Top Level Name

  ⌊ Superfamily (extended) Radical SAM 3-amino-3-carboxypropyl Radical Forming

    ⌊ Subgroup Diphthamide biosynthesis

     ⌊ Family Diphthamide biosynthesis family (Dph2)

  ⌊ FunctionalDomain S-adenosyl-L-methionine:L-histidine 3-amino-3-carboxypropyltransferase (ID 430921)

Superfamily Assignment Evidence Code(s) FSM PubMed:20559380
Family Assignment Evidence Code CFM ISS PubMed:20559380
This entry was last updated onJune 10, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Pyrococcus horikoshii Taxon ID: 53953 300508514
Pyrococcus horikoshii Taxon ID: 53953 300508513
Pyrococcus horikoshii Taxon ID: 53953 299689143
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Uniprot

Protein NameAccessionEC Number Identifier
2-(3-amino-3-carboxypropyl)histidine synthase O58832 DPH2_PYRHO (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 378 | Length of Functional Domain: 370

1       10        20        30        40        50        60

MGSHHHHHHDITSLYKKAGSAAAVLEENLYFQGSFTMLHEIPKSEILKELKRIGAKRVLI
QSPEGLRREAEELAGFLEENNIEVFLHGEINYGACDPADREAKLVGCDALIHLGHSYMKL
PLEVPTIFVPAFARVSVVEALKENIGEIKKLGRKIIVTTTAQHIHQLKEAKEFLESEGFE
VSIGRGDSRISWPGQVLGCNYSVAKVRGEGILFIGSGIFHPLGLAVATRKKVLAIDPYTK
AFSWIDPERFIRKRWAQIAKAMDAKKFGVIVSIKKGQLRLAEAKRIVKLLKKHGREARLI
VMNDVNYHKLEGFPFEAYVVVACPRVPLDDYGAWRKPVLTPKEVEILLGLREEYEFDEIL
GGPRESDEPFGISIHSTR
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

Subgroup CAR This EFD conserves 2/2 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
95 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
323 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
Family CAR This EFD conserves 1/3 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
96 Asp (D) side chain MISMATCH: This residue does not match the specified amino acid type of C, and thus may not function in the same manner as other sequences in the family
117 Tyr (Y) side chain MISMATCH: This residue does not match the specified amino acid type of C, and thus may not function in the same manner as other sequences in the family
323 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
3LZC Crystal Structure Of Dph2 From Pyrococcus Horikoshii Dph2 2 2.26 CSA • PDB • PDBSum
3LZD Crystal Structure Of Dph2 From Pyrococcus Horikoshii With 4Fe-4S Cluster Dph2 2 2.1 Iron/Sulfur Cluster • Sulfate Ion 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 5, 2014, 2:23 a.m. update curation agent holliday setDomainBoundaries.py
update domain end position 378 372
update domain start position 14 3
EC number assigned by UniProtKB accession ID.