Top Level Name

  ⌊ Superfamily (core) Radical SAM

    ⌊ Subgroup B12-binding domain containing

  ⌊ methyltransferase (Class B)

     ⌊ Family phosphonoacetaldehyde methylase (fom3-like)

  ⌊ FunctionalDomain Phosphonoacetaldehyde methylase (ID 391556)

Superfamily Assignment Evidence Code(s) ISS
Family Assignment Evidence Code CFM PubMed:19489722
This entry was last updated onApril 9, 2016

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Streptomyces wedmorensis Taxon ID: 43759 1061002

Uniprot

Protein NameAccessionEC Number Identifier
2-hydroxyethylphosphonate methyltransferase {ECO:0000305} Q56184 FOM3_STRWE (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 534 | Length of Functional Domain: 534

1       10        20        30        40        50        60

MTIGSLGSTEFALHGKPAIRWGDLPQRVGKPETRRYQKVLLLNPSATLFRHDLPRCTYPL
GLGYIAAVLEKYGYEVKILDVFAEGYYNAQPVDGDDQFLRYGLSDDDIVKVMKEFGPDVV
GISSIFSNQADNVHHLLKLADLVTPEAVTAIGGAHARYFPKACLDDPNLDAVFLGEGEMT
FLLWMEHLNGNVSDDEVHGIAWRDRDGKVQIKPELPLISSMRPEGPETGKSSPMLSMAGE
LDHIPFPAWHHYNMEKYFEIKAYQSPYTVGSRVGQLYTSRGCTAHCTFCTTTHFWGQKLR
RRSVQDVVDEVLRLRDEYGIDEFHIQDDNITNDMDHARELFRAFKEVGLPWATPQGTALW
RMDEELLDLMAESGAYQVTFAIESGVQRVLKELIKKPLNLERTSHLIKYARSLGMHVHGF
FIIGMPPMCGNAGESIEEMQASYDYAEEAGFSSASFFAASPIVGSELLRECIRQGFVDPE
ESLYRMTYKQGIINVPGLWDGEEIAELAAKFNRDFNARRDRAYTPQKQWNANQY
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
282 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
286 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
289 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
282 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
286 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
289 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
282 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
286 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
289 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA

Catalyzed Reaction

phosphonoacetaldehyde methylase

+ 2 + + +
2-hydroxyethylphosphonic acid(1-)
60991		 S-adenosyl-L-methioninate
67040		 (S)-2-hydroxypropylphosphonate
62246		 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, 3:36 a.m. update curation agent holliday setDomainBoundaries.py
update domain end position 470 534
update domain start position 38 1
Oct. 15, 2016, 5:26 a.m. update curation agent setDomainBoundaries.py holliday
update curation agent holliday setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.