Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q2JWR6 (Q2JWR6_SYNJA) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
S-adenosylmethionine decarboxylase proenzyme HAMAP-Rule MF_00464

Short name=AdoMetDC HAMAP-Rule MF_00464
Short name=SAMDC HAMAP-Rule MF_00464
EC=4.1.1.50 HAMAP-Rule MF_00464
Gene names
Name:speH HAMAP-Rule MF_00464
Ordered Locus Names:CYA_0574 EMBL ABC98790.1
OrganismSynechococcus sp. (strain JA-3-3Ab) (Cyanobacteria bacterium Yellowstone A-Prime) [Complete proteome] [HAMAP] EMBL ABC98790.1
Taxonomic identifier321327 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus

Protein attributes

Sequence length152 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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-Rule MF_00464

Catalytic activity

S-adenosyl-L-methionine = S-adenosyl 3-(methylthio)propylamine + CO2. HAMAP-Rule MF_00464 SAAS SAAS003826

Cofactor

Pyruvoyl group By similarity. HAMAP-Rule MF_00464

Pathway

Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1. HAMAP-Rule MF_00464 SAAS SAAS003826

Subunit structure

Heterotetramer of two alpha and two beta chains arranged as a dimer of alpha/beta heterodimers By similarity. HAMAP-Rule 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-Rule MF_00464

Sequence similarities

Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily. HAMAP-Rule MF_00464

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site761Schiff-base intermediate with substrate; via pyruvic acid By similarity HAMAP-Rule MF_00464
Active site811Proton acceptor; for processing activity By similarity HAMAP-Rule MF_00464
Active site961Proton donor; for catalytic activity By similarity HAMAP-Rule MF_00464
Site75 – 762Cleavage (non-hydrolytic); by autolysis By similarity HAMAP-Rule MF_00464

Amino acid modifications

Modified residue761Pyruvic acid (Ser); by autocatalysis By similarity HAMAP-Rule MF_00464

Sequences

Sequence LengthMass (Da)Tools
Q2JWR6 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: 8A9D3D82BB8AF51A

FASTA15216,870
        10         20         30         40         50         60 
MLHTLSGQLG DRSLALIGIH CILELYDCPA KLLDDVSLVQ QALREAARRS NSTLLGELCH 

        70         80         90        100        110        120 
PFEPQGITAL ALLGESHISI HTWPEAGYAA VDVFTCGRHT RPEAACEYLI QVFQARRYSL 

       130        140        150 
RKLPRRTTDA APIEEMADFP KALSCETAGR RR 

« Hide

References

[1]"Population level functional diversity in a microbial community revealed by comparative genomic and metagenomic analyses."
Bhaya D., Grossman A.R., Steunou A.S., Khuri N., Cohan F.M., Hamamura N., Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.
ISME J. 1:703-713(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JA-3-3Ab EMBL ABC98790.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000239 Genomic DNA. Translation: ABC98790.1.
RefSeqYP_474053.1. NC_007775.1.

3D structure databases

ProteinModelPortalQ2JWR6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING321327.CYA_0574.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC98790; ABC98790; CYA_0574.
GeneID3897371.
KEGGcya:CYA_0574.
PATRIC23809415. VBISynSp90045_0572.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1586.
HOGENOMHOG000216579.
KOK01611.
OMAGNLYGCN.
OrthoDBEOG6358J6.

Enzyme and pathway databases

BioCycSSP321327:GHFX-570-MONOMER.
UniPathwayUPA00331; UER00451.

Family and domain databases

Gene3D3.60.90.10. 1 hit.
HAMAPMF_00464. AdoMetDC_1.
InterProIPR003826. AdoMetDC_fam_prok.
IPR016067. S-AdoMet_deCO2ase_core.
IPR017716. S-AdoMet_deCOase_pro-enz.
[Graphical view]
PfamPF02675. AdoMet_dc. 1 hit.
[Graphical view]
SUPFAMSSF56276. SSF56276. 1 hit.
TIGRFAMsTIGR03330. SAM_DCase_Bsu. 1 hit.
ProtoNetSearch...

Entry information

Entry nameQ2JWR6_SYNJA
AccessionPrimary (citable) accession number: Q2JWR6
Entry history
Integrated into UniProtKB/TrEMBL: March 7, 2006
Last sequence update: March 7, 2006
Last modified: July 9, 2014
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)