Reviewed, UniProtKB/Swiss-Prot Q2S990 (SPED_HAHCH)

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 beta chain
    2- Recommended name:
            S-adenosylmethionine decarboxylase alpha chain

Gene names

Name:	speD
Ordered Locus Names:	HCH_06136

Organism

Hahella chejuensis (strain KCTC 2396) [Complete proteome] [HAMAP]

Taxonomic identifier

349521 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Oceanospirillales › Hahellaceae › Hahella

Protein attributes

Sequence length	264 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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.
Catalytic activity	S-adenosyl-L-methionine = (5-deoxy-5-adenosyl)(3-aminopropyl)-methylsulfonium salt + CO2. HAMAP MF_00465
Cofactor	Pyruvoyl group By similarity.
Pathway	Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1. HAMAP MF_00465
Subunit structure	Heterooctamer of four alpha and four beta chains arranged as a tetramer of alpha/beta heterodimers By similarity.
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 prokaryotic AdoMetDC family. Type 2 subfamily.

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
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
Molecule processing
	Chain	1 – 112	112	S-adenosylmethionine decarboxylase beta chain By similarity		PRO_0000273597
	Chain	113 – 264	152	S-adenosylmethionine decarboxylase alpha chain By similarity		PRO_0000273598
Sites
	Active site	113	1	Schiff-base intermediate with substrate; via pyruvic acid By similarity
	Active site	118	1	Proton acceptor; for processing activity By similarity
	Active site	141	1	Proton donor; for catalytic activity By similarity
	Site	112 – 113	2	Cleavage (non-hydrolytic); by autolysis By similarity
Amino acid modifications
	Modified residue	113	1	Pyruvic acid (Ser); by autocatalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2S990-1 [UniParc]. Last modified January 24, 2006. Version 1. Checksum: 7AE2060F8688F4C1	FASTA	264	30,181
	10 20 30 40 50 60 MSEKLKLHGF NNLTKSLSFN IYDICYAQSE KHRQEYIAYI DEQYNAERLT QILTDVVEII 70 80 90 100 110 120 GAHILNVSRQ DYDPHGASVT MLIAEHEVPP PADSSEESPG PLPDAVVAHL DKSHVTVHTY 130 140 150 160 170 180 PESHPDNGIS TFRADIDVST CGLISPLKAL NYLIHSFDSD IVTIDYRVRG FTRDIDGAKL 190 200 210 220 230 240 YIDHDINSIQ NFLSEDTQEA YQMIDVNVYQ ENLFHTKMIL KEFNLDNYLF GTGVSELNAN 250 260 EASNIRERLQ KEMLEIFYSR NMPY

References

[1]

"Genomic blueprint of Hahella chejuensis, a marine microbe producing an algicidal agent." Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G., Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K., Oh T.K., Kim J.F. Nucleic Acids Res. 33:7066-7073(2005) [PubMed: 16352867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000155 Genomic DNA. Translation: ABC32784.1.
RefSeq	YP_437209.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3839656.
GenomeReviews	Gene locus HCH_06136 in contig CP000155_GR.
KEGG	hch:HCH_06136.
NMPDR	fig|349521.5.peg.5379.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q2S990.
OMA	Q2S990. YNAERLT.
Enzyme and pathway databases
BioCyc	HCHE349521:HCH_06136-MON.
Family and domain databases
HAMAP	MF_00465. [Tree]
InterPro	IPR003826. S-AdoMet_decarboxylase-bac/arc. IPR009165. S-AdoMet_deCO2ase_bac. IPR016067. S-AdoMet_deCO2ase_core. [Graphical view]
Gene3D	G3DSA:3.60.90.10. SAM_decarbox. 1 hit.
Pfam	PF02675. AdoMet_dc. 1 hit. [Graphical view]
PIRSF	PIRSF001356. SAM_decarboxylas. 1 hit.
TIGRFAMs	TIGR03331. SAM_DCase_Eco. 1 hit.
ProtoNet	Search...

Entry information

Entry name

SPED_HAHCH

Accession

Primary (citable) accession number: Q2S990

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2007
Last sequence update:	January 24, 2006
Last modified:	June 16, 2009
This is version 23 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)