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A4XJ25 (SPEH_CALS8) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:Csac_1308
OrganismCaldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903) [Complete proteome] [HAMAP]
Taxonomic identifier351627 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacterales Family III. Incertae SedisCaldicellulosiruptor

Protein attributes

Sequence length124 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred 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-Rule MF_00464

Catalytic activity

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

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

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-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 By similarity
PRO_1000013670
Chain63 – 12462S-adenosylmethionine decarboxylase alpha chain By similarity
PRO_0000315023

Sites

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

Amino acid modifications

Modified residue631Pyruvic acid (Ser); by autocatalysis By similarity

Sequences

Sequence LengthMass (Da)Tools
A4XJ25 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: 4EA13C00427B88B4

FASTA12413,837
        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 

« Hide

References

[1]"Genome sequence of the thermophilic hydrogen-producing bacterium Caldicellulosiruptor saccharolyticus DSM 8903."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Lykidis A., van de Werken H.J.G., Verhaart M.R.A., VanFossen A.L., Lewis D.L., Nichols J.D., Goorissen H.P., van Niel E.W.J., Stams F.J.M., Willquist K.U., Ward D.E., van der Oost J., Kelly R.M., Kengen S.M.W., Richardson P.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43494 / DSM 8903.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000679 Genomic DNA. Translation: ABP66910.1.
RefSeqYP_001180101.1. NC_009437.1.

3D structure databases

ProteinModelPortalA4XJ25.
SMRA4XJ25. Positions 3-117.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING351627.Csac_1308.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABP66910; ABP66910; Csac_1308.
GeneID5088248.
KEGGcsc:Csac_1308.
PATRIC21252290. VBICalSac56748_1456.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1586.
HOGENOMHOG000216579.
KOK01611.
OMACGEHSDP.
OrthoDBEOG6358J6.
ProtClustDBPRK03124.

Enzyme and pathway databases

BioCycCSAC351627:GJ17-1341-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 nameSPEH_CALS8
AccessionPrimary (citable) accession number: A4XJ25
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 29, 2007
Last modified: February 19, 2014
This is version 42 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

PATHWAY comments

Index of metabolic and biosynthesis pathways