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Q04694 (DCAM_SOLTU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
S-adenosylmethionine decarboxylase proenzyme
Short name=AdoMetDC
Short name=SAMDC
EC=4.1.1.50
Alternative name(s):
Induced stolen tip protein TUB13

Cleaved into the following 2 chains:

  1. S-adenosylmethionine decarboxylase alpha chain
  2. S-adenosylmethionine decarboxylase beta chain
Gene names
Name:SAMDC
Synonyms:TUB13
OrganismSolanum tuberosum (Potato) [Reference proteome]
Taxonomic identifier4113 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Solanaceae › Solanoideae › Solaneae › Solanum

Protein attributes

Sequence length360 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

S-adenosyl-L-methionine = (5-deoxy-5-adenosyl)(3-aminopropyl)-methylsulfonium salt + CO2.

Cofactor

Pyruvoyl group.

Pathway

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

Tissue specificity

Stolon, also expressed in leaves, stems and roots. Ref.1

Developmental stage

Transcribed in the stolon tip during the early stages of tuberization. Maximum expression was in non-swelling stolon tips from stage b, and level declined as the tuber increased in size. Ref.1

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.

Sequence similarities

Belongs to the eukaryotic AdoMetDC family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 7272S-adenosylmethionine decarboxylase beta chain
PRO_0000030023
Chain73 – 360288S-adenosylmethionine decarboxylase alpha chain
PRO_0000030024

Sites

Active site131
Active site161
Active site731Schiff-base intermediate with substrate; via pyruvic acid By similarity
Active site871Proton donor; for catalytic activity By similarity
Active site2361Proton acceptor; for processing activity By similarity
Active site2491Proton acceptor; for processing activity By similarity
Site72 – 732Cleavage (non-hydrolytic); by autolysis

Amino acid modifications

Modified residue731Pyruvic acid (Ser); by autocatalysis

Experimental info

Sequence conflict1741S → P in AAB32507. Ref.2
Sequence conflict2571T → S in AAB32507. Ref.2
Sequence conflict2911V → I in AAB32507. Ref.2
Sequence conflict3051I → T in AAB32507. Ref.2

Secondary structure

1 .......................................................... 360
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q04694 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: EE8165FA54814B46

FASTA36039,726
        10         20         30         40         50         60 
MEMDLPVSAI GFEGFEKRLE ISFVEPGLFA DPNGKGLRSL SKAQLDEILG PAECTIVDNL 

        70         80         90        100        110        120 
SNDYVDSYVL SESSLFVYSY KIIIKTCGTT KLLLAIPPIL RLAETLSLKV QDVRYTRGSF 

       130        140        150        160        170        180 
IFPGAQSFPH RHFSEEVAVL DGYFGKLAAG SKAVIMGSPD KTQKWHVYSA SAGSVQSNDP 

       190        200        210        220        230        240 
VYTLEMCMTG LDREKASVFY KTEESSAAHM TVRSGIRKIL PKSEICDFEF EPCGYSMNSI 

       250        260        270        280        290        300 
EGAAVSTIHI TPEDGFTYAS FESVGYNPKT MELGPLVERV LACFEPAEFS VALHADVATK 

       310        320        330        340        350        360 
LLERICSVDV KGYSLAEWSP EEFGEGGSIV YQKFTRTPYC ESPKSVLKGC WKEEEKEGKE

« Hide

References

[1]"Expression and sequence analysis of cDNAs induced during the early stages of tuberisation in different organs of the potato plant (Solanum tuberosum L.)."
Taylor M.A., Mad Arif S.A., Kumar A., Davies H.V., Scobie L.A., Pearce S.R., Flavell A.J.
Plant Mol. Biol. 20:641-651(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Strain: cv. Record.
Tissue: Stolon tip.
[2]"Characterisation of the S-adenosylmethionine decarboxylase (SAMDC) gene of potato."
Mad Arif S.A., Taylor M.A., George L.A., Butler A.R., Burch L.R., Davies H.V., Stark M.J., Kumar A.
Plant Mol. Biol. 26:327-338(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: cv. Desiree.
[3]"Monomeric S-adenosylmethionine decarboxylase from plants provides an alternative to putrescine stimulation."
Bennett E.M., Ekstrom J.L., Pegg A.E., Ealick S.E.
Biochemistry 41:14509-14517(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z11680 mRNA. Translation: CAA77742.1.
S74514 Genomic DNA. Translation: AAB32507.1.
PIRS52662.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MHMX-ray2.30A74-360[»]
B1-72[»]
ProteinModelPortalQ04694.
SMRQ04694. Positions 15-72, 74-337.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00331; UER00451.

Family and domain databases

Gene3D3.60.90.10. 1 hit.
InterProIPR001985. S-AdoMet_decarboxylase.
IPR018167. S-AdoMet_decarboxylase_subgr.
IPR016067. S-AdoMet_deCO2ase_core.
IPR018166. S-AdoMet_deCO2ase_CS.
[Graphical view]
PANTHERPTHR11570. PTHR11570. 1 hit.
PfamPF01536. SAM_decarbox. 1 hit.
[Graphical view]
PIRSFPIRSF001355. S-AdenosylMet_decarboxylase. 1 hit.
SUPFAMSSF56276. S-AdenosylMet_decarbase_core. 1 hit.
TIGRFAMsTIGR00535. SAM_DCase. 1 hit.
PROSITEPS01336. ADOMETDC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ04694.

Entry information

Entry nameDCAM_SOLTU
AccessionPrimary (citable) accession number: Q04694
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: May 1, 2013
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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