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O28663 (SPEH_ARCFU) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:AF_1610
OrganismArchaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Taxonomic identifier224325 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Archaeoglobi › Archaeoglobales › Archaeoglobaceae › Archaeoglobus

Protein attributes

Sequence length112 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 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 – 6161S-adenosylmethionine decarboxylase beta chain By similarity
PRO_0000030131
Chain62 – 11251S-adenosylmethionine decarboxylase alpha chain By similarity
PRO_0000030132

Sites

Active site621Schiff-base intermediate with substrate; via pyruvic acid By similarity
Active site671Proton acceptor; for processing activity By similarity
Active site821Proton donor; for catalytic activity By similarity
Site61 – 622Cleavage (non-hydrolytic); by autolysis By similarity

Amino acid modifications

Modified residue621Pyruvic acid (Ser); by autocatalysis By similarity

Sequences

Sequence LengthMass (Da)Tools
O28663 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 95B250A1306D2F30

FASTA11212,733
        10         20         30         40         50         60 
MIVGRHIIAE LYGVKEELIA KEEVVRSIVE EVVDKAELTK VGSVYKQFNP HGVTGIVLIA 

        70         80         90        100        110 
ESHVSIHTWP EYGLVNLDIF TCGDTSKVEK AFKLFLEKFK PESYRHYVLD RG

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE000782 Genomic DNA. Translation: AAB89640.1.
PIRA69451.
RefSeqNP_070439.1. NC_000917.1.

3D structure databases

ProteinModelPortalO28663.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1484835.
GenomeReviewsGene locus AF_1610 in contig AE000782_GR.
KEGGafu:AF1610.
NMPDRfig|224325.1.peg.1600.
TIGRAF_1610.

Phylogenomic databases

HOGENOMHBG485559.
OMANILKPER.
ProtClustDBPRK01236.

Enzyme and pathway databases

BioCycAFUL224325:AF_1610-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_ARCFU
AccessionPrimary (citable) accession number: O28663
Entry history
Integrated into UniProtKB/Swiss-Prot: October 24, 2001
Last sequence update: January 1, 1998
Last modified: November 16, 2011
This is version 74 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

SIMILARITY comments

Index of protein domains and families

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