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A8FG39 (A8FG39_BACP2) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 23. Feed History...

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

Protein namesRecommended name:
S-adenosylmethionine decarboxylase proenzyme HAMAP MF_00464
Short name=AdoMetDC HAMAP MF_00464
Short name=SAMDC HAMAP MF_00464
EC=4.1.1.50 HAMAP MF_00464
Gene names
Name:speD EMBL ABV63206.1
Synonyms:speH HAMAP MF_00464
Ordered Locus Names:BPUM_2546
OrganismBacillus pumilus (strain SAFR-032) [Complete proteome] [HAMAP]
Taxonomic identifier315750 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length127 AA.
Sequence statusComplete.
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. HAMAP MF_00464

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. HAMAP MF_00464

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site641Schiff-base intermediate with substrate; via pyruvic acid By similarity HAMAP MF_00464
Active site691Proton acceptor; for processing activity By similarity HAMAP MF_00464
Active site841Proton donor; for catalytic activity By similarity HAMAP MF_00464
Site63 – 642Cleavage (non-hydrolytic); by autolysis By similarity HAMAP MF_00464

Amino acid modifications

Modified residue641Pyruvic acid (Ser); by autocatalysis By similarity HAMAP MF_00464

Sequences

Sequence LengthMass (Da)Tools
A8FG39 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: B87DCE789A0986A8

FASTA12713,880
        10         20         30         40         50         60 
MMETIGRHVI SELWGCDCDK LNDMDFIEKT FVNAALKSGA EVREVAFHKF APQGVSGVVI 

        70         80         90        100        110        120 
ISESHLTIHS FPEHGYASID VYTCGDLDPN IAADHIGDEL GAETRENIEI PRGMGPVQVK 


QAQVKAL

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000813 Genomic DNA. Translation: ABV63206.1.
RefSeqYP_001487766.1. NC_009848.1.

3D structure databases

ProteinModelPortalA8FG39.
ModBaseSearch...

Protein-protein interaction databases

STRINGA8FG39.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000064562; EBBACP00000062895; EBBACG00000064553.
GeneID5621816.
GenomeReviewsGene locus BPUM_2546 in contig CP000813_GR.
KEGGbpu:BPUM_2546.
PATRIC18969020. VBIBacPum16546_2604.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1586.
GeneTreeEBGT00050000001345.
HOGENOMHBG485559.
OMAMGPVQVK.
ProtClustDBPRK03124.

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 nameA8FG39_BACP2
AccessionPrimary (citable) accession number: A8FG39
Entry history
Integrated into UniProtKB/TrEMBL: November 13, 2007
Last sequence update: November 13, 2007
Last modified: December 14, 2011
This is version 23 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info