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Protein

S-adenosylmethionine decarboxylase proenzyme 1

Gene

Amd1

Organism
Mus musculus (Mouse)
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.1 Publication

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 1 (Amd1), S-adenosylmethionine decarboxylase proenzyme 2 (Amd2)
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: MGI
  • putrescine binding Source: GO_Central

GO - Biological processi

  • in utero embryonic development Source: MGI
  • S-adenosylmethioninamine biosynthetic process Source: UniProtKB-UniPathway
  • spermidine biosynthetic process Source: MGI
  • spermine biosynthetic process Source: MGI

Keywordsi

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

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
S-adenosylmethionine decarboxylase proenzyme 1 (EC:4.1.1.50By similarity)
Short name:
AdoMetDC 1
Short name:
SAMDC 1
Cleaved into the following 2 chains:
Gene namesi
Name:Amd1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:88004. Amd1.

Subcellular locationi

GO - Cellular componenti

Pathology & Biotechi

Disruption phenotypei

Embryonic lethal with developmental arrest between E3.5 and E6.5. Arrest of blastocysts cultured in vitro is rescued by the addition of spermidine.1 Publication

Chemistry databases

ChEMBLiCHEMBL3584.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000299631 – 67S-adenosylmethionine decarboxylase 1 beta chainAdd BLAST67
ChainiPRO_000002996468 – 334S-adenosylmethionine decarboxylase 1 alpha chainAdd BLAST267

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 similarity

Sites

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

Keywords - PTMi

Autocatalytic cleavage, Phosphoprotein, Zymogen

Proteomic databases

PaxDbiP0DMN7.
PRIDEiP0DMN7.

PTM databases

iPTMnetiP0DMN7.
PhosphoSitePlusiP0DMN7.

Expressioni

Tissue specificityi

Expressed in embryonic stem cells; subsequently down-regulated in differentiating neural precursor cells.1 Publication

Gene expression databases

BgeeiENSMUSG00000075232.
CleanExiMM_AMD1.
GenevisibleiP0DMN7. MM.

Interactioni

Subunit structurei

Heterotetramer of two alpha and two beta chains.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Shc1P980837EBI-644529,EBI-300201

Protein-protein interaction databases

IntActiP0DMN7. 2 interactors.
MINTiMINT-1657447.
STRINGi10090.ENSMUSP00000097528.

Structurei

3D structure databases

ProteinModelPortaliP0DMN7.
SMRiP0DMN7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the eukaryotic AdoMetDC family.Curated

Phylogenomic databases

eggNOGiKOG0788. Eukaryota.
ENOG410XRN0. LUCA.
GeneTreeiENSGT00390000011776.
HOGENOMiHOG000159915.
HOVERGENiHBG000761.
KOiK01611.
OMAiGDHWYLY.
OrthoDBiEOG091G1467.
PhylomeDBiP0DMN7.

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.

P0DMN7-1 [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 TLDFPESRVI SQPDQTLEIL 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 QQQS
Length:334
Mass (Da):38,272
Last modified:October 1, 2014 - v1
Checksum:i7950A1E9A9ACBD72
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z14986 mRNA. Translation: CAA78710.1.
D12780 mRNA. Translation: BAA02243.1.
AB025024 Genomic DNA. Translation: BAA83784.1.
AK146840 mRNA. Translation: BAE27473.1.
AK166187 mRNA. Translation: BAE38617.1.
AK168165 mRNA. Translation: BAE40126.1.
CT010192 mRNA. Translation: CAJ18400.1.
CH466540 Genomic DNA. Translation: EDL04951.1.
BC011110 mRNA. Translation: AAH11110.1.
BC071220 mRNA. Translation: AAH71220.1.
BC080791 mRNA. Translation: AAH80791.1.
BC092072 mRNA. Translation: AAH92072.1.
BC138696 mRNA. Translation: AAI38697.1.
BC138697 mRNA. Translation: AAI38698.1.
CCDSiCCDS48544.1.
RefSeqiNP_033795.1. NM_009665.5.
UniGeneiMm.253533.
Mm.476925.

Genome annotation databases

EnsembliENSMUST00000099945; ENSMUSP00000097528; ENSMUSG00000075232.
GeneIDi11702.
KEGGimmu:11702.

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.

Entry informationi

Entry nameiDCAM1_MOUSE
AccessioniPrimary (citable) accession number: P0DMN7
Secondary accession number(s): P31154, P82184, Q58E47
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 2014
Last sequence update: October 1, 2014
Last modified: June 7, 2017
This is version 23 of the entry and version 1 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families