UniProtKB - Q38IY3 (DCAM_SOLCI)
Protein
S-adenosylmethionine decarboxylase proenzyme
Gene
SAMDC
Organism
Solanum chilense (Tomato) (Lycopersicon chilense)
Status
Functioni
Catalytic activityi
- EC:4.1.1.50
Cofactori
pyruvateBy similarityNote: Binds 1 pyruvoyl group covalently per subunit.By similarity
: 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 (EJD97_001170), S-adenosylmethionine decarboxylase alpha chain (EJD97_010873), S-adenosylmethionine decarboxylase alpha chain, S-adenosylmethionine decarboxylase proenzyme (SAMDC), S-adenosylmethionine decarboxylase alpha chain (CT093), S-adenosylmethionine decarboxylase alpha chain (CT093), S-adenosylmethionine decarboxylase proenzyme (EJD97_005020), S-adenosylmethionine decarboxylase alpha chain (CT093), S-adenosylmethionine decarboxylase proenzyme (EJD97_025563), S-adenosylmethionine decarboxylase alpha chain (CT093), S-adenosylmethionine decarboxylase alpha chain (CT093), S-adenosylmethionine decarboxylase alpha chain (CT093), S-adenosylmethionine decarboxylase alpha chain (CT093), S-adenosylmethionine decarboxylase alpha chain (CT093), S-adenosylmethionine decarboxylase alpha chain (CT093), S-adenosylmethionine decarboxylase alpha chain (CT093), S-adenosylmethionine decarboxylase proenzyme (EJD97_011601), S-adenosylmethionine decarboxylase alpha chain (CT093)
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 | 11 | By similarity | 1 | |
Active sitei | 14 | By similarity | 1 | |
Active sitei | 71 | Schiff-base intermediate with substrate; via pyruvic acidBy similarity | 1 | |
Active sitei | 85 | Proton donor; for catalytic activityBy similarity | 1 | |
Active sitei | 234 | Proton acceptor; for processing activityBy similarity | 1 | |
Active sitei | 247 | Proton acceptor; for processing activityBy similarity | 1 |
GO - Molecular functioni
- adenosylmethionine decarboxylase activity Source: UniProtKB-EC
GO - Biological processi
- S-adenosylmethioninamine biosynthetic process Source: UniProtKB-UniPathway
- spermidine biosynthetic process Source: UniProtKB-KW
- spermine biosynthetic process Source: InterPro
Keywordsi
Molecular function | Decarboxylase, Lyase |
Biological process | Polyamine biosynthesis, Spermidine biosynthesis |
Ligand | Pyruvate, S-adenosyl-L-methionine, Schiff base |
Enzyme and pathway databases
UniPathwayi | UPA00331;UER00451 |
Names & Taxonomyi
Protein namesi | Recommended name: S-adenosylmethionine decarboxylase proenzyme (EC:4.1.1.50)Short name: AdoMetDC Short name: SAMDC Cleaved into the following 2 chains: |
Gene namesi | Name:SAMDC |
Organismi | Solanum chilense (Tomato) (Lycopersicon chilense) |
Taxonomic identifieri | 4083 [NCBI] |
Taxonomic lineagei | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliopsida › eudicotyledons › Gunneridae › Pentapetalae › asterids › lamiids › Solanales › Solanaceae › Solanoideae › Solaneae › Solanum › Solanum subgen. Lycopersicon |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000252660 | 1 – 70 | S-adenosylmethionine decarboxylase beta chainBy similarityAdd BLAST | 70 | |
ChainiPRO_0000252661 | 71 – 358 | S-adenosylmethionine decarboxylase alpha chainBy similarityAdd BLAST | 288 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 71 | Pyruvic acid (Ser); by autocatalysisBy similarity | 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 | 70 – 71 | Cleavage (non-hydrolytic); by autolysisBy similarity | 2 |
Keywords - PTMi
Autocatalytic cleavage, ZymogenFamily & Domainsi
Sequence similaritiesi
Belongs to the eukaryotic AdoMetDC family.Curated
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
Q38IY3-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MDLPVSAIGF EGFEKRLEIS FVEPGLFADP NGKGLRSLTK AQLDEILGPA
60 70 80 90 100
ECTIVDNLSN DYVDSYVLSE SSLFVYSYKI IIKTCGTTKL LLAIPPILRL
110 120 130 140 150
AETLSLKVQD VRYTRGSFIF PGAQSFPHRH FSEEVAVLDG YFGKLAAGSK
160 170 180 190 200
AVIMGNPDKT QKWHVYSASA GTVQCNDPVY TLEMCMAGLD REKASVFYKT
210 220 230 240 250
EESSAAHMTV RSGIRKILPK FEICDFEFEP CGYSMNSIEG AAVSTIHITP
260 270 280 290 300
EDGFSYASFE SVGYDPKTTE LGPLVERVLA CFEPAEFSIA LHADVATKLL
310 320 330 340 350
ERVCSVDVKG YSLAEWSPEE FGKGGSIVYQ KFTRTPYCES PKSVLKGCWK
EEEKEEKE
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | DQ224276 mRNA Translation: ABB02530.1 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | DQ224276 mRNA Translation: ABB02530.1 |
3D structure databases
SMRi | Q38IY3 |
ModBasei | Search... |
Enzyme and pathway databases
UniPathwayi | UPA00331;UER00451 |
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_SOLCI | |
Accessioni | Q38IY3Primary (citable) accession number: Q38IY3 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 17, 2006 |
Last sequence update: | November 22, 2005 | |
Last modified: | August 12, 2020 | |
This is version 52 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
Documents
- PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families