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Q9WZC3 (SPEH_THEMA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
S-adenosylmethionine decarboxylase proenzyme

Short name=AdoMetDC
Short name=SAMDC
EC=4.1.1.50
Gene names
Name:speH
Ordered Locus Names:TM_0655
OrganismThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) [Reference proteome] [HAMAP]
Taxonomic identifier243274 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga

Protein attributes

Sequence length130 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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

Cofactor

Pyruvoyl group Probable.

Pathway

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

Subunit structure

Heterotetramer of two alpha and two beta chains arranged as a dimer of alpha/beta heterodimers. Ref.2

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 Probable. HAMAP-Rule MF_00464

Sequence similarities

Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 6262S-adenosylmethionine decarboxylase beta chain Probable
PRO_0000030123
Chain63 – 13068S-adenosylmethionine decarboxylase alpha chain Probable
PRO_0000030124

Sites

Active site631Schiff-base intermediate with substrate; via pyruvic acid By similarity
Active site681Proton acceptor; for processing activity Probable
Active site831Proton donor; for catalytic activity Probable
Site62 – 632Cleavage (non-hydrolytic); by autolysis Probable

Amino acid modifications

Modified residue631Pyruvic acid (Ser); by autocatalysis Probable

Experimental info

Mutagenesis551S → A: Cleaves more rapidly than the wild-type. Ref.2
Mutagenesis631S → A: Loss of processing. Ref.2
Mutagenesis681H → A: Cleaves much more slowly than the wild-type, but the addition of hydroxylamine which is known to cleave ester bonds leads to the cleavage of this mutant. Ref.2
Mutagenesis831C → A: Cleaves more rapidly than the wild-type. Ref.2

Secondary structure

....................... 130
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9WZC3 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 7659FE20A2019928

FASTA13014,785
        10         20         30         40         50         60 
MKSLGRHLVA EFYECDREVL DNVQLIEQEM KQAAYESGAT IVTSTFHRFL PYGVSGVVVI 

        70         80         90        100        110        120 
SESHLTIHTW PEYGYAAIDL FTCGEDVDPW KAFEHLKKAL KAKRVHVVEH ERGRYDEIGI 

       130 
PEDSPHKAAV 

« Hide

References

« Hide 'large scale' references
[1]"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima."
Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. expand/collapse author list , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.
Nature 399:323-329(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[2]"Evolutionary links as revealed by the structure of Thermotoga maritima S-adenosylmethionine decarboxylase."
Toms A.V., Kinsland C., McCloskey D.E., Pegg A.E., Ealick S.E.
J. Biol. Chem. 279:33837-33846(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF WILD-TYPE AND MUTANT ALA-63, SUBUNIT, SELF-PROCESSING, ACTIVE SITES, MUTAGENESIS OF SER-55; SER-63; HIS-68 AND CYS-83.
[3]"Crystal structure of S-adenosylmethionine decarboxylase proenzyme (tm0655) from Thermotoga maritima at 1.2-A resolution."
Joint center for structural genomics (JCSG)
Submitted (MAR-2005) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000512 Genomic DNA. Translation: AAD35739.1.
PIRD72348.
RefSeqNP_228464.1. NC_000853.1.
YP_007977005.1. NC_021214.1.
YP_008990376.1. NC_023151.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1TLUX-ray1.55A/B1-130[»]
1TMIX-ray1.70A/B1-130[»]
1VR7X-ray1.20A/B1-130[»]
3IWBX-ray2.06A/C64-130[»]
B/D1-62[»]
3IWCX-ray1.90A/C64-130[»]
B/D1-62[»]
3IWDX-ray1.90A/C64-130[»]
B/D1-62[»]
ProteinModelPortalQ9WZC3.
SMRQ9WZC3. Positions 2-121.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243274.TM0655.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD35739; AAD35739; TM_0655.
GeneID897764.
KEGGtma:TM0655.
tmi:THEMA_01390.
tmm:Tmari_0655.
PATRIC23936224. VBITheMar51294_0665.

Phylogenomic databases

eggNOGCOG1586.
KOK01611.
OMAINPWDAC.
OrthoDBEOG6358J6.

Enzyme and pathway databases

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...

Other

EvolutionaryTraceQ9WZC3.

Entry information

Entry nameSPEH_THEMA
AccessionPrimary (citable) accession number: Q9WZC3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 24, 2001
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways