P79888 (DCAM_XENLA) Reviewed, UniProtKB/Swiss-Prot

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

Gene names

Name:

amd1

Organism

Xenopus laevis (African clawed frog)

Taxonomic identifier

8355 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Mesobatrachia › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length	335 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)

Function	Involved in the biosynthesis of the polyamines, spermine 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.
Developmental stage	First expressed at stage I of oocyte development, and is maximally expressed at stage II. Levels decline during oocyte maturation and after fertilization, and also in the early neurula. Levels increase dramatically during the late neurula stage reaching a maximum at the tail bud stage.
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.
Caution	It is uncertain whether Met-1 or Met-3 is the initiator.

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	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 – 69	69	S-adenosylmethionine decarboxylase beta chain		PRO_0000029971
	Chain	70 – 335	266	S-adenosylmethionine decarboxylase alpha chain		PRO_0000029972
Sites
	Active site	12	1	By similarity
	Active site	15	1	By similarity
	Active site	70	1	Schiff-base intermediate with substrate; via pyruvic acid By similarity
	Active site	84	1	Proton donor; for catalytic activity By similarity
	Active site	231	1	Proton acceptor; for processing activity By similarity
	Active site	245	1	Proton acceptor; for processing activity By similarity
	Site	69 – 70	2	Cleavage (non-hydrolytic); by autolysis By similarity
Amino acid modifications
	Modified residue	70	1	Pyruvic acid (Ser); by autocatalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	P79888 [UniParc]. Last modified May 1, 1997. Version 1. Checksum: BA158A226F21F28C	FASTA	335	38,819
	10 20 30 40 50 60 MKMEESAAHF FEGTEKLLEL WFSQQDASKG SGDLRDIPRF EWDKLLENVH CLIISVTKTD 70 80 90 100 110 120 KQEAYVLSES SMFVSKRRFI LKTCGTTLLL QALVPLLELA REYCGFDGIQ NFFYSRKNFM 130 140 150 160 170 180 KPNHQEYPHR NFHEEVEFLN QIFPNGAAYC MGRINSDCWY LYTLDIPDEY VISQPDQTLE 190 200 210 220 230 240 ILMSELDPEV MDQFYMKEGV TANDVTRVSG IRDLITGSVI DATMFSPCGY SMNGMKSDGT 250 260 270 280 290 300 YWTIHITPEP DFSYVSFETN VSLTTYDDLI SKVVDVFKPR KFVTTLFVNQ SSKCRTTFSC 310 320 330 AQKIEGFRRV DRQFAQFNDY NFVFTSFAKI QPQQS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Maternal and zygotic expression of mRNA for S-adenosylmethionine decarboxylase and its relevance to the unique polyamine composition in Xenopus oocytes and embryos." Shinga J., Kashiwagi K., Tashiro K., Igarashi K., Shiokawa K. Biochim. Biophys. Acta 1308:31-40(1996) [PubMed: 8765748] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Tail bud.
[2]	NIH - Xenopus Gene Collection (XGC) project Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	S82621 mRNA. Translation: AAB36519.1. BC042281 mRNA. Translation: AAH42281.1.
PIR	S72197.
RefSeq	NP_001080360.1. NM_001086891.1.
UniGene	Xl.7078.
3D structure databases
ProteinModelPortal	P79888.
SMR	P79888. Positions 8-329.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	380052.
KEGG	xla:380052.
Organism-specific databases
CTD	262.
Xenbase	XB-GENE-484615. amd1.
Phylogenomic databases
HOVERGEN	HBG000761.
Family and domain databases
InterPro	IPR001985. S-AdoMet_decarboxylase. IPR018167. S-AdoMet_decarboxylase_subgr. IPR016067. S-AdoMet_deCO2ase_core. IPR018166. S-AdoMet_deCO2ase_CS. [Graphical view]
Gene3D	G3DSA:3.60.90.10. SAM_decarbox. 1 hit.
KO	K01611.
PANTHER	PTHR11570. SAM_decarbox. 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

DCAM_XENLA

Accession

Primary (citable) accession number: P79888
Secondary accession number(s): Q5D0C5

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	May 1, 1997
Last modified:	November 16, 2011
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program