A4YI24 (A4YI24_METS5) 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:	Msed_1936

Organism

Metallosphaera sedula (strain ATCC 51363 / DSM 5348) [Complete proteome] [HAMAP]

Taxonomic identifier

399549 [NCBI]

Taxonomic lineage

Archaea › Crenarchaeota › Thermoprotei › Sulfolobales › Sulfolobaceae › Metallosphaera

Protein attributes

Sequence length	129 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)
	A4YI24 [UniParc]. Last modified May 29, 2007. Version 1. Checksum: BBE6A67E35D7B8AD	FASTA	129	14,416
	10 20 30 40 50 60 MGGQNMMGVE LRGTPRVVGK EVFGNLYDCD TEILKDSEKL KQIAVQATKE GNMTLLDVRA 70 80 90 100 110 120 WKIGEGVSVV AIVLESHVTI HTWPEHNFAT VDVYSCGSHT DPRKAFNYIV TELKAKRFNV NEADRSSEF

References

[1]

"The genome sequence of the metal-mobilizing, extremely thermoacidophilic archaeon Metallosphaera sedula provides insights into bioleaching-associated metabolism." Auernik K.S., Maezato Y., Blum P.H., Kelly R.M. Appl. Environ. Microbiol. 74:682-692(2008) [PubMed: 18083856] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000682 Genomic DNA. Translation: ABP96076.1.
RefSeq	YP_001192000.1. NC_009440.1.
3D structure databases
ProteinModelPortal	A4YI24.
ModBase	Search...
Protein-protein interaction databases
STRING	A4YI24.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5103323.
GenomeReviews	Gene locus Msed_1936 in contig CP000682_GR.
KEGG	mse:Msed_1936.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	arNOG10813.
HOGENOM	HBG485559.
OMA	ISNKFEP.
ProtClustDB	PRK00458.
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

A4YI24_METS5

Accession

Primary (citable) accession number: A4YI24

Entry history

Integrated into UniProtKB/TrEMBL:	May 29, 2007
Last sequence update:	May 29, 2007
Last modified:	November 16, 2011
This is version 29 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)