B5YF62 (B5YF62_DICT6) Unreviewed, UniProtKB/TrEMBL
Last modified
December 14, 2011.
Version 17.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize orderNames 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 |
| ||||
| Organism | Dictyoglomus thermophilum (strain ATCC 35947 / DSM 3960 / H-6-12) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 309799 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Dictyoglomi › Dictyoglomales › Dictyoglomaceae › Dictyoglomus |
Protein attributes
| Sequence length | 142 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 processInferred 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 | 67 | 1 | Schiff-base intermediate with substrate; via pyruvic acid By similarity HAMAP MF_00464 | ||||||
| Active site | 72 | 1 | Proton acceptor; for processing activity By similarity HAMAP MF_00464 | ||||||
| Active site | 87 | 1 | Proton donor; for catalytic activity By similarity HAMAP MF_00464 | ||||||
| Site | 66 – 67 | 2 | Cleavage (non-hydrolytic); by autolysis By similarity HAMAP MF_00464 | ||||||
Amino acid modifications | |||||||||
| Modified residue | 67 | 1 | Pyruvic acid (Ser); by autocatalysis By similarity HAMAP MF_00464 | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "The complete genome sequence of Dictyoglomus thermophilum strain ATCC 35947 / DSM 3960 / H-6-12." Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G. Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP001146 Genomic DNA. Translation: ACI19352.1. |
| RefSeq | YP_002251170.1. NC_011297.1. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | B5YF62. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 6944906. |
| GenomeReviews | Gene locus DICTH_1351 in contig CP001146_GR. |
| KEGG | dth:DICTH_1351. |
| PATRIC | 21807326. VBIDicThe33784_1294. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG485559. |
| OMA | SYFFKFS. |
| ProtClustDB | CLSK2409695. |
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 | B5YF62_DICT6 | ||||||||
| Accession | Primary (citable) accession number: B5YF62 | ||||||||
| Entry history |
| ||||||||
| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

Clusters with