Top Level Name

  ⌊ Superfamily (core) Radical SAM

    ⌊ Subgroup B12-binding domain containing

  ⌊ methyltransferase (Class B)

     ⌊ Family P-methyltransferase (PhpK-like)

  ⌊ FunctionalDomain P-methyltransferase PhpK (ID 412962)

Superfamily Assignment Evidence Code(s) ISS
Family Assignment Evidence Code CFM PubMed:21950770
This entry was last updated onJune 10, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Streptomyces viridochromogenes Taxon ID: 1938 490086675 WP_003988629.1 (RefSeq) URP
Streptomyces viridochromogenes DSM 40736 Taxon ID: 591159 302467421 EFL30514.1 (Genbank) URP
Streptomyces viridochromogenes Taxon ID: 1938 51317960 AAU00085.1 (Genbank) URP
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Uniprot

Protein NameAccessionEC Number Identifier
n/a Q5IW50 Q5IW50_STRVR (TrEMBL)
n/a D9XF35 D9XF35_STRVT (TrEMBL)

Sequence

Length of Enzyme (full-length): 549 | Length of Functional Domain: 540

1       10        20        30        40        50        60

MKHCIVVGYHETDMSGEELQLALEHGGDELPAPIRSMLRTKITFGGAHYSYLDALSEVRN
QDRGTDHAYTVSELPSLGTLYLVNYLQEQGHPADFVNSYTFEQDQLVKLLADNPASVAIT
TTFYMMPAPVIEIVRFIRRHNPSVPVIVGGPLVDNQCRAGRDDRLNRFFDRVGADYYVWE
SQGEAALAGVVGAIVDGDVPTEVPNVFLRSATGEWKLTRKRPEANDLNACSVRWNRFDPT
VLGPTLSTRTARSCAFSCAFCDYPERAGALTLADLSTVERELEELADMGVKRVAFIDDTF
NVPMRRFKDLCRMLVRRDFGIEWFSYFRCGHAREPDVYDLMYDSGCRGVLLGIESGDDQV
LLNMDKRATTAHYQYGIEQLKARGIFTHASFVIGFPGESPQTVQNTIDFINRAGPDTFAV
NHWYYMHATPIHVRAPQFELTGNGHTWSHRSMNSREALEAADQIFDSVVNAAWMPVNGLD
FWGVPYLLGKGMDRSEIVRFLELAKPLTVANVSRGSAEEAAAAEHRFREFVTGLDLAPAR
YRTAGSEFR
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
254 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
258 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
261 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
254 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
258 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
261 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
254 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
258 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
261 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA

Catalyzed Reaction

P-methyltransferase

2 + + + +
S-adenosyl-L-methionine zwitterion
59789		 N-Acetyldemethylphosphinothricinate (2-)
86401		 S-adenosyl-L-homocysteine zwitterion
57856		 L-methionine zwitterion
57844		 5'-deoxyadenosine
17319		 N-acetylphosphinatothricinate(2-)
58879

EC: 2.1.1.- | IntEnz: 2.1.1.- | Kegg: 2.1.1.- | BioCyc: 2.1.1.- | BRENDA: 2.1.1.- |

Curation History
Time Change Annotation Old Value New Value
May 14, 2014, 3:03 a.m. update curation agent holliday setDomainBoundaries.py
update domain end position 451 540
update domain start position 73 1
EC number assigned by UniProtKB accession ID.