B9MLX4 (SPEH_ANATD) 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 beta chain
2. S-adenosylmethionine decarboxylase alpha chain

Gene names

Name:	speH
Ordered Locus Names:	Athe_2122

Organism

Anaerocellum thermophilum (strain DSM 6725 / Z-1320) [Complete proteome] [HAMAP]

Taxonomic identifier

521460 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Thermoanaerobacterales › Thermoanaerobacterales Family III. Incertae Sedis › Caldicellulosiruptor

Protein attributes

Sequence length	124 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. 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.
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.

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	spermidine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
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 – 62	62	S-adenosylmethionine decarboxylase beta chain By similarity		PRO_1000193167
	Chain	63 – 124	62	S-adenosylmethionine decarboxylase alpha chain By similarity		PRO_1000193168
Sites
	Active site	63	1	Schiff-base intermediate with substrate; via pyruvic acid By similarity
	Active site	68	1	Proton acceptor; for processing activity By similarity
	Active site	83	1	Proton donor; for catalytic activity By similarity
	Site	62 – 63	2	Cleavage (non-hydrolytic); by autolysis By similarity
Amino acid modifications
	Modified residue	63	1	Pyruvic acid (Ser); by autocatalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	B9MLX4 [UniParc]. Last modified March 24, 2009. Version 1. Checksum: 4EA13C00427B88B4	FASTA	124	13,837
	10 20 30 40 50 60 MHALGRHIIA ELYGCDKEVL NNRELIEKIM VESALKAGAE VREVAFHKFS PQGVSGVVVI 70 80 90 100 110 120 SESHLTIHTW PELGYAAVDV FTCGERVDPW QACNYITEML KASHMTTTEV KRGLFEQPVK VANL

References

[1]

"Complete sequence of chromosome of Anaerocellum thermophilum DSM 6725." Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Meincke L., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Kataeva I., Adams M.W.W. Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 6725 / Z-1320.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001393 Genomic DNA. Translation: ACM61197.1.
RefSeq	YP_002573970.1. NC_012034.1.
3D structure databases
ProteinModelPortal	B9MLX4.
SMR	B9MLX4. Positions 3-117.
ModBase	Search...
Protein-protein interaction databases
STRING	B9MLX4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	7408831.
GenomeReviews	Gene locus Athe_2122 in contig CP001393_GR.
KEGG	ate:Athe_2122.
PATRIC	20901498. VBIAnaThe135187_2237.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	ISNKFEP.
ProtClustDB	PRK03124.
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

SPEH_ANATD

Accession

Primary (citable) accession number: B9MLX4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 28, 2009
Last sequence update:	March 24, 2009
Last modified:	January 25, 2012
This is version 18 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program