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Protein

S-adenosylmethionine decarboxylase proenzyme

Gene

speH

Organism
Bacillus cereus subsp. cytotoxis (strain NVH 391-98)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

S-adenosyl-L-methionine = S-adenosyl 3-(methylthio)propylamine + CO2.UniRule annotation

Cofactori

pyruvateUniRule annotationNote: Binds 1 pyruvoyl group covalently per subunit.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei65 – 662Cleavage (non-hydrolytic); by autolysisUniRule annotation
Active sitei66 – 661Schiff-base intermediate with substrate; via pyruvic acidUniRule annotation
Active sitei71 – 711Proton acceptor; for processing activityUniRule annotation
Active sitei86 – 861Proton donor; for catalytic activityUniRule annotation

GO - Molecular functioni

  1. adenosylmethionine decarboxylase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. S-adenosylmethioninamine biosynthetic process Source: UniProtKB-HAMAP
  2. spermidine biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

Polyamine biosynthesis, Spermidine biosynthesis

Keywords - Ligandi

Pyruvate, S-adenosyl-L-methionine, Schiff base

Enzyme and pathway databases

BioCyciBCYT315749:GH2A-3377-MONOMER.
UniPathwayiUPA00331; UER00451.

Names & Taxonomyi

Protein namesi
Recommended name:
S-adenosylmethionine decarboxylase proenzymeUniRule annotation (EC:4.1.1.50UniRule annotation)
Short name:
AdoMetDCUniRule annotation
Short name:
SAMDCUniRule annotation
Cleaved into the following 2 chains:
S-adenosylmethionine decarboxylase beta chainUniRule annotation
S-adenosylmethionine decarboxylase alpha chainUniRule annotation
Gene namesi
Name:speHUniRule annotation
Ordered Locus Names:Bcer98_3267
OrganismiBacillus cereus subsp. cytotoxis (strain NVH 391-98)
Taxonomic identifieri315749 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
ProteomesiUP000002300 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 6565S-adenosylmethionine decarboxylase beta chainUniRule annotationPRO_1000081168Add
BLAST
Chaini66 – 13065S-adenosylmethionine decarboxylase alpha chainUniRule annotationPRO_1000081169Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei66 – 661Pyruvic acid (Ser); by autocatalysisUniRule annotation

Post-translational modificationi

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.UniRule annotation

Keywords - PTMi

Autocatalytic cleavage, Zymogen

Interactioni

Subunit structurei

Heterotetramer of two alpha and two beta chains arranged as a dimer of alpha/beta heterodimers.UniRule annotation

Protein-protein interaction databases

STRINGi315749.Bcer98_3267.

Family & Domainsi

Sequence similaritiesi

Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG1586.
HOGENOMiHOG000216579.
KOiK01611.
OMAiAAMDIFT.
OrthoDBiEOG6358J6.

Family and domain databases

Gene3Di3.60.90.10. 1 hit.
HAMAPiMF_00464. AdoMetDC_1.
InterProiIPR003826. AdoMetDC_fam_prok.
IPR016067. S-AdoMet_deCO2ase_core.
IPR017716. S-AdoMet_deCOase_pro-enz.
[Graphical view]
PfamiPF02675. AdoMet_dc. 1 hit.
[Graphical view]
SUPFAMiSSF56276. SSF56276. 1 hit.
TIGRFAMsiTIGR03330. SAM_DCase_Bsu. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

A7GTM8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDTMDTMGRH VIAELWDCDF DKLNDMPFIE QLFVDAALRA GAEVREVAFH
60 70 80 90 100
KFAPQGVSGV VIISESHLTI HSFPEHGYAS IDVYTCGDRI DPNVAAEYIA
110 120 130
EGLNAKTRES IELPRGTGSF EIKQRETKAL
Length:130
Mass (Da):14,471
Last modified:September 10, 2007 - v1
Checksum:i12AD847064A61956
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000764 Genomic DNA. Translation: ABS23486.1.
RefSeqiYP_001376481.1. NC_009674.1.

Genome annotation databases

EnsemblBacteriaiABS23486; ABS23486; Bcer98_3267.
KEGGibcy:Bcer98_3267.
PATRICi18935176. VBIBacCyt128034_3429.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000764 Genomic DNA. Translation: ABS23486.1.
RefSeqiYP_001376481.1. NC_009674.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi315749.Bcer98_3267.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABS23486; ABS23486; Bcer98_3267.
KEGGibcy:Bcer98_3267.
PATRICi18935176. VBIBacCyt128034_3429.

Phylogenomic databases

eggNOGiCOG1586.
HOGENOMiHOG000216579.
KOiK01611.
OMAiAAMDIFT.
OrthoDBiEOG6358J6.

Enzyme and pathway databases

UniPathwayiUPA00331; UER00451.
BioCyciBCYT315749:GH2A-3377-MONOMER.

Family and domain databases

Gene3Di3.60.90.10. 1 hit.
HAMAPiMF_00464. AdoMetDC_1.
InterProiIPR003826. AdoMetDC_fam_prok.
IPR016067. S-AdoMet_deCO2ase_core.
IPR017716. S-AdoMet_deCOase_pro-enz.
[Graphical view]
PfamiPF02675. AdoMet_dc. 1 hit.
[Graphical view]
SUPFAMiSSF56276. SSF56276. 1 hit.
TIGRFAMsiTIGR03330. SAM_DCase_Bsu. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: NVH 391-98.

Entry informationi

Entry nameiSPEH_BACCN
AccessioniPrimary (citable) accession number: A7GTM8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 19, 2008
Last sequence update: September 10, 2007
Last modified: March 31, 2015
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.