Skip Header

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

D5U0K8 (D5U0K8_THEAM) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 20. 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
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-Rule MF_00464
Short name=AdoMetDC HAMAP-Rule MF_00464
Short name=SAMDC HAMAP-Rule MF_00464
EC=4.1.1.50 HAMAP-Rule MF_00464
Gene names
Name:speH HAMAP-Rule MF_00464
Ordered Locus Names:Tagg_0383
OrganismThermosphaera aggregans (strain DSM 11486 / M11TL) [Complete proteome] [HAMAP] EMBL ADG90658.1
Taxonomic identifier633148 [NCBI]
Taxonomic lineageArchaea › Crenarchaeota › Thermoprotei › Desulfurococcales › Desulfurococcaceae › Thermosphaera ›

Protein attributes

Sequence length120 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-Rule MF_00464

Catalytic activity

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

Cofactor

Pyruvoyl group By similarity. HAMAP-Rule MF_00464

Pathway

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

Subunit structure

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

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site661Schiff-base intermediate with substrate; via pyruvic acid By similarity HAMAP-Rule MF_00464
Active site711Proton acceptor; for processing activity By similarity HAMAP-Rule MF_00464
Active site861Proton donor; for catalytic activity By similarity HAMAP-Rule MF_00464
Site65 – 662Cleavage (non-hydrolytic); by autolysis By similarity HAMAP-Rule MF_00464

Amino acid modifications

Modified residue661Pyruvic acid (Ser); by autocatalysis By similarity HAMAP-Rule MF_00464

Sequences

Sequence LengthMass (Da)Tools
D5U0K8 [UniParc].

Last modified July 13, 2010. Version 1.
Checksum: C804D8608EEC7C8A

FASTA12013,540
        10         20         30         40         50         60 
MLTLKKVIGK HVYGEAYQCD PAILSDEKAL EKIVRNAAVE GNLTLLDVKA WKINPGVSIV 

        70         80         90        100        110        120 
GIILESHISI HTWPEYEFAT IDVYTCGSTS DPIKAFKYII KELKAKKYSM KVSSRDYEEM

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001939 Genomic DNA. Translation: ADG90658.1.
RefSeqYP_003649610.1. NC_014160.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADG90658; ADG90658; Tagg_0383.
GeneID9165396.
KEGGtag:Tagg_0383.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000216579.
KOK01611.
OMALMAKEHS.

Enzyme and pathway databases

UniPathwayUPA00331; UER00451.

Family and domain databases

Gene3D3.60.90.10. 1 hit.
HAMAPMF_00464. AdoMetDC_1.
InterProIPR003826. S-AdoMet_decarboxylase-bac/arc.
IPR016067. S-AdoMet_deCO2ase_core.
IPR017716. S-AdoMet_deCOase_pro-enz.
[Graphical view]
PfamPF02675. AdoMet_dc. 1 hit.
[Graphical view]
SUPFAMSSF56276. S-AdenosylMet_decarbase_core. 1 hit.
TIGRFAMsTIGR03330. SAM_DCase_Bsu. 1 hit.
ProtoNetSearch...

Entry information

Entry nameD5U0K8_THEAM
AccessionPrimary (citable) accession number: D5U0K8
Entry history
Integrated into UniProtKB/TrEMBL: July 13, 2010
Last sequence update: July 13, 2010
Last modified: May 1, 2013
This is version 20 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info