Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

S-adenosylmethionine decarboxylase proenzyme

Gene

Amd1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Essential for biosynthesis of the polyamines spermidine and spermine. Promotes maintenance and self-renewal of embryonic stem cells, by maintaining spermine levels.By similarity

Catalytic activityi

S-adenosyl-L-methionine = S-adenosyl 3-(methylthio)propylamine + CO2.By similarity

Cofactori

pyruvateNote: Binds 1 pyruvoyl group covalently per subunit.

Pathwayi: S-adenosylmethioninamine biosynthesis

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:
  1. S-adenosylmethionine decarboxylase proenzyme (Amd1)
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 keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei7SubstrateBy similarity1
Active sitei8By similarity1
Active sitei11By similarity1
Binding sitei67SubstrateBy similarity1
Active sitei68Schiff-base intermediate with substrate; via pyruvic acidBy similarity1
Active sitei82Proton donor; for catalytic activityBy similarity1
Binding sitei223SubstrateBy similarity1
Active sitei229Proton acceptor; for processing activityBy similarity1
Active sitei243Proton acceptor; for processing activityBy similarity1
Binding sitei247SubstrateBy similarity1

GO - Molecular functioni

  • adenosylmethionine decarboxylase activity Source: RGD
  • putrescine binding Source: RGD

GO - Biological processi

  • 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 functionDecarboxylase, Lyase
Biological processPolyamine biosynthesis, Spermidine biosynthesis
LigandPyruvate, S-adenosyl-L-methionine, Schiff base

Enzyme and pathway databases

ReactomeiR-RNO-351202. Metabolism of polyamines.
UniPathwayiUPA00331; 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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 20

Organism-specific databases

RGDi2104. Amd1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: RGD

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3808.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000299691 – 67S-adenosylmethionine decarboxylase beta chainAdd BLAST67
ChainiPRO_000002997068 – 333S-adenosylmethionine decarboxylase alpha chainAdd BLAST266

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei68Pyruvic acid (Ser); by autocatalysisBy similarity1
Modified residuei298PhosphoserineBy similarity1

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 keyPosition(s)DescriptionActionsGraphical viewLength
Sitei67 – 68Cleavage (non-hydrolytic); by autolysisBy similarity2

Keywords - PTMi

Autocatalytic cleavage, Phosphoprotein, Zymogen

Proteomic databases

PaxDbiP17708.
PRIDEiP17708.

PTM databases

iPTMnetiP17708.
PhosphoSitePlusiP17708.

Expressioni

Gene expression databases

BgeeiENSRNOG00000000585.
GenevisibleiP17708. RN.

Interactioni

Subunit structurei

Heterotetramer of two alpha and two beta chains.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000000715.

Chemistry databases

BindingDBiP17708.

Structurei

3D structure databases

ProteinModelPortaliP17708.
SMRiP17708.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the eukaryotic AdoMetDC family.Curated

Phylogenomic databases

eggNOGiKOG0788. Eukaryota.
ENOG410XRN0. LUCA.
GeneTreeiENSGT00390000011776.
HOGENOMiHOG000159915.
HOVERGENiHBG000761.
InParanoidiP17708.
KOiK01611.
OMAiGDHWYLY.
OrthoDBiEOG091G1467.

Family and domain databases

Gene3Di3.60.90.10. 1 hit.
InterProiView protein in InterPro
IPR001985. S-AdoMet_decarboxylase.
IPR016067. S-AdoMet_deCO2ase_core.
IPR018166. S-AdoMet_deCO2ase_CS.
PfamiView protein in Pfam
PF01536. SAM_decarbox. 1 hit.
PIRSFiPIRSF001355. S-AdenosylMet_decarboxylase. 1 hit.
SUPFAMiSSF56276. SSF56276. 1 hit.
TIGRFAMsiTIGR00535. SAM_DCase. 1 hit.
PROSITEiView protein in PROSITE
PS01336. ADOMETDC. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P17708-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:333
Mass (Da):38,137
Last modified:July 1, 1993 - v3
Checksum:i9323E2D38BD8FEF1
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti5H → P (PubMed:2460457).Curated1
Sequence conflicti146A → G in AAA40683 (PubMed:2323572).Curated1

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.
PIRiJQ0439. DCRTDM.
RefSeqiNP_112273.3. NM_031011.3.
UniGeneiRn.56270.

Genome annotation databases

EnsembliENSRNOT00000000715; ENSRNOP00000000715; ENSRNOG00000000585.
GeneIDi81640.
KEGGirno:81640.
UCSCiRGD:2104. rat.

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.
PIRiJQ0439. DCRTDM.
RefSeqiNP_112273.3. NM_031011.3.
UniGeneiRn.56270.

3D structure databases

ProteinModelPortaliP17708.
SMRiP17708.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000000715.

Chemistry databases

BindingDBiP17708.
ChEMBLiCHEMBL3808.

PTM databases

iPTMnetiP17708.
PhosphoSitePlusiP17708.

Proteomic databases

PaxDbiP17708.
PRIDEiP17708.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000000715; ENSRNOP00000000715; ENSRNOG00000000585.
GeneIDi81640.
KEGGirno:81640.
UCSCiRGD:2104. rat.

Organism-specific databases

CTDi262.
RGDi2104. Amd1.

Phylogenomic databases

eggNOGiKOG0788. Eukaryota.
ENOG410XRN0. LUCA.
GeneTreeiENSGT00390000011776.
HOGENOMiHOG000159915.
HOVERGENiHBG000761.
InParanoidiP17708.
KOiK01611.
OMAiGDHWYLY.
OrthoDBiEOG091G1467.

Enzyme and pathway databases

UniPathwayiUPA00331; UER00451.
ReactomeiR-RNO-351202. Metabolism of polyamines.

Miscellaneous databases

PROiPR:P17708.

Gene expression databases

BgeeiENSRNOG00000000585.
GenevisibleiP17708. RN.

Family and domain databases

Gene3Di3.60.90.10. 1 hit.
InterProiView protein in InterPro
IPR001985. S-AdoMet_decarboxylase.
IPR016067. S-AdoMet_deCO2ase_core.
IPR018166. S-AdoMet_deCO2ase_CS.
PfamiView protein in Pfam
PF01536. SAM_decarbox. 1 hit.
PIRSFiPIRSF001355. S-AdenosylMet_decarboxylase. 1 hit.
SUPFAMiSSF56276. SSF56276. 1 hit.
TIGRFAMsiTIGR00535. SAM_DCase. 1 hit.
PROSITEiView protein in PROSITE
PS01336. ADOMETDC. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiDCAM_RAT
AccessioniPrimary (citable) accession number: P17708
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: July 1, 1993
Last modified: June 7, 2017
This is version 143 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.