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UniProtKB - P17708 (DCAM_RAT)
Protein
S-adenosylmethionine decarboxylase proenzyme
Gene
Amd1
Organism
Rattus norvegicus (Rat)
Status
Functioni
Essential for biosynthesis of the polyamines spermidine and spermine. Promotes maintenance and self-renewal of embryonic stem cells, by maintaining spermine levels.
By similarityCatalytic activityi
- EC:4.1.1.50By similarity
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. This subpathway is part of the pathway S-adenosylmethioninamine biosynthesis, which is itself part of Amine and polyamine biosynthesis.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 |
---|---|---|---|---|
Binding sitei | 7 | SubstrateBy similarity | 1 | |
Active sitei | 8 | By similarity | 1 | |
Active sitei | 11 | By similarity | 1 | |
Binding sitei | 67 | SubstrateBy similarity | 1 | |
Active sitei | 68 | Schiff-base intermediate with substrate; via pyruvic acidBy similarity | 1 | |
Active sitei | 82 | Proton donor; for catalytic activityBy similarity | 1 | |
Binding sitei | 223 | SubstrateBy similarity | 1 | |
Active sitei | 229 | Proton acceptor; for processing activityBy similarity | 1 | |
Active sitei | 243 | Proton acceptor; for processing activityBy similarity | 1 | |
Binding sitei | 247 | SubstrateBy similarity | 1 |
GO - Molecular functioni
- adenosylmethionine decarboxylase activity Source: RGD
- identical protein binding Source: RGD
- putrescine binding Source: RGD
GO - Biological processi
- in utero embryonic development Source: RGD
- polyamine metabolic process Source: RGD
- S-adenosylmethioninamine biosynthetic process Source: UniProtKB-UniPathway
- S-adenosylmethionine metabolic process Source: RGD
- spermidine biosynthetic process Source: RGD
- spermine biosynthetic process Source: RGD
Keywordsi
Molecular function | Decarboxylase, Lyase |
Biological process | Polyamine biosynthesis, Spermidine biosynthesis |
Ligand | Pyruvate, S-adenosyl-L-methionine, Schiff base |
Enzyme and pathway databases
Reactomei | R-RNO-351202, Metabolism of polyamines |
UniPathwayi | UPA00331;UER00451 |
Names & Taxonomyi
Protein namesi | Recommended name: S-adenosylmethionine decarboxylase proenzyme (EC:4.1.1.50By similarity)Short name: AdoMetDC Short name: SAMDC Cleaved into the following 2 chains: |
Gene namesi | Name:Amd1 |
Organismi | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 2104, Amd1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000029969 | 1 – 67 | S-adenosylmethionine decarboxylase beta chainAdd BLAST | 67 | |
ChainiPRO_0000029970 | 68 – 333 | S-adenosylmethionine decarboxylase alpha chainAdd BLAST | 266 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 68 | Pyruvic acid (Ser); by autocatalysisBy similarity | 1 | |
Modified residuei | 298 | PhosphoserineBy 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 similarity1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 67 – 68 | Cleavage (non-hydrolytic); by autolysisBy similarity | 2 |
Keywords - PTMi
Autocatalytic cleavage, Phosphoprotein, ZymogenProteomic databases
PaxDbi | P17708 |
PTM databases
iPTMneti | P17708 |
PhosphoSitePlusi | P17708 |
Expressioni
Gene expression databases
Bgeei | ENSRNOG00000000585, Expressed in brain and 21 other tissues |
Genevisiblei | P17708, RN |
Interactioni
Subunit structurei
Heterotetramer of two alpha and two beta chains.
By similarityGO - Molecular functioni
- identical protein binding Source: RGD
Protein-protein interaction databases
STRINGi | 10116.ENSRNOP00000000715 |
Chemistry databases
BindingDBi | P17708 |
Family & Domainsi
Sequence similaritiesi
Belongs to the eukaryotic AdoMetDC family.Curated
Phylogenomic databases
eggNOGi | KOG0788, Eukaryota |
GeneTreei | ENSGT00390000011776 |
HOGENOMi | CLU_023050_1_0_1 |
InParanoidi | P17708 |
OMAi | LEIWFEE |
OrthoDBi | 932490at2759 |
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
P17708-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MEAAHFFEGT EKLLEVWFSR QQSDASQGSG DLRTIPRSEW DVLLKDVQCS
60 70 80 90 100
IISVTKTDKQ EAYVLSESSM FVSKRRFILK TCGTTLLLKA LVPLLKLARD
110 120 130 140 150
YSGFDSIQSF FYSRKNFMKP SHQGYPHRNF QEEIEFLNAI FPNGAAYCMG
160 170 180 190 200
RMNSDCWYLY TLDLPESRVI NQPDQTLEIL MSELDPAVMD QFYMKDGVTA
210 220 230 240 250
KDVTRESGIR DLIPGSVIDA TLFNPCGYSM NGMKSDGTYW TIHITPEPEF
260 270 280 290 300
SYVSFETNLS QTSYDDLIRK VVEVFKPGKF VTTLFVNQSS KCRTVLSSPQ
310 320 330
KIDGFKRLDC QSAMFNDYNF VFTSFAKKQQ QQS
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 5 | H → P (PubMed:2460457).Curated | 1 | |
Sequence conflicti | 146 | A → G in AAA40683 (PubMed:2323572).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M34464 mRNA Translation: AAA40683.1 M64274 Genomic DNA Translation: AAA42105.1 Z15109, Z15122, Z15123 Genomic DNA Translation: CAA78814.1 BC061532 mRNA Translation: AAH61532.1 |
PIRi | JQ0439, DCRTDM |
RefSeqi | NP_112273.3, NM_031011.3 |
Genome annotation databases
Ensembli | ENSRNOT00000000715; ENSRNOP00000000715; ENSRNOG00000000585 |
GeneIDi | 81640 |
KEGGi | rno:81640 |
UCSCi | RGD:2104, rat |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M34464 mRNA Translation: AAA40683.1 M64274 Genomic DNA Translation: AAA42105.1 Z15109, Z15122, Z15123 Genomic DNA Translation: CAA78814.1 BC061532 mRNA Translation: AAH61532.1 |
PIRi | JQ0439, DCRTDM |
RefSeqi | NP_112273.3, NM_031011.3 |
3D structure databases
SMRi | P17708 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 10116.ENSRNOP00000000715 |
Chemistry databases
BindingDBi | P17708 |
ChEMBLi | CHEMBL3808 |
DrugCentrali | P17708 |
PTM databases
iPTMneti | P17708 |
PhosphoSitePlusi | P17708 |
Proteomic databases
PaxDbi | P17708 |
Genome annotation databases
Ensembli | ENSRNOT00000000715; ENSRNOP00000000715; ENSRNOG00000000585 |
GeneIDi | 81640 |
KEGGi | rno:81640 |
UCSCi | RGD:2104, rat |
Organism-specific databases
CTDi | 262 |
RGDi | 2104, Amd1 |
Phylogenomic databases
eggNOGi | KOG0788, Eukaryota |
GeneTreei | ENSGT00390000011776 |
HOGENOMi | CLU_023050_1_0_1 |
InParanoidi | P17708 |
OMAi | LEIWFEE |
OrthoDBi | 932490at2759 |
Enzyme and pathway databases
UniPathwayi | UPA00331;UER00451 |
Reactomei | R-RNO-351202, Metabolism of polyamines |
Miscellaneous databases
PROi | PR:P17708 |
Gene expression databases
Bgeei | ENSRNOG00000000585, Expressed in brain and 21 other tissues |
Genevisiblei | P17708, RN |
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 |
MobiDBi | Search... |
Entry informationi
Entry namei | DCAM_RAT | |
Accessioni | P17708Primary (citable) accession number: P17708 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | August 1, 1990 |
Last sequence update: | July 1, 1993 | |
Last modified: | February 23, 2022 | |
This is version 159 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families