNDPDMVRVMTFL
PQEGTPLEGFRDKSNLSELKIISVLRLMFPKRLIPASLDLEGIDGMVLRLNAGANIVTSI
LPPDSQLEGVANYDRDLEERDRDIKSVVRRLEIMGMKPARQADFEAVLGC
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
71 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
75 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
78 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
71 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
75 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
78 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
64 Phe (F) side chain Van der Waals binding of substrate substrate binding -- binding ISS PubMed:22095926
71 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS PubMed:22095926
75 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS PubMed:22095926
78 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS PubMed:22095926
112 Asp (D) side chain Binds substrate substrate binding -- binding ISS PubMed:22095926
146 Ser (S) side chain Binds substrate substrate binding -- binding ISS PubMed:22095926
169 Tyr (Y) side chain Binds substrate substrate binding -- binding ISS PubMed:22095926
171 Glu (E) side chain Binds AdoMet cofactor binding -- binding ISS PubMed:22095926
190 Arg (R) side chain Binds AdoMet cofactor binding -- binding ISS PubMed:22095926
235 Arg (R) side chain Binds substrate substrate binding -- binding ISS PubMed:22095926
237 Met (M) side chain Van der Waals binding of substrate substrate binding -- binding ISS PubMed:22095926
277 Ser (S) side chain Binds substrate substrate binding -- binding ISS PubMed:22095926
279 Asp (D) side chain Binds substrate substrate binding -- binding ISS PubMed:22095926

Catalyzed Reaction

methylornithine synthase

L-lysinium(1+)
32551		 (3R)-3-methyl-D-ornithine(1+)
64642

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

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 348 350
update domain start position 9 3
Sept. 15, 2014, 5:17 a.m. update curation agent setDomainBoundaries.py holliday
update family assignment evidence code CFM,ISS CFM
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
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
Oct. 15, 2016, 6:29 a.m. update curation agent setDomainBoundaries.py holliday
update curation agent holliday setDomainBoundaries.py
update name Methylornithine synthase (PylB) 3-methylornithine synthase (PylB)
EC number assigned by UniProtKB accession ID.