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A8ALG9 (SPED_CITK8) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 38. 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:speD
Ordered Locus Names:CKO_03248
OrganismCitrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696) [Complete proteome] [HAMAP]
Taxonomic identifier290338 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeCitrobacter

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-Rule MF_00465

Catalytic activity

S-adenosyl-L-methionine = S-adenosyl 3-(methylthio)propylamine + CO2. HAMAP-Rule MF_00465

Cofactor

Pyruvoyl group By similarity. HAMAP-Rule MF_00465

Pathway

Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1. HAMAP-Rule 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-Rule 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 – 111111S-adenosylmethionine decarboxylase beta chain By similarity
PRO_1000013688
Chain112 – 264153S-adenosylmethionine decarboxylase alpha chain By similarity
PRO_0000315014

Sites

Active site1121Schiff-base intermediate with substrate; via pyruvic acid By similarity
Active site1171Proton acceptor; for processing activity By similarity
Active site1401Proton donor; for catalytic activity By similarity
Site111 – 1122Cleavage (non-hydrolytic); by autolysis By similarity

Amino acid modifications

Modified residue1121Pyruvic acid (Ser); by autocatalysis By similarity

Sequences

Sequence LengthMass (Da)Tools
A8ALG9 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: EFA8ACA5EE924EA1

FASTA26430,367
        10         20         30         40         50         60 
MKKLKLHGFN NLTKSLSFCI YDICYAKTAE ERDGYIAYID ELYNANRLTE ILSETCSIIG 

        70         80         90        100        110        120 
ANILNIARQD YEPQGASVTI LVSEEPVDPQ LIDKTEHPGP LPEAVVAHLD KSHICVHTYP 

       130        140        150        160        170        180 
ESHPEGGLCT FRADIEVSTC GVISPLKALN YLIHQLESDI VTIDYRVRGF TRDVNGMKHF 

       190        200        210        220        230        240 
IDHEINSIQN FMSDDMKSLY DMVDVNVYQE NIFHTKMLLK EFDLKHYMFH TKPEDLTETE 

       250        260 
RKEITAALWK EMREIYYGRN IPAV 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000822 Genomic DNA. Translation: ABV14332.1.
RefSeqYP_001454768.1. NC_009792.1.

3D structure databases

ProteinModelPortalA8ALG9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING290338.CKO_03248.

Proteomic databases

PRIDEA8ALG9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV14332; ABV14332; CKO_03248.
GeneID5583015.
KEGGcko:CKO_03248.
PATRIC20389092. VBICitKos71230_2724.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1586.
HOGENOMHOG000116821.
KOK01611.
OMAVKHYIDH.
OrthoDBEOG68Q0SQ.

Enzyme and pathway databases

BioCycCKOS290338:GJ8L-3241-MONOMER.
UniPathwayUPA00331; UER00451.

Family and domain databases

Gene3D3.60.90.10. 1 hit.
HAMAPMF_00465. AdoMetDC_2.
InterProIPR003826. AdoMetDC_fam_prok.
IPR009165. S-AdoMet_deCO2ase_bac.
IPR016067. S-AdoMet_deCO2ase_core.
[Graphical view]
PfamPF02675. AdoMet_dc. 1 hit.
[Graphical view]
PIRSFPIRSF001356. SAM_decarboxylas. 1 hit.
SUPFAMSSF56276. SSF56276. 2 hits.
TIGRFAMsTIGR03331. SAM_DCase_Eco. 1 hit.
ProtoNetSearch...

Entry information

Entry nameSPED_CITK8
AccessionPrimary (citable) accession number: A8ALG9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 23, 2007
Last modified: May 14, 2014
This is version 38 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