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D5U0K8

- D5U0K8_THEAM

UniProt

D5U0K8 - D5U0K8_THEAM

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Protein

S-adenosylmethionine decarboxylase proenzyme

Gene
speH, Tagg_0383
Organism
Thermosphaera aggregans (strain DSM 11486 / M11TL)
Status
Unreviewed - 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 By similarity.UniRule annotation

Catalytic activityi

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

Cofactori

Pyruvoyl group By similarity.UniRule annotation

Pathwayi

Sites

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

DecarboxylaseUniRule annotation, Lyase

Keywords - Biological processi

Polyamine biosynthesisUniRule annotation, Spermidine biosynthesisUniRule annotation

Keywords - Ligandi

PyruvateUniRule annotation, S-adenosyl-L-methionineUniRule annotation, Schiff baseUniRule annotation

Enzyme and pathway databases

BioCyciTAGG633148:GHBI-392-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
Gene namesi
Name:speHUniRule annotation
Ordered Locus Names:Tagg_0383Imported
OrganismiThermosphaera aggregans (strain DSM 11486 / M11TL)Imported
Taxonomic identifieri633148 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiDesulfurococcalesDesulfurococcaceaeThermosphaera
ProteomesiUP000002376: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei66 – 661Pyruvic acid (Ser); by autocatalysis By similarityUniRule 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 By similarity.UniRule annotation

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 By similarity.UniRule annotation

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000216579.
KOiK01611.
OMAiLMAKEHS.

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.

D5U0K8-1 [UniParc]FASTAAdd to Basket

« Hide

MLTLKKVIGK HVYGEAYQCD PAILSDEKAL EKIVRNAAVE GNLTLLDVKA    50
WKINPGVSIV GIILESHISI HTWPEYEFAT IDVYTCGSTS DPIKAFKYII 100
KELKAKKYSM KVSSRDYEEM 120
Length:120
Mass (Da):13,540
Last modified:July 13, 2010 - v1
Checksum:iC804D8608EEC7C8A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001939 Genomic DNA. Translation: ADG90658.1.
RefSeqiWP_013129251.1. NC_014160.1.
YP_003649610.1. NC_014160.1.

Genome annotation databases

EnsemblBacteriaiADG90658; ADG90658; Tagg_0383.
GeneIDi9165396.
KEGGitag:Tagg_0383.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001939 Genomic DNA. Translation: ADG90658.1 .
RefSeqi WP_013129251.1. NC_014160.1.
YP_003649610.1. NC_014160.1.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ADG90658 ; ADG90658 ; Tagg_0383 .
GeneIDi 9165396.
KEGGi tag:Tagg_0383.

Phylogenomic databases

HOGENOMi HOG000216579.
KOi K01611.
OMAi LMAKEHS.

Enzyme and pathway databases

UniPathwayi UPA00331 ; UER00451 .
BioCyci TAGG633148:GHBI-392-MONOMER.

Family and domain databases

Gene3Di 3.60.90.10. 1 hit.
HAMAPi MF_00464. AdoMetDC_1.
InterProi IPR003826. AdoMetDC_fam_prok.
IPR016067. S-AdoMet_deCO2ase_core.
IPR017716. S-AdoMet_deCOase_pro-enz.
[Graphical view ]
Pfami PF02675. AdoMet_dc. 1 hit.
[Graphical view ]
SUPFAMi SSF56276. SSF56276. 1 hit.
TIGRFAMsi TIGR03330. SAM_DCase_Bsu. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 11486 / M11TL.
  2. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: DSM 11486.

Entry informationi

Entry nameiD5U0K8_THEAM
AccessioniPrimary (citable) accession number: D5U0K8
Entry historyi
Integrated into UniProtKB/TrEMBL: July 13, 2010
Last sequence update: July 13, 2010
Last modified: September 3, 2014
This is version 28 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome

External Data

Dasty 3

Similar proteinsi