UniProtKB - Q96286 (DCAM1_ARATH)
Protein
S-adenosylmethionine decarboxylase proenzyme 1
Gene
SAMDC1
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Functioni
Essential for biosynthesis of the polyamines spermidine and spermine. Essential for polyamine homeostasis, and normal plant embryogenesis, growth and development.1 Publication
Catalytic activityi
- EC:4.1.1.501 Publication
Cofactori
pyruvateBy similarityNote: Binds 1 pyruvoyl group covalently per subunit.By similarity
Kineticsi
- KM=23.1 µM for S-adenosyl-L-methionine1 Publication
pH dependencei
Optimum pH is 6.8-7.2.1 Publication
: S-adenosylmethioninamine biosynthesis Pathwayi
This protein is involved in step 1 of the subpathway that synthesizes S-adenosylmethioninamine from S-adenosyl-L-methionine.CuratedProteins known to be involved in this subpathway in this organism are:
- S-adenosylmethionine decarboxylase proenzyme 4 (SAMDC4), Uncharacterized protein (At3g17717), (thale cress) hypothetical protein (AT9943_LOCUS11324), S-adenosylmethionine decarboxylase proenzyme (AXX17_At5g18760), S-adenosylmethionine decarboxylase proenzyme (AN1_LOCUS14019), S-adenosylmethionine decarboxylase proenzyme (At3g17717), S-adenosylmethionine decarboxylase proenzyme (AT9943_LOCUS12031), S-adenosylmethionine decarboxylase proenzyme (AXX17_At3g27520), S-adenosylmethionine decarboxylase proenzyme 3 (SAMDC3), S-adenosylmethionine decarboxylase proenzyme (AXX17_At5g15520), S-adenosylmethionine decarboxylase proenzyme 2 (SAMDC2), Uncharacterized protein (AN1_LOCUS13172), S-adenosylmethionine decarboxylase proenzyme 1 (SAMDC1), S-adenosylmethionine decarboxylase proenzyme (AT9943_LOCUS19261), Uncharacterized protein, S-adenosylmethionine decarboxylase proenzyme (AXX17_At3g01690), S-adenosylmethionine decarboxylase proenzyme, S-adenosylmethionine decarboxylase proenzyme (C24_LOCUS22263)
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 | 9 | By similarity | 1 | |
Active sitei | 12 | By similarity | 1 | |
Binding sitei | 68 | SubstrateBy similarity | 1 | |
Active sitei | 69 | Schiff-base intermediate with substrate; via pyruvic acidBy similarity | 1 | |
Active sitei | 83 | Proton donor; for catalytic activityBy similarity | 1 | |
Active sitei | 233 | Proton acceptor; for processing activityBy similarity | 1 | |
Active sitei | 246 | Proton acceptor; for processing activityBy similarity | 1 | |
Binding sitei | 250 | SubstrateBy similarity | 1 |
GO - Molecular functioni
- adenosylmethionine decarboxylase activity Source: TAIR
GO - Biological processi
- gene silencing Source: TAIR
- plant organ development Source: UniProtKB
- polyamine biosynthetic process Source: TAIR
- S-adenosylmethioninamine biosynthetic process Source: UniProtKB-UniPathway
- spermidine biosynthetic process Source: UniProtKB
- spermine biosynthetic process Source: UniProtKB
- viral genome replication Source: TAIR
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, 399 |
SABIO-RKi | Q96286 |
UniPathwayi | UPA00331;UER00451 |
Names & Taxonomyi
Protein namesi | Recommended name: S-adenosylmethionine decarboxylase proenzyme 1Curated (EC:4.1.1.501 Publication)Short name: AdoMetDC11 Publication Cleaved into the following 2 chains: S-adenosylmethionine decarboxylase 1 alpha chainBy similarity S-adenosylmethionine decarboxylase 1 beta chainBy similarity |
Gene namesi | Name:SAMDC11 Publication Synonyms:SAMDC1 Publication Ordered Locus Names:At3g02470 ORF Names:F16B3.10 |
Organismi | Arabidopsis thaliana (Mouse-ear cress) |
Taxonomic identifieri | 3702 [NCBI] |
Taxonomic lineagei | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliopsida › eudicotyledons › Gunneridae › Pentapetalae › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis |
Proteomesi |
|
Organism-specific databases
Araporti | AT3G02470 |
TAIRi | locus:2076834, AT3G02470 |
Pathology & Biotechi
Disruption phenotypei
Reduction in the length of stem internodes. Increased thickness of veins in leaves and inflorescence stems. Altered morphology of xylem vessel elements. The double mutants of bud2-1 and samdc1-1 are embryonic lethal.1 Publication
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 50 | C → A: Slightly reduces activity. 1 Publication | 1 | |
Mutagenesisi | 81 | K → A: Reduces activity 2-fold. Increases substrate specificity for lysine 6-fold. 1 Publication | 1 | |
Mutagenesisi | 83 | C → A: Reduces activity 10-fold. 1 Publication | 1 | |
Mutagenesisi | 230 | C → A: Slightly reduces activity. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000029987 | 1 – 68 | S-adenosylmethionine decarboxylase 1 beta chainBy similarityAdd BLAST | 68 | |
ChainiPRO_0000029988 | 69 – 366 | S-adenosylmethionine decarboxylase 1 alpha chainBy similarityAdd BLAST | 298 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 69 | 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
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 68 – 69 | Cleavage (non-hydrolytic); by autolysisBy similarity | 2 |
Keywords - PTMi
Autocatalytic cleavage, ZymogenProteomic databases
PaxDbi | Q96286 |
PRIDEi | Q96286 |
ProteomicsDBi | 224680 |
Expressioni
Inductioni
Down-regulated by auxin.1 Publication
Gene expression databases
ExpressionAtlasi | Q96286, baseline and differential |
Genevisiblei | Q96286, AT |
Interactioni
Protein-protein interaction databases
BioGRIDi | 6547, 2 interactors |
IntActi | Q96286, 1 interactor |
STRINGi | 3702.AT3G02470.1 |
Family & Domainsi
Sequence similaritiesi
Belongs to the eukaryotic AdoMetDC family.Curated
Phylogenomic databases
eggNOGi | KOG0788, Eukaryota |
HOGENOMi | CLU_023050_2_1_1 |
InParanoidi | Q96286 |
OMAi | FKNSANG |
OrthoDBi | 932490at2759 |
PhylomeDBi | Q96286 |
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
Q96286-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MALSAIGFEG YEKRLEVTFF EPSIFQDSKG LGLRALTKSQ LDEILTPAAC
60 70 80 90 100
TIVSSLSNDQ LDSYVLSESS FFVYPYKVII KTCGTTKLLL SIPPLLKLAG
110 120 130 140 150
ELSLSVKSVK YTRGSFLCPG GQPFPHRSFS EEVSVLDGHF TQLGLNSVAY
160 170 180 190 200
LMGNDDETKK WHVYAASAQD SSNCNNNVYT LEMCMTGLDR EKAAVFYKDE
210 220 230 240 250
ADKTGSMTDN SGIRKILPKS EICDFEFEPC GYSMNSIEGD AISTIHVTPE
260 270 280 290 300
DGFSYASFEA VGYDFNTLDL SQLVTRVLSC FEPKQFSVAV HSSVGANSYK
310 320 330 340 350
PEITVDLEDY GCRERTFESL GEESGTVMYQ TFEKLGKYCG SPRSTLKCEW
360
SSNNSCSSED EKDEGI
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 123 | P → L in CAA69073 (PubMed:11139406).Curated | 1 | |
Sequence conflicti | 150 | Y → T in AAB17665 (Ref. 2) Curated | 1 | |
Sequence conflicti | 216 | I → N in AAB17665 (Ref. 2) Curated | 1 | |
Sequence conflicti | 245 | I → N in AAB17665 (Ref. 2) Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | Y07765 Genomic DNA Translation: CAA69073.1 U63633 mRNA Translation: AAB17665.1 AC021640 Genomic DNA Translation: AAF32454.1 CP002686 Genomic DNA Translation: AEE73812.1 CP002686 Genomic DNA Translation: AEE73813.1 CP002686 Genomic DNA Translation: AEE73814.1 AF428468 mRNA Translation: AAL16237.1 AY042824 mRNA Translation: AAK68764.1 AY081446 mRNA Translation: AAM10008.1 AK316891 mRNA Translation: BAH19598.1 |
RefSeqi | NP_001078093.1, NM_001084624.1 NP_001154585.1, NM_001161113.1 NP_186896.1, NM_111114.2 |
Genome annotation databases
EnsemblPlantsi | AT3G02470.1; AT3G02470.1; AT3G02470 AT3G02470.3; AT3G02470.3; AT3G02470 AT3G02470.4; AT3G02470.4; AT3G02470 |
GeneIDi | 821214 |
Gramenei | AT3G02470.1; AT3G02470.1; AT3G02470 AT3G02470.3; AT3G02470.3; AT3G02470 AT3G02470.4; AT3G02470.4; AT3G02470 |
KEGGi | ath:AT3G02470 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | Y07765 Genomic DNA Translation: CAA69073.1 U63633 mRNA Translation: AAB17665.1 AC021640 Genomic DNA Translation: AAF32454.1 CP002686 Genomic DNA Translation: AEE73812.1 CP002686 Genomic DNA Translation: AEE73813.1 CP002686 Genomic DNA Translation: AEE73814.1 AF428468 mRNA Translation: AAL16237.1 AY042824 mRNA Translation: AAK68764.1 AY081446 mRNA Translation: AAM10008.1 AK316891 mRNA Translation: BAH19598.1 |
RefSeqi | NP_001078093.1, NM_001084624.1 NP_001154585.1, NM_001161113.1 NP_186896.1, NM_111114.2 |
3D structure databases
SMRi | Q96286 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 6547, 2 interactors |
IntActi | Q96286, 1 interactor |
STRINGi | 3702.AT3G02470.1 |
Proteomic databases
PaxDbi | Q96286 |
PRIDEi | Q96286 |
ProteomicsDBi | 224680 |
Genome annotation databases
EnsemblPlantsi | AT3G02470.1; AT3G02470.1; AT3G02470 AT3G02470.3; AT3G02470.3; AT3G02470 AT3G02470.4; AT3G02470.4; AT3G02470 |
GeneIDi | 821214 |
Gramenei | AT3G02470.1; AT3G02470.1; AT3G02470 AT3G02470.3; AT3G02470.3; AT3G02470 AT3G02470.4; AT3G02470.4; AT3G02470 |
KEGGi | ath:AT3G02470 |
Organism-specific databases
Araporti | AT3G02470 |
TAIRi | locus:2076834, AT3G02470 |
Phylogenomic databases
eggNOGi | KOG0788, Eukaryota |
HOGENOMi | CLU_023050_2_1_1 |
InParanoidi | Q96286 |
OMAi | FKNSANG |
OrthoDBi | 932490at2759 |
PhylomeDBi | Q96286 |
Enzyme and pathway databases
UniPathwayi | UPA00331;UER00451 |
BRENDAi | 4.1.1.50, 399 |
SABIO-RKi | Q96286 |
Miscellaneous databases
PROi | PR:Q96286 |
Gene expression databases
ExpressionAtlasi | Q96286, baseline and differential |
Genevisiblei | Q96286, AT |
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 | DCAM1_ARATH | |
Accessioni | Q96286Primary (citable) accession number: Q96286 Secondary accession number(s): B9DFT1, Q96531, Q9M893 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | December 15, 1998 |
Last sequence update: | August 14, 2001 | |
Last modified: | December 2, 2020 | |
This is version 154 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Plant Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- Arabidopsis thaliana
Arabidopsis thaliana: entries and gene names - PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families