A3DPI4 (A3DPI4_STAMF) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
S-adenosylmethionine decarboxylase proenzyme HAMAP MF_00464
Short name=AdoMetDC HAMAP MF_00464
Short name=SAMDC HAMAP MF_00464
EC=4.1.1.50 HAMAP MF_00464

Gene names

Name:	speH HAMAP MF_00464
Ordered Locus Names:	Smar_1454

Organism

Staphylothermus marinus (strain ATCC 43588 / DSM 3639 / F1) [Complete proteome] [HAMAP]

Taxonomic identifier

399550 [NCBI]

Taxonomic lineage

Archaea › Crenarchaeota › Thermoprotei › Desulfurococcales › Desulfurococcaceae › Staphylothermus

Protein attributes

Sequence length	130 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine By similarity. HAMAP MF_00464
Catalytic activity	S-adenosyl-L-methionine = (5-deoxy-5-adenosyl)(3-aminopropyl)-methylsulfonium salt + CO2. HAMAP MF_00464
Cofactor	Pyruvoyl group By similarity. HAMAP MF_00464
Pathway	Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1. HAMAP MF_00464
Subunit structure	Heterotetramer of two alpha and two beta chains arranged as a dimer of alpha/beta heterodimers By similarity. HAMAP MF_00464
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. HAMAP MF_00464
Sequence similarities	Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily. HAMAP MF_00464

Ontologies

Keywords
Biological process	Polyamine biosynthesis HAMAP MF_00464 Spermidine biosynthesis HAMAP MF_00464
Ligand	Pyruvate HAMAP MF_00464 S-adenosyl-L-methionine HAMAP MF_00464 Schiff base HAMAP MF_00464
Molecular function	Decarboxylase HAMAP MF_00464 Lyase
PTM	Autocatalytic cleavage HAMAP MF_00464 Zymogen HAMAP MF_00464
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	S-adenosylmethioninamine biosynthetic process Inferred from electronic annotation. Source: HAMAP spermidine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular function	adenosylmethionine decarboxylase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Sites
	Active site	76	1	Schiff-base intermediate with substrate; via pyruvic acid By similarity HAMAP MF_00464
	Active site	81	1	Proton acceptor; for processing activity By similarity HAMAP MF_00464
	Active site	96	1	Proton donor; for catalytic activity By similarity HAMAP MF_00464
	Site	75 – 76	2	Cleavage (non-hydrolytic); by autolysis By similarity HAMAP MF_00464
Amino acid modifications
	Modified residue	76	1	Pyruvic acid (Ser); by autocatalysis By similarity HAMAP MF_00464

Sequences

	Sequence		Length	Mass (Da)
	A3DPI4 [UniParc]. Last modified March 20, 2007. Version 1. Checksum: B78B4D60F0E425D4	FASTA	130	14,660
	10 20 30 40 50 60 MLMEREMLLK ENTEKPVIGK HVYGELYGCD PEILSDAEKL VEIVRKASEI GGFTLLDVKA 70 80 90 100 110 120 WRISPGVSVV GIVLESHISI HTWPEYGFAT VDVYTCGETG DPVSAYLYIV KSLRAKKYTL 130 KTSDRSYEWV

References

[1]

"Complete genome sequence of Staphylothermus marinus Stetter and Fiala 1986 type strain F1." Anderson I.J., Sun H., Lapidus A., Copeland A., Glavina Del Rio T., Tice H., Dalin E., Lucas S., Barry K., Land M., Richardson P., Huber H., Kyrpides N.C. Stand. Genomic Sci. 1:183-188(2009) Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

[2]

"The complete genome sequence of Staphylothermus marinus reveals differences in sulfur metabolism among heterotrophic Crenarchaeota." Anderson I.J., Dharmarajan L., Rodriguez J., Hooper S., Porat I., Ulrich L.E., Elkins J.G., Mavromatis K., Sun H., Land M., Lapidus A., Lucas S., Barry K., Huber H., Zhulin I.B., Whitman W.B., Mukhopadhyay B., Woese C., Bristow J., Kyrpides N. BMC Genomics 10:145-145(2009) [PubMed: 19341479] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000575 Genomic DNA. Translation: ABN70544.1.
RefSeq	YP_001041452.1. NC_009033.1.
3D structure databases
ProteinModelPortal	A3DPI4.
ModBase	Search...
Protein-protein interaction databases
STRING	A3DPI4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4907002.
GenomeReviews	Gene locus Smar_1454 in contig CP000575_GR.
KEGG	smr:Smar_1454.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	arNOG10813.
HOGENOM	HBG485559.
OMA	ISNKFEP.
ProtClustDB	CLSK2399751.
Enzyme and pathway databases
BioCyc	SMAR399550:SMAR_1454-MONOMER.
Family and domain databases
HAMAP	MF_00464. AdoMetDC_1. [Tree]
InterPro	IPR003826. S-AdoMet_decarboxylase-bac/arc. IPR016067. S-AdoMet_deCO2ase_core. IPR017716. S-AdoMet_deCOase_pro-enz. [Graphical view]
Gene3D	G3DSA:3.60.90.10. SAM_decarbox. 1 hit.
KO	K01611.
Pfam	PF02675. AdoMet_dc. 1 hit. [Graphical view]
SUPFAM	SSF56276. S-AdenosylMet_decarbase_core. 1 hit.
TIGRFAMs	TIGR03330. SAM_DCase_Bsu. 1 hit.
ProtoNet	Search...

Entry information

Entry name

A3DPI4_STAMF

Accession

Primary (citable) accession number: A3DPI4

Entry history

Integrated into UniProtKB/TrEMBL:	March 20, 2007
Last sequence update:	March 20, 2007
Last modified:	November 16, 2011
This is version 30 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)