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Reviewed, UniProtKB/Swiss-Prot Q2S990 (SPED_HAHCH)

Last modified June 16, 2009. Version 23. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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- Recommended name:
            S-adenosylmethionine decarboxylase beta chain
    2- Recommended name:
            S-adenosylmethionine decarboxylase alpha chain
Gene names
Name: speD
Ordered Locus Names: HCH_06136
OrganismHahella chejuensis (strain KCTC 2396) [Complete proteome] [HAMAP]
Taxonomic identifier349521 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaOceanospirillalesHahellaceaeHahella

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.

Catalytic activity

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

Cofactor

Pyruvoyl group By similarity.

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.

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_0000273597
Chain113 – 264152S-adenosylmethionine decarboxylase alpha chain By similarity
PRO_0000273598

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
Q2S990-1 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: 7AE2060F8688F4C1

FASTA26430,181
        10         20         30         40         50         60 
MSEKLKLHGF NNLTKSLSFN IYDICYAQSE KHRQEYIAYI DEQYNAERLT QILTDVVEII 

        70         80         90        100        110        120 
GAHILNVSRQ DYDPHGASVT MLIAEHEVPP PADSSEESPG PLPDAVVAHL DKSHVTVHTY 

       130        140        150        160        170        180 
PESHPDNGIS TFRADIDVST CGLISPLKAL NYLIHSFDSD IVTIDYRVRG FTRDIDGAKL 

       190        200        210        220        230        240 
YIDHDINSIQ NFLSEDTQEA YQMIDVNVYQ ENLFHTKMIL KEFNLDNYLF GTGVSELNAN 

       250        260 
EASNIRERLQ KEMLEIFYSR NMPY 

« Hide

References

[1]"Genomic blueprint of Hahella chejuensis, a marine microbe producing an algicidal agent."
Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G., Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K., Oh T.K., Kim J.F.
Nucleic Acids Res. 33:7066-7073(2005) [PubMed: 16352867] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000155 Genomic DNA. Translation: ABC32784.1.
RefSeqYP_437209.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3839656.
GenomeReviewsGene locus HCH_06136 in contig CP000155_GR.
KEGGhch:HCH_06136.
NMPDRfig|349521.5.peg.5379.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ2S990.
OMAQ2S990. YNAERLT.

Enzyme and pathway databases

BioCycHCHE349521:HCH_06136-MON.

Family and domain databases

HAMAPMF_00465.
[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.
PfamPF02675. AdoMet_dc. 1 hit.
[Graphical view]
PIRSFPIRSF001356. SAM_decarboxylas. 1 hit.
TIGRFAMsTIGR03331. SAM_DCase_Eco. 1 hit.
ProtoNetSearch...

Entry information

Entry nameSPED_HAHCH
AccessionPrimary (citable) accession number: Q2S990
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: January 24, 2006
Last modified: June 16, 2009
This is version 23 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents