Reviewed, UniProtKB/Swiss-Prot P21182 (DCAM_YEAST)

Names and origin

Protein names

Recommended name:
    S-adenosylmethionine decarboxylase proenzyme
      Short name=AdoMetDC
      Short name=SAMDC
    EC=4.1.1.50
Cleaved into the following 2 chains:
    1- Recommended name:
            S-adenosylmethionine decarboxylase alpha chain
    2- Recommended name:
            S-adenosylmethionine decarboxylase beta chain

Gene names

Name:	SPE2
Ordered Locus Names:	YOL052C
ORF Names:	O1275

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	396 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	S-adenosylmethionine decarboxylase is essential for normal growth, sporulation, maintenance of ds-RNA virus, biosynthesis of spermine and spermidine.
Catalytic activity	S-adenosyl-L-methionine = (5-deoxy-5-adenosyl)(3-aminopropyl)-methylsulfonium salt + CO2.
Cofactor	Pyruvoyl group.
Pathway	Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1.
Post-translational modification	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.
Miscellaneous	Present with 7060 molecules/cell in log phase SD medium. Ref.4
Sequence similarities	Belongs to the eukaryotic AdoMetDC family.

Ontologies

Keywords
Biological process	Polyamine biosynthesis Spermidine biosynthesis
Ligand	Pyruvate S-adenosyl-L-methionine Schiff base
Molecular function	Decarboxylase Lyase
PTM	Autocatalytic cleavage Zymogen
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	pantothenate biosynthetic process Inferred from mutant phenotype. Source: SGD spermidine biosynthetic process Inferred from mutant phenotype. Source: SGD spermine biosynthetic process Inferred from mutant phenotype. Source: SGD
Cellular component	cytoplasm Inferred from direct assay. Source: SGD nucleus Inferred from direct assay. Source: SGD
Molecular function	adenosylmethionine decarboxylase activity Ref.1 Inferred from direct assay. Source: SGD protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
AHA1	Q12449	1	EBI-5655,EBI-37072

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 87	87	S-adenosylmethionine decarboxylase beta chain		PRO_0000030033
	Chain	88 – 396	309	S-adenosylmethionine decarboxylase alpha chain		PRO_0000030034
Sites
	Active site	29	1	By similarity
	Active site	32	1	By similarity
	Active site	88	1	Schiff-base intermediate with substrate; via pyruvic acid By similarity
	Active site	102	1	Proton donor; for catalytic activity By similarity
	Active site	287	1	Proton acceptor; for processing activity By similarity
	Active site	301	1	Proton acceptor; for processing activity By similarity
	Site	87 – 88	2	Cleavage (non-hydrolytic); by autolysis
Amino acid modifications
	Modified residue	88	1	Pyruvic acid (Ser); by autocatalysis

Sequences

	Sequence		Length	Mass (Da)
	P21182-1 [UniParc]. Last modified May 1, 1991. Version 1. Checksum: 8B63676CB5636D71	FASTA	396	46,232
	10 20 30 40 50 60 MTVTIKELTN HNYIDHELSA TLDSTDAFEG PEKLLEIWFF PHKKSITTEK TLRNIGMDRW 70 80 90 100 110 120 IEILKLVKCE VLSMKKTKEL DAFLLSESSL FVFDHKLTMK TCGTTTTLFC LEKLFQIVEQ 130 140 150 160 170 180 ELSWAFRTTQ GGKYKPFKVF YSRRCFLFPC KQAAIHQNWA DEVDYLNKFF DNGKSYSVGR 190 200 210 220 230 240 NDKSNHWNLY VTETDRSTPK GKEYIEDDDE TFEVLMTELD PECASKFVCG PEASTTALVE 250 260 270 280 290 300 PNEDKGHNLG YQMTKNTRLD EIYVNSAQDS DLSFHHDAFA FTPCGYSSNM ILAEKYYYTL 310 320 330 340 350 360 HVTPEKGWSY ASFESNIPVF DISQGKQDNL DVLLHILNVF QPREFSMTFF TKNYQNQSFQ 370 380 390 KLLSINESLP DYIKLDKIVY DLDDYHLFYM KLQKKI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 2266128] [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: 8789261] [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: 9169874] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[4]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M38434 Genomic DNA. Translation: AAA34421.1. X91067 Genomic DNA. Translation: CAA62536.1. Z74794 Genomic DNA. Translation: CAA99058.1.
PIR	DCBYDM. S12772.
RefSeq	NP_014590.1.
3D structure databases
SMR	P21182. Positions 25-87, 89-394.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-361N.
IntAct	P21182. 1 interaction.
STRING	P21182.
Genome annotation databases
Ensembl	YOL052C; YOL052C; YOL052C; Saccharomyces cerevisiae. [Genome view]
GeneID	854105.
KEGG	sce:YOL052C.
NMPDR	fig|4932.3.peg.5682.
Organism-specific databases
CYGD	YOL052c.
SGD	S000005412. SPE2.
Phylogenomic databases
eggNOG	fuNOG04264.
HOGENOM	HBG610629.
OMA	DIARCKI.
OrthoDB	EOG9Z0CPH.
PhylomeDB	P21182.
Enzyme and pathway databases
BRENDA	4.1.1.50. 250.
Gene expression databases
ArrayExpress	P21182.
Genevestigator	P21182.
GermOnline	YOL052C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR001985. S-AdoMet_decarboxylase. IPR018167. S-AdoMet_decarboxylase_sg. IPR016067. S-AdoMet_deCO2ase_core. IPR018166. S-AdoMet_deCO2ase_CS. [Graphical view]
Gene3D	G3DSA:3.60.90.10. SAM_decarbox. 1 hit.
PANTHER	PTHR11570. SAM_decarbox. 1 hit.
Pfam	PF01536. SAM_decarbox. 1 hit. [Graphical view]
PIRSF	PIRSF001355. S-AdenosylMet_decarboxylase. 1 hit.
TIGRFAMs	TIGR00535. SAM_DCase. 1 hit.
PROSITE	PS01336. ADOMETDC. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	975786.

Entry information

Entry name

DCAM_YEAST

Accession

Primary (citable) accession number: P21182

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	May 1, 1991
Last modified:	February 9, 2010
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)