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O66615 (SPEH_AQUAE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
S-adenosylmethionine decarboxylase proenzyme
Short name=AdoMetDC
Short name=SAMDC
EC=4.1.1.50

Cleaved into the following 2 chains:

  1. S-adenosylmethionine decarboxylase beta chain
  2. S-adenosylmethionine decarboxylase alpha chain
Gene names
Name:speH
Ordered Locus Names:aq_254
OrganismAquifex aeolicus (strain VF5)
Taxonomic identifier224324 [NCBI]
Taxonomic lineageBacteria › Aquificae › Aquificales › Aquificaceae › Aquifex

Protein attributes

Sequence length135 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 6363S-adenosylmethionine decarboxylase beta chain By similarity
PRO_0000030079
Chain64 – 13572S-adenosylmethionine decarboxylase alpha chain By similarity
PRO_0000030080

Sites

Active site641Schiff-base intermediate with substrate; via pyruvic acid By similarity
Active site691Proton acceptor; for processing activity By similarity
Active site841Proton donor; for catalytic activity By similarity
Site63 – 642Cleavage (non-hydrolytic); by autolysis By similarity

Amino acid modifications

Modified residue641Pyruvic acid (Ser); by autocatalysis By similarity

Secondary structure

1 ...................... 135
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O66615 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 3C048331A9118872

FASTA13515,200
        10         20         30         40         50         60 
MAKTLGLHIL ADLYGVDADK IDRVEDIREL LEGAVKYANL TKISSHYYQF QPHGATGVVL 

        70         80         90        100        110        120 
LAESHISIHT WPEHGLATVD VYTCGDPSKA YRAMDYIITQ LNPKRIDKQV HERGIVEEES 

       130 
NQSEAEKLRS ILLQV

« Hide

References

« Hide 'large scale' references
[1]"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.
Nature 392:353-358(1998) [PubMed: 9537320] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VF5.
[2]"Crystal structure of the adenosylmethionine decarboxylase (aq_254) from Aquifex aeolicus VF5."
RIKEN structural genomics initiative (RSGI)
Submitted (OCT-2007) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
Strain: VF5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE000657 Genomic DNA. Translation: AAC06577.1.
PIRC70323.
RefSeqNP_213175.1. NC_000918.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2IIIX-ray2.30A1-135[»]
ProteinModelPortalO66615.
SMRO66615. Positions 2-122.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1192849.
GenomeReviewsGene locus aq_254 in contig AE000657_GR.
KEGGaae:aq_254.
NMPDRfig|224324.1.peg.190.
PATRIC20958138. VBIAquAeo85532_0209.

Phylogenomic databases

HOGENOMHBG485559.
OMANILKPER.
PhylomeDBO66615.
ProtClustDBPRK01236.

Enzyme and pathway databases

BioCycAAEO224324:AQ_254-MONOMER.

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 nameSPEH_AQUAE
AccessionPrimary (citable) accession number: O66615
Entry history
Integrated into UniProtKB/Swiss-Prot: October 24, 2001
Last sequence update: August 1, 1998
Last modified: January 25, 2012
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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