UniProtKB - Q04694 (DCAM_SOLTU)
Protein
S-adenosylmethionine decarboxylase proenzyme
Gene
SAMDC
Organism
Solanum tuberosum (Potato)
Status
Functioni
Catalytic activityi
- EC:4.1.1.50
Cofactori
pyruvateNote: Binds 1 pyruvoyl group covalently per subunit.
: S-adenosylmethioninamine biosynthesis Pathwayi
This protein is involved in step 1 of the subpathway that synthesizes S-adenosylmethioninamine from S-adenosyl-L-methionine.Proteins known to be involved in this subpathway in this organism are:
- S-adenosylmethionine decarboxylase proenzyme (102595539), S-adenosylmethionine decarboxylase proenzyme (SAMDC), S-adenosylmethionine decarboxylase proenzyme, S-adenosylmethionine decarboxylase proenzyme (102606123), S-adenosylmethionine decarboxylase alpha chain (102596192), S-adenosylmethionine decarboxylase proenzyme (102589057)
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 13 | 1 | ||
Active sitei | 16 | 1 | ||
Active sitei | 73 | Schiff-base intermediate with substrate; via pyruvic acidBy similarity | 1 | |
Active sitei | 87 | Proton donor; for catalytic activityBy similarity | 1 | |
Active sitei | 236 | Proton acceptor; for processing activityBy similarity | 1 | |
Active sitei | 249 | Proton acceptor; for processing activityBy similarity | 1 |
GO - Molecular functioni
- adenosylmethionine decarboxylase activity Source: GO_Central
GO - Biological processi
- S-adenosylmethioninamine biosynthetic process Source: UniProtKB-UniPathway
- spermidine biosynthetic process Source: GO_Central
- spermine biosynthetic process Source: GO_Central
Keywordsi
Molecular function | Decarboxylase, Lyase |
Biological process | Polyamine biosynthesis, Spermidine biosynthesis |
Ligand | Pyruvate, S-adenosyl-L-methionine, Schiff base |
Enzyme and pathway databases
BRENDAi | 4.1.1.50, 5757 |
UniPathwayi | UPA00331;UER00451 |
Names & Taxonomyi
Protein namesi | Recommended name: S-adenosylmethionine decarboxylase proenzyme (EC:4.1.1.50)Short name: AdoMetDC Short name: SAMDC Alternative name(s): Induced stolen tip protein TUB13 Cleaved into the following 2 chains: |
Gene namesi | Name:SAMDC Synonyms:TUB13 |
Organismi | Solanum tuberosum (Potato) |
Taxonomic identifieri | 4113 [NCBI] |
Taxonomic lineagei | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliopsida › eudicotyledons › Gunneridae › Pentapetalae › asterids › lamiids › Solanales › Solanaceae › Solanoideae › Solaneae › Solanum |
Proteomesi |
|
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000030023 | 1 – 72 | S-adenosylmethionine decarboxylase beta chainAdd BLAST | 72 | |
ChainiPRO_0000030024 | 73 – 360 | S-adenosylmethionine decarboxylase alpha chainAdd BLAST | 288 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 73 | Pyruvic acid (Ser); by autocatalysis1 Publication | 1 |
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).By similarity
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 72 – 73 | Cleavage (non-hydrolytic); by autolysis | 2 |
Keywords - PTMi
Autocatalytic cleavage, ZymogenExpressioni
Tissue specificityi
Stolon, also expressed in leaves, stems and roots.1 Publication
Developmental stagei
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.1 Publication
Gene expression databases
ExpressionAtlasi | Q04694, baseline and differential |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | Q04694 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q04694 |
Family & Domainsi
Sequence similaritiesi
Belongs to the eukaryotic AdoMetDC family.Curated
Phylogenomic databases
eggNOGi | KOG0788, Eukaryota |
InParanoidi | Q04694 |
Family and domain databases
InterProi | View protein in InterPro IPR001985, S-AdoMet_decarboxylase IPR016067, S-AdoMet_deCO2ase_core IPR018166, S-AdoMet_deCO2ase_CS |
PANTHERi | PTHR11570, PTHR11570, 1 hit |
Pfami | View protein in Pfam PF01536, SAM_decarbox, 1 hit |
PIRSFi | PIRSF001355, S-AdenosylMet_decarboxylase, 1 hit |
SUPFAMi | SSF56276, SSF56276, 1 hit |
TIGRFAMsi | TIGR00535, SAM_DCase, 1 hit |
PROSITEi | View protein in PROSITE PS01336, ADOMETDC, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
Q04694-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MEMDLPVSAI GFEGFEKRLE ISFVEPGLFA DPNGKGLRSL SKAQLDEILG
60 70 80 90 100
PAECTIVDNL SNDYVDSYVL SESSLFVYSY KIIIKTCGTT KLLLAIPPIL
110 120 130 140 150
RLAETLSLKV QDVRYTRGSF IFPGAQSFPH RHFSEEVAVL DGYFGKLAAG
160 170 180 190 200
SKAVIMGSPD KTQKWHVYSA SAGSVQSNDP VYTLEMCMTG LDREKASVFY
210 220 230 240 250
KTEESSAAHM TVRSGIRKIL PKSEICDFEF EPCGYSMNSI EGAAVSTIHI
260 270 280 290 300
TPEDGFTYAS FESVGYNPKT MELGPLVERV LACFEPAEFS VALHADVATK
310 320 330 340 350
LLERICSVDV KGYSLAEWSP EEFGEGGSIV YQKFTRTPYC ESPKSVLKGC
360
WKEEEKEGKE
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 174 | S → P in AAB32507 (PubMed:7948879).Curated | 1 | |
Sequence conflicti | 257 | T → S in AAB32507 (PubMed:7948879).Curated | 1 | |
Sequence conflicti | 291 | V → I in AAB32507 (PubMed:7948879).Curated | 1 | |
Sequence conflicti | 305 | I → T in AAB32507 (PubMed:7948879).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | Z11680 mRNA Translation: CAA77742.1 S74514 Genomic DNA Translation: AAB32507.1 |
PIRi | S52662 |
RefSeqi | NP_001306788.1, NM_001319859.1 |
Genome annotation databases
GeneIDi | 102601725 |
KEGGi | sot:102601725 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | Z11680 mRNA Translation: CAA77742.1 S74514 Genomic DNA Translation: AAB32507.1 |
PIRi | S52662 |
RefSeqi | NP_001306788.1, NM_001319859.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1MHM | X-ray | 2.30 | A | 73-360 | [»] | |
B | 1-72 | [»] | ||||
SMRi | Q04694 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 4113.PGSC0003DMT400019451 |
Genome annotation databases
GeneIDi | 102601725 |
KEGGi | sot:102601725 |
Phylogenomic databases
eggNOGi | KOG0788, Eukaryota |
InParanoidi | Q04694 |
Enzyme and pathway databases
UniPathwayi | UPA00331;UER00451 |
BRENDAi | 4.1.1.50, 5757 |
Miscellaneous databases
EvolutionaryTracei | Q04694 |
Gene expression databases
ExpressionAtlasi | Q04694, baseline and differential |
Family and domain databases
InterProi | View protein in InterPro IPR001985, S-AdoMet_decarboxylase IPR016067, S-AdoMet_deCO2ase_core IPR018166, S-AdoMet_deCO2ase_CS |
PANTHERi | PTHR11570, PTHR11570, 1 hit |
Pfami | View protein in Pfam PF01536, SAM_decarbox, 1 hit |
PIRSFi | PIRSF001355, S-AdenosylMet_decarboxylase, 1 hit |
SUPFAMi | SSF56276, SSF56276, 1 hit |
TIGRFAMsi | TIGR00535, SAM_DCase, 1 hit |
PROSITEi | View protein in PROSITE PS01336, ADOMETDC, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | DCAM_SOLTU | |
Accessioni | Q04694Primary (citable) accession number: Q04694 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 1, 1993 |
Last sequence update: | October 1, 1993 | |
Last modified: | April 7, 2021 | |
This is version 119 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Plant Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- 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