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Q3K5V8 (SPED_PSEPF) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 45. 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:speD
Ordered Locus Names:Pfl01_5109
OrganismPseudomonas fluorescens (strain Pf0-1) [Complete proteome] [HAMAP]
Taxonomic identifier205922 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length264 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_00465

Catalytic activity

S-adenosyl-L-methionine = (5-deoxy-5-adenosyl)(3-aminopropyl)-methylsulfonium salt + CO2. HAMAP MF_00465

Cofactor

Pyruvoyl group By similarity. HAMAP MF_00465

Pathway

Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1. HAMAP MF_00465

Subunit structure

Heterooctamer of four alpha and four beta chains arranged as a tetramer 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_00465

Sequence similarities

Belongs to the prokaryotic AdoMetDC family. Type 2 subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 112112S-adenosylmethionine decarboxylase beta chain By similarity
PRO_0000273601
Chain113 – 264152S-adenosylmethionine decarboxylase alpha chain By similarity
PRO_0000273602

Sites

Active site1131Schiff-base intermediate with substrate; via pyruvic acid By similarity
Active site1181Proton acceptor; for processing activity By similarity
Active site1411Proton donor; for catalytic activity By similarity
Site112 – 1132Cleavage (non-hydrolytic); by autolysis By similarity

Amino acid modifications

Modified residue1131Pyruvic acid (Ser); by autocatalysis By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3K5V8 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: D82085F01F6E6D09

FASTA26430,207
        10         20         30         40         50         60 
MKSKLKLHGF NNLTKTLSFN IYDICYAETP QDQQAYVEYI NQEYNAERLT QILTEVVEII 

        70         80         90        100        110        120 
GANILNIASQ NYEPQGASVT ILISEEPVTP TESQIEESPG PLPEIILAHL DKSHITVHTY 

       130        140        150        160        170        180 
PEIHPDAGIA TFRVDIDVST CGVISPLKAL NFLIHQFDSD IVTVDYRVRG FTRDVEGNKH 

       190        200        210        220        230        240 
FIDHEINSIQ NYLSEDTRDA YQMTDVNVYQ ENLFHTKMLL KNFELDNYLF GDATSNLSSE 

       250        260 
QRAQVTERVK HEMLEIFYAR NMPS

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000094 Genomic DNA. Translation: ABA76846.1.
RefSeqYP_350837.1. NC_007492.2.

3D structure databases

ProteinModelPortalQ3K5V8.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3K5V8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3716449.
GenomeReviewsGene locus Pfl01_5109 in contig CP000094_GR.
KEGGpfo:Pfl01_5109.
PATRIC19892440. VBIPseFlu44242_5126.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1586.
HOGENOMHBG303125.
OMAISTFRAD.
ProtClustDBPRK05462.

Enzyme and pathway databases

BioCycPFLU205922:PFL_5109-MONOMER.

Family and domain databases

HAMAPMF_00465. AdoMetDC_2.
[Tree]
InterProIPR003826. S-AdoMet_decarboxylase-bac/arc.
IPR009165. S-AdoMet_deCO2ase_bac.
IPR016067. S-AdoMet_deCO2ase_core.
[Graphical view]
Gene3DG3DSA:3.60.90.10. SAM_decarbox. 1 hit.
KOK01611.
PfamPF02675. AdoMet_dc. 1 hit.
[Graphical view]
PIRSFPIRSF001356. SAM_decarboxylas. 1 hit.
SUPFAMSSF56276. S-AdenosylMet_decarbase_core. 1 hit.
TIGRFAMsTIGR03331. SAM_DCase_Eco. 1 hit.
ProtoNetSearch...

Entry information

Entry nameSPED_PSEPF
AccessionPrimary (citable) accession number: Q3K5V8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: November 8, 2005
Last modified: January 25, 2012
This is version 45 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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