Q39677 (DCAM2_DIACA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
S-adenosylmethionine decarboxylase proenzyme 2
Short name=AdoMetDC 2
Short name=SAMDC 2
EC=4.1.1.50

Cleaved into the following 2 chains:

1. S-adenosylmethionine decarboxylase 2 alpha chain
2. S-adenosylmethionine decarboxylase 2 beta chain

Gene names

Name:	SAMDC2
Synonyms:	SAMDC16

Organism

Dianthus caryophyllus (Carnation) (Clove pink)

Taxonomic identifier

3570 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › Caryophyllales › Caryophyllaceae › Dianthus

Protein attributes

Sequence length	377 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Catalytic activity	S-adenosyl-L-methionine = (5-deoxy-5-adenosyl)(3-aminopropyl)-methylsulfonium salt + CO2.
Cofactor	Pyruvoyl group By similarity.
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.
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
Gene Ontology (GO)
Biological_process	S-adenosylmethioninamine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway spermidine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW spermine biosynthetic process Inferred from electronic annotation. Source: InterPro
Molecular_function	adenosylmethionine decarboxylase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 83	83	S-adenosylmethionine decarboxylase 2 beta chain By similarity		PRO_0000030005
	Chain	84 – 377	294	S-adenosylmethionine decarboxylase 2 alpha chain By similarity		PRO_0000030006
Sites
	Active site	24	1	By similarity
	Active site	27	1	By similarity
	Active site	84	1	Schiff-base intermediate with substrate; via pyruvic acid By similarity
	Active site	98	1	Proton donor; for catalytic activity By similarity
	Active site	246	1	Proton acceptor; for processing activity By similarity
	Active site	259	1	Proton acceptor; for processing activity By similarity
	Site	83 – 84	2	Cleavage (non-hydrolytic); by autolysis By similarity
Amino acid modifications
	Modified residue	84	1	Pyruvic acid (Ser); by autocatalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q39677 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: C3E58AAD143F1AD6	FASTA	377	41,344
	10 20 30 40 50 60 MTIPMMGNTT DDNNNMTISA IGFEGFEKRL EISFFEPGIF VDPEGKGLRA LSKAHLDEIL 70 80 90 100 110 120 GPAECTIVDS LANESVDSYV LSESSLFVYS YKIIIKTCGT TKLLNSIPPI LRLAETLFLD 130 140 150 160 170 180 VKSVRYTRGS FIFPGAQSFP HRSFSEEVAV LDNYFAKLGA GSKAIVMGSP GKPQKWHVYS 190 200 210 220 230 240 ATAETNYDDP VYTLEMCMTG LDKEKASVFF KSQSASAAVM TESSGIRKIL PDSVICDFDF 250 260 270 280 290 300 EPCGYSMNAI EGPAVSTIHI TPEDGFSYAS FEAVGYDLQV VDLNLLVERV LACFEPKEFS 310 320 330 340 350 360 IAVHADTDTA DKVLARNCSV NVIGYSREEG GIEELGLGGS VFYQKFCKGT APVCPPAPKK 370 TLKCCWKEEE IDEEMEF

References

[1]	"Nucleotide sequence of cDNAs encoding S-adenosylmethionine decarboxylase from carnation flower." Lee M.M., Lee S.H., Park K.Y. Plant Gene Register PGR95-139 Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. White Sim. Tissue: Petal.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U38527 mRNA. Translation: AAD09840.1.
PIR	T10708.
3D structure databases
ProteinModelPortal	Q39677.
SMR	Q39677. Positions 26-83, 85-348.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
UniPathway	UPA00331; UER00451.
Family and domain databases
Gene3D	3.60.90.10. 1 hit.
InterPro	IPR001985. S-AdoMet_decarboxylase. IPR018167. S-AdoMet_decarboxylase_subgr. IPR016067. S-AdoMet_deCO2ase_core. IPR018166. S-AdoMet_deCO2ase_CS. [Graphical view]
PANTHER	PTHR11570. PTHR11570. 1 hit.
Pfam	PF01536. SAM_decarbox. 1 hit. [Graphical view]
PIRSF	PIRSF001355. S-AdenosylMet_decarboxylase. 1 hit.
SUPFAM	SSF56276. S-AdenosylMet_decarbase_core. 1 hit.
TIGRFAMs	TIGR00535. SAM_DCase. 1 hit.
PROSITE	PS01336. ADOMETDC. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DCAM2_DIACA

Accession

Primary (citable) accession number: Q39677

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	November 1, 1996
Last modified:	March 6, 2013
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program