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Protein

S-adenosylmethionine decarboxylase proenzyme

Gene

speH

Organism
Aquifex aeolicus (strain VF5)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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: S-adenosylmethioninamine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes S-adenosylmethioninamine from S-adenosyl-L-methionine.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. S-adenosylmethionine decarboxylase proenzyme (speH)
This subpathway is part of the pathway S-adenosylmethioninamine biosynthesis, which is itself part of Amine and polyamine biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes S-adenosylmethioninamine from S-adenosyl-L-methionine, the pathway S-adenosylmethioninamine biosynthesis and in Amine and polyamine biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei64 – 641Schiff-base intermediate with substrate; via pyruvic acidUniRule annotation
Active sitei69 – 691Proton acceptor; for processing activityUniRule annotation
Active sitei84 – 841Proton donor; for catalytic activityUniRule annotation

GO - Molecular functioni

GO - Biological processi

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

BioCyciAAEO224324:GJBH-190-MONOMER.
BRENDAi4.1.1.50. 396.
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:aq_254
OrganismiAquifex aeolicus (strain VF5)
Taxonomic identifieri224324 [NCBI]
Taxonomic lineageiBacteriaAquificaeAquificalesAquificaceaeAquifex
Proteomesi
  • UP000000798 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 6363S-adenosylmethionine decarboxylase beta chainUniRule annotationPRO_0000030079Add
BLAST
Chaini64 – 13572S-adenosylmethionine decarboxylase alpha chainUniRule annotationPRO_0000030080Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei64 – 641Pyruvic 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei63 – 642Cleavage (non-hydrolytic); by autolysisUniRule 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

STRINGi224324.aq_254.

Structurei

Secondary structure

1
135
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 1513Combined sources
Helixi18 – 203Combined sources
Beta strandi21 – 233Combined sources
Helixi24 – 3714Combined sources
Beta strandi42 – 498Combined sources
Beta strandi51 – 533Combined sources
Beta strandi55 – 617Combined sources
Beta strandi65 – 717Combined sources
Helixi72 – 743Combined sources
Beta strandi76 – 8510Combined sources
Helixi87 – 10115Combined sources
Beta strandi104 – 11613Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IIIX-ray2.30A1-135[»]
ProteinModelPortaliO66615.
SMRiO66615. Positions 2-122.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO66615.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105X3E. Bacteria.
COG1586. LUCA.
HOGENOMiHOG000216579.
InParanoidiO66615.
KOiK01611.
OMAiAHVSEIK.
OrthoDBiPOG091H02FE.

Family and domain databases

Gene3Di3.60.90.10. 1 hit.
HAMAPiMF_00464. AdoMetDC_1. 1 hit.
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.

O66615-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKTLGLHIL ADLYGVDADK IDRVEDIREL LEGAVKYANL TKISSHYYQF
60 70 80 90 100
QPHGATGVVL LAESHISIHT WPEHGLATVD VYTCGDPSKA YRAMDYIITQ
110 120 130
LNPKRIDKQV HERGIVEEES NQSEAEKLRS ILLQV
Length:135
Mass (Da):15,200
Last modified:August 1, 1998 - v1
Checksum:i3C048331A9118872
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000657 Genomic DNA. Translation: AAC06577.1.
PIRiC70323.
RefSeqiNP_213175.1. NC_000918.1.
WP_010880113.1. NC_000918.1.

Genome annotation databases

EnsemblBacteriaiAAC06577; AAC06577; aq_254.
GeneIDi1192849.
KEGGiaae:aq_254.
PATRICi20958138. VBIAquAeo85532_0209.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000657 Genomic DNA. Translation: AAC06577.1.
PIRiC70323.
RefSeqiNP_213175.1. NC_000918.1.
WP_010880113.1. NC_000918.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IIIX-ray2.30A1-135[»]
ProteinModelPortaliO66615.
SMRiO66615. Positions 2-122.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224324.aq_254.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC06577; AAC06577; aq_254.
GeneIDi1192849.
KEGGiaae:aq_254.
PATRICi20958138. VBIAquAeo85532_0209.

Phylogenomic databases

eggNOGiENOG4105X3E. Bacteria.
COG1586. LUCA.
HOGENOMiHOG000216579.
InParanoidiO66615.
KOiK01611.
OMAiAHVSEIK.
OrthoDBiPOG091H02FE.

Enzyme and pathway databases

UniPathwayiUPA00331; UER00451.
BioCyciAAEO224324:GJBH-190-MONOMER.
BRENDAi4.1.1.50. 396.

Miscellaneous databases

EvolutionaryTraceiO66615.

Family and domain databases

Gene3Di3.60.90.10. 1 hit.
HAMAPiMF_00464. AdoMetDC_1. 1 hit.
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...

Entry informationi

Entry nameiSPEH_AQUAE
AccessioniPrimary (citable) accession number: O66615
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 24, 2001
Last sequence update: August 1, 1998
Last modified: September 7, 2016
This is version 102 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.