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Protein

S-adenosylmethionine decarboxylase proenzyme

Gene

speD

Organism
Yersinia pestis
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
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

  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

BioCyciYPES214092:GKDD-3366-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:YPO3412, y0774, YP_0273
OrganismiYersinia pestis
Taxonomic identifieri632 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia
ProteomesiUP000000815: Chromosome, UP000001019: Chromosome, UP000002490: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 111111S-adenosylmethionine decarboxylase beta chainUniRule annotationPRO_0000030075Add
BLAST
Chaini112 – 264153S-adenosylmethionine decarboxylase alpha chainUniRule annotationPRO_0000030076Add
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

PRIDEiQ8ZBJ7.

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

STRINGi214092.YPO3412.

Structurei

3D structure databases

ProteinModelPortaliQ8ZBJ7.
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.

Q8ZBJ7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSKLKLHGFN NLTKSLSFCI YDICYAKTAD DRDGYIAYID EQYNANRLTE
60 70 80 90 100
ILSETCSIIG ANILNIARQD YDPQGASVTI LVSEEPVDPR DVDTSEHPGP
110 120 130 140 150
LPSAVVAHLD KSHICVHTYP ESHPEAGLCT FRADIEVSTC GVISPLKALN
160 170 180 190 200
YLIHQLESDI VTMDYRVRGF TRDINGVKHF IDHKINSIQN FMSDDMKSLY
210 220 230 240 250
HMMDVNVYQE NIFHTKMMLK DFDLKHYLFN AKPEELSAEE KEQITRLLYK
260
EMQEIYYGRN VPEV
Length:264
Mass (Da):30,293
Last modified:March 1, 2002 - v1
Checksum:iE4C0AEE946FEDC89
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL590842 Genomic DNA. Translation: CAL22001.1.
AE009952 Genomic DNA. Translation: AAM84361.1.
AE017042 Genomic DNA. Translation: AAS60549.1.
PIRiAF0414.
RefSeqiNP_668110.1. NC_004088.1.
NP_991672.1. NC_005810.1.
YP_002348304.1. NC_003143.1.

Genome annotation databases

EnsemblBacteriaiAAM84361; AAM84361; y0774.
AAS60549; AAS60549; YP_0273.
GeneIDi1145721.
1176229.
2766455.
KEGGiype:YPO3412.
ypk:y0774.
ypm:YP_0273.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL590842 Genomic DNA. Translation: CAL22001.1.
AE009952 Genomic DNA. Translation: AAM84361.1.
AE017042 Genomic DNA. Translation: AAS60549.1.
PIRiAF0414.
RefSeqiNP_668110.1. NC_004088.1.
NP_991672.1. NC_005810.1.
YP_002348304.1. NC_003143.1.

3D structure databases

ProteinModelPortaliQ8ZBJ7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi214092.YPO3412.

Proteomic databases

PRIDEiQ8ZBJ7.

Protocols and materials databases

DNASUi1145721.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAM84361; AAM84361; y0774.
AAS60549; AAS60549; YP_0273.
GeneIDi1145721.
1176229.
2766455.
KEGGiype:YPO3412.
ypk:y0774.
ypm:YP_0273.

Phylogenomic databases

eggNOGiCOG1586.
HOGENOMiHOG000116821.
KOiK01611.
OMAiICYAKTP.
OrthoDBiEOG68Q0SQ.

Enzyme and pathway databases

UniPathwayiUPA00331; UER00451.
BioCyciYPES214092:GKDD-3366-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: CO-92 / Biovar Orientalis.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: KIM10+ / Biovar Mediaevalis.
  3. "Complete genome sequence of Yersinia pestis strain 91001, an isolate avirulent to humans."
    Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D., Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L., Dai R.
    , Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H., Wang J., Huang P., Yang R.
    DNA Res. 11:179-197(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 91001 / Biovar Mediaevalis.

Entry informationi

Entry nameiSPED_YERPE
AccessioniPrimary (citable) accession number: Q8ZBJ7
Secondary accession number(s): Q0WBN4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: March 1, 2002
Last modified: January 7, 2015
This is version 93 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.