Skip Header

Contribute Send feedback
Read comments (?) or add your own

B5YF62 (B5YF62_DICT6) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 17. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
S-adenosylmethionine decarboxylase proenzyme HAMAP MF_00464

Short name=AdoMetDC HAMAP MF_00464
Short name=SAMDC HAMAP MF_00464
EC=4.1.1.50 HAMAP MF_00464
Gene names
Name:speH HAMAP MF_00464
Ordered Locus Names:DICTH_1351
OrganismDictyoglomus thermophilum (strain ATCC 35947 / DSM 3960 / H-6-12) [Complete proteome] [HAMAP]
Taxonomic identifier309799 [NCBI]
Taxonomic lineageBacteriaDictyoglomiDictyoglomalesDictyoglomaceaeDictyoglomus

Protein attributes

Sequence length142 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine By similarity. HAMAP MF_00464

Catalytic activity

S-adenosyl-L-methionine = (5-deoxy-5-adenosyl)(3-aminopropyl)-methylsulfonium salt + CO2. HAMAP MF_00464

Cofactor

Pyruvoyl group By similarity. HAMAP MF_00464

Pathway

Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1. HAMAP MF_00464

Subunit structure

Heterotetramer of two alpha and two beta chains arranged as a dimer of alpha/beta heterodimers By similarity. HAMAP MF_00464

Post-translational modification

Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain By similarity. HAMAP MF_00464

Sequence similarities

Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily. HAMAP MF_00464

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site671Schiff-base intermediate with substrate; via pyruvic acid By similarity HAMAP MF_00464
Active site721Proton acceptor; for processing activity By similarity HAMAP MF_00464
Active site871Proton donor; for catalytic activity By similarity HAMAP MF_00464
Site66 – 672Cleavage (non-hydrolytic); by autolysis By similarity HAMAP MF_00464

Amino acid modifications

Modified residue671Pyruvic acid (Ser); by autocatalysis By similarity HAMAP MF_00464

Sequences

Sequence LengthMass (Da)Tools
B5YF62 [UniParc].

Last modified November 25, 2008. Version 1.
Checksum: 79B05749C4B15242

FASTA14216,009
        10         20         30         40         50         60 
MKITGKSLGR HILAEMYNCN REILNDVEKI KEIMVKAAIE AGAEVVEVVF HKFSPYGVSG 

        70         80         90        100        110        120 
VVVISESHLA IHTWPEYGFA AADLFTCGDH VNPWKAFEYL NNYLQAEQFI TFEAKRGILP 

       130        140 
IEAGNFTYKP EENKKEVKET VG 

« Hide

References

[1]"The complete genome sequence of Dictyoglomus thermophilum strain ATCC 35947 / DSM 3960 / H-6-12."
Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.
Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001146 Genomic DNA. Translation: ACI19352.1.
RefSeqYP_002251170.1. NC_011297.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGB5YF62.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6944906.
GenomeReviewsGene locus DICTH_1351 in contig CP001146_GR.
KEGGdth:DICTH_1351.
PATRIC21807326. VBIDicThe33784_1294.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG485559.
OMASYFFKFS.
ProtClustDBCLSK2409695.

Family and domain databases

HAMAPMF_00464. AdoMetDC_1.
[Tree]
InterProIPR003826. S-AdoMet_decarboxylase-bac/arc.
IPR016067. S-AdoMet_deCO2ase_core.
IPR017716. S-AdoMet_deCOase_pro-enz.
[Graphical view]
Gene3DG3DSA:3.60.90.10. SAM_decarbox. 1 hit.
KOK01611.
PfamPF02675. AdoMet_dc. 1 hit.
[Graphical view]
SUPFAMSSF56276. S-AdenosylMet_decarbase_core. 1 hit.
TIGRFAMsTIGR03330. SAM_DCase_Bsu. 1 hit.
ProtoNetSearch...

Entry information

Entry nameB5YF62_DICT6
AccessionPrimary (citable) accession number: B5YF62
Entry history
Integrated into UniProtKB/TrEMBL: November 25, 2008
Last sequence update: November 25, 2008
Last modified: December 14, 2011
This is version 17 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)