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Q8ZBJ7 (SPED_YERPE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
S-adenosylmethionine decarboxylase proenzyme

Short name=AdoMetDC
Short name=SAMDC
EC=4.1.1.50
Gene names
Name:speD
Ordered Locus Names:YPO3412, y0774, YP_0273
OrganismYersinia pestis [Reference proteome] [HAMAP]
Taxonomic identifier632 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

Protein attributes

Sequence length264 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

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. HAMAP-Rule MF_00465

Catalytic activity

S-adenosyl-L-methionine = S-adenosyl 3-(methylthio)propylamine + CO2. HAMAP-Rule MF_00465

Cofactor

Pyruvoyl group By similarity. HAMAP-Rule MF_00465

Pathway

Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1. HAMAP-Rule MF_00465

Subunit structure

Heterooctamer of four alpha and four beta chains arranged as a tetramer of alpha/beta heterodimers By similarity.

Post-translational modification

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. HAMAP-Rule MF_00465

Sequence similarities

Belongs to the prokaryotic AdoMetDC family. Type 2 subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 111111S-adenosylmethionine decarboxylase beta chain By similarity
PRO_0000030075
Chain112 – 264153S-adenosylmethionine decarboxylase alpha chain By similarity
PRO_0000030076

Sites

Active site1121Schiff-base intermediate with substrate; via pyruvic acid By similarity
Active site1171Proton acceptor; for processing activity By similarity
Active site1401Proton donor; for catalytic activity By similarity
Site111 – 1122Cleavage (non-hydrolytic); by autolysis By similarity

Amino acid modifications

Modified residue1121Pyruvic acid (Ser); by autocatalysis By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8ZBJ7 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: E4C0AEE946FEDC89

FASTA26430,293
        10         20         30         40         50         60 
MSKLKLHGFN NLTKSLSFCI YDICYAKTAD DRDGYIAYID EQYNANRLTE ILSETCSIIG 

        70         80         90        100        110        120 
ANILNIARQD YDPQGASVTI LVSEEPVDPR DVDTSEHPGP LPSAVVAHLD KSHICVHTYP 

       130        140        150        160        170        180 
ESHPEAGLCT FRADIEVSTC GVISPLKALN YLIHQLESDI VTMDYRVRGF TRDINGVKHF 

       190        200        210        220        230        240 
IDHKINSIQN FMSDDMKSLY HMMDVNVYQE NIFHTKMMLK DFDLKHYLFN AKPEELSAEE 

       250        260 
KEQITRLLYK EMQEIYYGRN VPEV 

« Hide

References

[1]"Genome sequence of Yersinia pestis, the causative agent of plague."
Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G., Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L., Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M., Chillingworth T., Cronin A., Davies R.M. expand/collapse author list , Davis P., Dougan G., Feltwell T., Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S., Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S., Barrell B.G.
Nature 413:523-527(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CO-92 / Biovar Orientalis.
[2]"Genome sequence of Yersinia pestis KIM."
Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P., Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D., Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A., Nilles M.L. expand/collapse author list , Matson J.S., Blattner F.R., Perry R.D.
J. Bacteriol. 184:4601-4611(2002) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL590842 Genomic DNA. Translation: CAL22001.1.
AE009952 Genomic DNA. Translation: AAM84361.1.
AE017042 Genomic DNA. Translation: AAS60549.1.
PIRAF0414.
RefSeqNP_668110.1. NC_004088.1.
NP_991672.1. NC_005810.1.
YP_002348304.1. NC_003143.1.

3D structure databases

ProteinModelPortalQ8ZBJ7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING214092.YPO3412.

Proteomic databases

PRIDEQ8ZBJ7.

Protocols and materials databases

DNASU1145721.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM84361; AAM84361; y0774.
AAS60549; AAS60549; YP_0273.
GeneID1145721.
1176229.
2766455.
KEGGype:YPO3412.
ypk:y0774.
ypm:YP_0273.

Phylogenomic databases

eggNOGCOG1586.
HOGENOMHOG000116821.
KOK01611.
OMAVKHYIDH.
OrthoDBEOG68Q0SQ.

Enzyme and pathway databases

BioCycYPES214092:GKDD-3366-MONOMER.
UniPathwayUPA00331; UER00451.

Family and domain databases

Gene3D3.60.90.10. 1 hit.
HAMAPMF_00465. AdoMetDC_2.
InterProIPR003826. AdoMetDC_fam_prok.
IPR009165. S-AdoMet_deCO2ase_bac.
IPR016067. S-AdoMet_deCO2ase_core.
[Graphical view]
PfamPF02675. AdoMet_dc. 1 hit.
[Graphical view]
PIRSFPIRSF001356. SAM_decarboxylas. 1 hit.
SUPFAMSSF56276. SSF56276. 2 hits.
TIGRFAMsTIGR03331. SAM_DCase_Eco. 1 hit.
ProtoNetSearch...

Entry information

Entry nameSPED_YERPE
AccessionPrimary (citable) accession number: Q8ZBJ7
Secondary accession number(s): Q0WBN4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: March 1, 2002
Last modified: May 14, 2014
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways