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Protein

S-adenosylmethionine decarboxylase proenzyme

Gene

speD

Organism
Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696)
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

Pathway: 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 (speD)
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
Sitei111 – 1122Cleavage (non-hydrolytic); by autolysisUniRule annotation
Active sitei112 – 1121Schiff-base intermediate with substrate; via pyruvic acidUniRule annotation
Active sitei117 – 1171Proton acceptor; for processing activityUniRule annotation
Active sitei140 – 1401Proton 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

BioCyciCKOS290338:GJ8L-3241-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:speDUniRule annotation
Ordered Locus Names:CKO_03248
OrganismiCitrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696)
Taxonomic identifieri290338 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeCitrobacter
ProteomesiUP000008148 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 111111S-adenosylmethionine decarboxylase beta chainUniRule annotationPRO_1000013688Add
BLAST
Chaini112 – 264153S-adenosylmethionine decarboxylase alpha chainUniRule annotationPRO_0000315014Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei112 – 1121Pyruvic 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

Proteomic databases

PRIDEiA8ALG9.

Interactioni

Subunit structurei

Heterooctamer of four alpha and four beta chains arranged as a tetramer of alpha/beta heterodimers.UniRule annotation

Protein-protein interaction databases

STRINGi290338.CKO_03248.

Structurei

3D structure databases

ProteinModelPortaliA8ALG9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the prokaryotic AdoMetDC family. Type 2 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG1586.
HOGENOMiHOG000116821.
KOiK01611.
OMAiICYAKTP.
OrthoDBiEOG68Q0SQ.

Family and domain databases

Gene3Di3.60.90.10. 1 hit.
HAMAPiMF_00465. AdoMetDC_2.
InterProiIPR003826. AdoMetDC_fam_prok.
IPR009165. S-AdoMet_deCO2ase_bac.
IPR016067. S-AdoMet_deCO2ase_core.
[Graphical view]
PfamiPF02675. AdoMet_dc. 1 hit.
[Graphical view]
PIRSFiPIRSF001356. SAM_decarboxylas. 1 hit.
SUPFAMiSSF56276. SSF56276. 2 hits.
TIGRFAMsiTIGR03331. SAM_DCase_Eco. 1 hit.

Sequencei

Sequence statusi: Complete.

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

A8ALG9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKLKLHGFN NLTKSLSFCI YDICYAKTAE ERDGYIAYID ELYNANRLTE
60 70 80 90 100
ILSETCSIIG ANILNIARQD YEPQGASVTI LVSEEPVDPQ LIDKTEHPGP
110 120 130 140 150
LPEAVVAHLD KSHICVHTYP ESHPEGGLCT FRADIEVSTC GVISPLKALN
160 170 180 190 200
YLIHQLESDI VTIDYRVRGF TRDVNGMKHF IDHEINSIQN FMSDDMKSLY
210 220 230 240 250
DMVDVNVYQE NIFHTKMLLK EFDLKHYMFH TKPEDLTETE RKEITAALWK
260
EMREIYYGRN IPAV
Length:264
Mass (Da):30,367
Last modified:October 23, 2007 - v1
Checksum:iEFA8ACA5EE924EA1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000822 Genomic DNA. Translation: ABV14332.1.
RefSeqiWP_012134037.1. NC_009792.1.

Genome annotation databases

EnsemblBacteriaiABV14332; ABV14332; CKO_03248.
KEGGicko:CKO_03248.
PATRICi20389092. VBICitKos71230_2724.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000822 Genomic DNA. Translation: ABV14332.1.
RefSeqiWP_012134037.1. NC_009792.1.

3D structure databases

ProteinModelPortaliA8ALG9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi290338.CKO_03248.

Proteomic databases

PRIDEiA8ALG9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABV14332; ABV14332; CKO_03248.
KEGGicko:CKO_03248.
PATRICi20389092. VBICitKos71230_2724.

Phylogenomic databases

eggNOGiCOG1586.
HOGENOMiHOG000116821.
KOiK01611.
OMAiICYAKTP.
OrthoDBiEOG68Q0SQ.

Enzyme and pathway databases

UniPathwayiUPA00331; UER00451.
BioCyciCKOS290338:GJ8L-3241-MONOMER.

Family and domain databases

Gene3Di3.60.90.10. 1 hit.
HAMAPiMF_00465. AdoMetDC_2.
InterProiIPR003826. AdoMetDC_fam_prok.
IPR009165. S-AdoMet_deCO2ase_bac.
IPR016067. S-AdoMet_deCO2ase_core.
[Graphical view]
PfamiPF02675. AdoMet_dc. 1 hit.
[Graphical view]
PIRSFiPIRSF001356. SAM_decarboxylas. 1 hit.
SUPFAMiSSF56276. SSF56276. 2 hits.
TIGRFAMsiTIGR03331. SAM_DCase_Eco. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-895 / CDC 4225-83 / SGSC4696.

Entry informationi

Entry nameiSPED_CITK8
AccessioniPrimary (citable) accession number: A8ALG9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 23, 2007
Last modified: June 24, 2015
This is version 47 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.