Top Level Name

  ⌊ Superfamily (core) Radical SAM

    ⌊ Subgroup anaerobic coproporphyrinogen-III oxidase like

  methyltransferase (class C)

     ⌊ Family methylation of yatakemycin (YTK)

  ⌊ FunctionalDomain C-methyltransferase (YtkT) (ID 449310)

Superfamily Assignment Evidence Code(s) ISS PubMed:22612591
Family Assignment Evidence Code CFM PubMed:22612591
This entry was last updated onJune 10, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Streptomyces sp. TP-A2060 Taxon ID: 991125 325452085 ADZ13556.1 (Genbank)

Uniprot

Protein NameAccessionEC Number Identifier
n/a I3NN68 I3NN68_9ACTN (TrEMBL)

Sequence

Length of Enzyme (full-length): 506 | Length of Functional Domain: 461

1       10        20        30        40        50        60

MTEAPNAAAAAKETITRNFLDTPSFWREYPDRDIEFVRWYPCNIGPLTSDQMFTTIENRP
KTVSFYL
HIPFCNQVCTSCPYNKLHTRNTLVTDYLEALKAEILLYSRLGYLDGVKFSSGY
FGGGTPTTLRAEQLDDLLGFLRRHLEFTDDYTVTIESTPVDIDQHKIDVLLRHGVNRVSM
GVQTFHDPLLRYLGRARAHTGESALRTIELLDRNGMENICIDFMIGIPGQTPE
LWAQDIA
TLTSIPVTSFSVYNYAVLPGSEAFFAVQSGITPPCPSTKEADAMYHYMHEELLSKNYLAL
TYNDFAEPMKPEWAAKGAQTFPILPDGSKPFRGLKADSLSLTDHLAQVWGRCGDMVAIGA
GAYGYLNNHLYCTEPDIGRYIETVNSGRLPAVMGAYTDEHERRCRSLVLGLKLLRVSRAD
YRARHGVDPYEYFTEKIDGLVDKGLLEVTDDALQVTYPKGWHYIDNISKTFYSEANHRLP
QPTSASTEILNWQVRPENGR
RLLNIV
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
72 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
76 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
79 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
72 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
76 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
79 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
Family CAR This EFD conserves 3/3 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
72 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
76 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
79 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS

Catalyzed Reaction

yatakemycin methyltransferase

+ + + +
YTM-T
87402
S-adenosyl-L-methioninate
67040
Me-YTM-T
87403
S-adenosyl-L-homocysteine zwitterion
57856
L-methionine zwitterion
57844
5'-deoxyadenosine
17319

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

Curation History

Time Change Annotation Old Value New Value
May 14, 2014, 3:26 a.m. update curation agent holliday setDomainBoundaries.py
update domain end position 288 504
update domain start position 62 40
July 15, 2014, 6:50 a.m. update curation agent setDomainBoundaries.py holliday
update family assignment evidence code ISS CFM
Oct. 16, 2014, 7:22 a.m. update curation agent holliday setDomainBoundaries.py
July 13, 2015, 3:26 p.m. update domain end position 504 502
Oct. 15, 2016, 7:23 a.m. update domain end position 502 500
EC number assigned by UniProtKB accession ID.