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Protein

S-adenosylmethionine decarboxylase proenzyme

Gene

speH

Organism
Thermosphaera aggregans (strain DSM 11486 / M11TL)
Status
Unreviewed-Annotation score: -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: 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)DescriptionActionsGraphical viewLength
Active sitei66Schiff-base intermediate with substrate; via pyruvic acidUniRule annotation1
Active sitei71Proton acceptor; for processing activityUniRule annotation1
Active sitei86Proton donor; for catalytic activityUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDecarboxylaseUniRule annotation, Lyase
Biological processPolyamine biosynthesisUniRule annotation, Spermidine biosynthesisUniRule annotation
LigandPyruvateUniRule annotation, S-adenosyl-L-methionineUniRule annotation, Schiff baseUniRule annotation

Enzyme and pathway databases

BioCyciTAGG633148:G1GKM-386-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 alpha chainUniRule annotation
S-adenosylmethionine decarboxylase beta chainUniRule annotation
Gene namesi
Name:speHUniRule annotation
Ordered Locus Names:Tagg_0383Imported
OrganismiThermosphaera aggregans (strain DSM 11486 / M11TL)Imported
Taxonomic identifieri633148 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiDesulfurococcalesDesulfurococcaceaeThermosphaera
Proteomesi
  • UP000002376 Componenti: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei66Pyruvic acid (Ser); by autocatalysisUniRule annotation1

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)DescriptionActionsGraphical viewLength
Sitei65 – 66Cleavage (non-hydrolytic); by autolysisUniRule annotation2

Keywords - PTMi

Autocatalytic cleavageUniRule annotation, ZymogenUniRule annotation

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

STRINGi633148.Tagg_0383

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiarCOG00279 Archaea
COG1586 LUCA
HOGENOMiHOG000216579
KOiK01611
OMAiLCVHQFS
OrthoDBiPOG093Z0GPL

Family and domain databases

HAMAPiMF_00464 AdoMetDC_1, 1 hit
InterProiView protein in InterPro
IPR003826 AdoMetDC_fam_prok
IPR016067 S-AdoMet_deCO2ase_core
IPR017716 S-AdoMet_deCOase_pro-enz
PANTHERiPTHR33866 PTHR33866, 1 hit
PfamiView protein in Pfam
PF02675 AdoMet_dc, 1 hit
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.

D5U0K8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLTLKKVIGK HVYGEAYQCD PAILSDEKAL EKIVRNAAVE GNLTLLDVKA
60 70 80 90 100
WKINPGVSIV GIILESHISI HTWPEYEFAT IDVYTCGSTS DPIKAFKYII
110 120
KELKAKKYSM KVSSRDYEEM
Length:120
Mass (Da):13,540
Last modified:July 13, 2010 - v1
Checksum:iC804D8608EEC7C8A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001939 Genomic DNA Translation: ADG90658.1
RefSeqiWP_013129251.1, NC_014160.1

Genome annotation databases

EnsemblBacteriaiADG90658; ADG90658; Tagg_0383
GeneIDi9165396
KEGGitag:Tagg_0383

Similar proteinsi

Entry informationi

Entry nameiD5U0K8_THEAM
AccessioniPrimary (citable) accession number: D5U0K8
Entry historyiIntegrated into UniProtKB/TrEMBL: July 13, 2010
Last sequence update: July 13, 2010
Last modified: March 28, 2018
This is version 50 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

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