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Protein

S-adenosylmethionine decarboxylase proenzyme

Gene

SPE2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

S-adenosylmethionine decarboxylase is essential for normal growth, sporulation, maintenance of ds-RNA virus, biosynthesis of spermine and spermidine.

Catalytic activityi

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

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 (SPE2)
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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei29 – 291By similarity
Active sitei32 – 321By similarity
Active sitei88 – 881Schiff-base intermediate with substrate; via pyruvic acidBy similarity
Active sitei102 – 1021Proton donor; for catalytic activityBy similarity
Active sitei287 – 2871Proton acceptor; for processing activityBy similarity
Active sitei301 – 3011Proton acceptor; for processing activityBy similarity

GO - Molecular functioni

  • adenosylmethionine decarboxylase activity Source: SGD

GO - Biological processi

  • pantothenate biosynthetic process Source: SGD
  • S-adenosylmethioninamine biosynthetic process Source: UniProtKB-UniPathway
  • spermidine biosynthetic process Source: SGD
  • spermine biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

Polyamine biosynthesis, Spermidine biosynthesis

Keywords - Ligandi

Pyruvate, S-adenosyl-L-methionine, Schiff base

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER3O-32361.
MetaCyc:MONOMER3O-32362.
YEAST:MONOMER3O-32362.
BRENDAi4.1.1.50. 984.
ReactomeiR-SCE-351202. Metabolism of polyamines.
UniPathwayiUPA00331; 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:SPE2
Ordered Locus Names:YOL052C
ORF Names:O1275
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOL052C.
SGDiS000005412. SPE2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 8787S-adenosylmethionine decarboxylase beta chainPRO_0000030033Add
BLAST
Chaini88 – 396309S-adenosylmethionine decarboxylase alpha chainPRO_0000030034Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei88 – 881Pyruvic acid (Ser); by autocatalysis

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei87 – 882Cleavage (non-hydrolytic); by autolysis

Keywords - PTMi

Autocatalytic cleavage, Zymogen

Proteomic databases

MaxQBiP21182.

Interactioni

Protein-protein interaction databases

BioGridi34352. 84 interactions.
DIPiDIP-361N.
IntActiP21182. 1 interaction.
MINTiMINT-535164.

Structurei

3D structure databases

ProteinModelPortaliP21182.
SMRiP21182. Positions 28-395.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the eukaryotic AdoMetDC family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000011776.
HOGENOMiHOG000159915.
InParanoidiP21182.
KOiK01611.
OMAiFHHDAFA.
OrthoDBiEOG70PC6X.

Family and domain databases

Gene3Di3.60.90.10. 1 hit.
InterProiIPR001985. S-AdoMet_decarboxylase.
IPR018167. S-AdoMet_decarboxylase_subgr.
IPR016067. S-AdoMet_deCO2ase_core.
IPR018166. S-AdoMet_deCO2ase_CS.
[Graphical view]
PANTHERiPTHR11570. PTHR11570. 1 hit.
PfamiPF01536. SAM_decarbox. 1 hit.
[Graphical view]
PIRSFiPIRSF001355. S-AdenosylMet_decarboxylase. 1 hit.
SUPFAMiSSF56276. SSF56276. 1 hit.
TIGRFAMsiTIGR00535. SAM_DCase. 1 hit.
PROSITEiPS01336. ADOMETDC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P21182-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTVTIKELTN HNYIDHELSA TLDSTDAFEG PEKLLEIWFF PHKKSITTEK
60 70 80 90 100
TLRNIGMDRW IEILKLVKCE VLSMKKTKEL DAFLLSESSL FVFDHKLTMK
110 120 130 140 150
TCGTTTTLFC LEKLFQIVEQ ELSWAFRTTQ GGKYKPFKVF YSRRCFLFPC
160 170 180 190 200
KQAAIHQNWA DEVDYLNKFF DNGKSYSVGR NDKSNHWNLY VTETDRSTPK
210 220 230 240 250
GKEYIEDDDE TFEVLMTELD PECASKFVCG PEASTTALVE PNEDKGHNLG
260 270 280 290 300
YQMTKNTRLD EIYVNSAQDS DLSFHHDAFA FTPCGYSSNM ILAEKYYYTL
310 320 330 340 350
HVTPEKGWSY ASFESNIPVF DISQGKQDNL DVLLHILNVF QPREFSMTFF
360 370 380 390
TKNYQNQSFQ KLLSINESLP DYIKLDKIVY DLDDYHLFYM KLQKKI
Length:396
Mass (Da):46,232
Last modified:May 1, 1991 - v1
Checksum:i8B63676CB5636D71
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M38434 Genomic DNA. Translation: AAA34421.1.
X91067 Genomic DNA. Translation: CAA62536.1.
Z74794 Genomic DNA. Translation: CAA99058.1.
BK006948 Genomic DNA. Translation: DAA10732.1.
PIRiS12772. DCBYDM.
RefSeqiNP_014590.1. NM_001183306.1.

Genome annotation databases

EnsemblFungiiYOL052C; YOL052C; YOL052C.
GeneIDi854105.
KEGGisce:YOL052C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M38434 Genomic DNA. Translation: AAA34421.1.
X91067 Genomic DNA. Translation: CAA62536.1.
Z74794 Genomic DNA. Translation: CAA99058.1.
BK006948 Genomic DNA. Translation: DAA10732.1.
PIRiS12772. DCBYDM.
RefSeqiNP_014590.1. NM_001183306.1.

3D structure databases

ProteinModelPortaliP21182.
SMRiP21182. Positions 28-395.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34352. 84 interactions.
DIPiDIP-361N.
IntActiP21182. 1 interaction.
MINTiMINT-535164.

Proteomic databases

MaxQBiP21182.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOL052C; YOL052C; YOL052C.
GeneIDi854105.
KEGGisce:YOL052C.

Organism-specific databases

EuPathDBiFungiDB:YOL052C.
SGDiS000005412. SPE2.

Phylogenomic databases

GeneTreeiENSGT00390000011776.
HOGENOMiHOG000159915.
InParanoidiP21182.
KOiK01611.
OMAiFHHDAFA.
OrthoDBiEOG70PC6X.

Enzyme and pathway databases

UniPathwayiUPA00331; UER00451.
BioCyciMetaCyc:MONOMER3O-32361.
MetaCyc:MONOMER3O-32362.
YEAST:MONOMER3O-32362.
BRENDAi4.1.1.50. 984.
ReactomeiR-SCE-351202. Metabolism of polyamines.

Miscellaneous databases

PROiP21182.

Family and domain databases

Gene3Di3.60.90.10. 1 hit.
InterProiIPR001985. S-AdoMet_decarboxylase.
IPR018167. S-AdoMet_decarboxylase_subgr.
IPR016067. S-AdoMet_deCO2ase_core.
IPR018166. S-AdoMet_deCO2ase_CS.
[Graphical view]
PANTHERiPTHR11570. PTHR11570. 1 hit.
PfamiPF01536. SAM_decarbox. 1 hit.
[Graphical view]
PIRSFiPIRSF001355. S-AdenosylMet_decarboxylase. 1 hit.
SUPFAMiSSF56276. SSF56276. 1 hit.
TIGRFAMsiTIGR00535. SAM_DCase. 1 hit.
PROSITEiPS01336. ADOMETDC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Spermidine biosynthesis in Saccharomyces cerevisiae. Biosynthesis and processing of a proenzyme form of S-adenosylmethionine decarboxylase."
    Kashiwagi K., Taneja S.K., Liu T.-Y., Tabor C.W., Tabor H.
    J. Biol. Chem. 265:22321-22328(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
  2. "Analysis of a 26 kb region on the left arm of yeast chromosome XV."
    Mannhaupt G., Vetter I., Schwarzlose C., Mitzel S., Feldmann H.
    Yeast 12:67-76(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 90843 / S288c / FY73.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiDCAM_YEAST
AccessioniPrimary (citable) accession number: P21182
Secondary accession number(s): D6W216
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: July 6, 2016
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 7060 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

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.