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Q5JDS7 (SPEH_THEKO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
S-adenosylmethionine decarboxylase proenzyme

Short name=AdoMetDC
Short name=SAMDC
EC=4.1.1.50
Gene names
Name:speH
Ordered Locus Names:TK1592
OrganismThermococcus kodakaraensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1)) [Reference proteome] [HAMAP]
Taxonomic identifier69014 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaeThermococcus

Protein attributes

Sequence length143 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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 = S-adenosyl 3-(methylthio)propylamine + 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.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 6565S-adenosylmethionine decarboxylase beta chain By similarity
PRO_0000030147
Chain66 – 14378S-adenosylmethionine decarboxylase alpha chain By similarity
PRO_0000030148

Sites

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

Amino acid modifications

Modified residue661Pyruvic acid (Ser); by autocatalysis By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5JDS7 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: 556F2CEABE1E0C71

FASTA14315,880
        10         20         30         40         50         60 
MTEIETIGFH YVVEAAGCDP EVLGNADRIR QIFLEAAKVG NMEVKASYFF KFSPTGVSGV 

        70         80         90        100        110        120 
VIVAESHISV HTWPEKGYAA LDVYTCGTKA NPEKAVDYIL EQFKAKYAHV SEIKRGIEED 

       130        140 
DETFTHMIMT WEEALRKNGN GSG 

« Hide

References

[1]"Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes."
Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.
Genome Res. 15:352-363(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-918 / JCM 12380 / KOD1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006878 Genomic DNA. Translation: BAD85781.1.
RefSeqYP_184005.1. NC_006624.1.

3D structure databases

ProteinModelPortalQ5JDS7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING69014.TK1592.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD85781; BAD85781; TK1592.
GeneID3234568.
KEGGtko:TK1592.

Phylogenomic databases

eggNOGCOG1586.
HOGENOMHOG000216579.
KOK01611.
OMALMAKEHS.

Enzyme and pathway databases

BioCycTKOD69014:GH72-1624-MONOMER.
UniPathwayUPA00331; UER00451.

Family and domain databases

Gene3D3.60.90.10. 1 hit.
HAMAPMF_00464. AdoMetDC_1.
InterProIPR003826. AdoMetDC_fam_prok.
IPR016067. S-AdoMet_deCO2ase_core.
IPR017716. S-AdoMet_deCOase_pro-enz.
[Graphical view]
PfamPF02675. AdoMet_dc. 1 hit.
[Graphical view]
SUPFAMSSF56276. SSF56276. 1 hit.
TIGRFAMsTIGR03330. SAM_DCase_Bsu. 1 hit.
ProtoNetSearch...

Entry information

Entry nameSPEH_THEKO
AccessionPrimary (citable) accession number: Q5JDS7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: February 15, 2005
Last modified: May 14, 2014
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways