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Q9WZC3

- SPEH_THEMA

UniProt

Q9WZC3 - SPEH_THEMA

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Protein

S-adenosylmethionine decarboxylase proenzyme

Gene

speH

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Cofactori

Pyruvoyl group.Curated

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei62 – 632Cleavage (non-hydrolytic); by autolysisCurated
Active sitei63 – 631Schiff-base intermediate with substrate; via pyruvic acidBy similarity
Active sitei68 – 681Proton acceptor; for processing activity1 Publication
Active sitei83 – 831Proton donor; for catalytic activity1 Publication

GO - Molecular functioni

  1. adenosylmethionine decarboxylase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. S-adenosylmethioninamine biosynthetic process Source: UniProtKB-HAMAP
  2. spermidine biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

Polyamine biosynthesis, Spermidine biosynthesis

Keywords - Ligandi

Pyruvate, S-adenosyl-L-methionine, Schiff base

Enzyme and pathway databases

UniPathwayiUPA00331; UER00451.

Names & Taxonomyi

Protein namesi
Recommended name:
S-adenosylmethionine decarboxylase proenzyme (EC:4.1.1.50)
Short name:
AdoMetDC
Short name:
SAMDC
Cleaved into the following 2 chains:
Gene namesi
Name:speH
Ordered Locus Names:TM_0655
OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Taxonomic identifieri243274 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
ProteomesiUP000008183: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi55 – 551S → A: Cleaves more rapidly than the wild-type. 1 Publication
Mutagenesisi63 – 631S → A: Loss of processing. 1 Publication
Mutagenesisi68 – 681H → 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. 1 Publication
Mutagenesisi83 – 831C → A: Cleaves more rapidly than the wild-type. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 6262S-adenosylmethionine decarboxylase beta chainCuratedPRO_0000030123Add
BLAST
Chaini63 – 13068S-adenosylmethionine decarboxylase alpha chainCuratedPRO_0000030124Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei63 – 631Pyruvic acid (Ser); by autocatalysisCurated

Post-translational modificationi

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).Curated

Keywords - PTMi

Autocatalytic cleavage, Zymogen

Interactioni

Subunit structurei

Heterotetramer of two alpha and two beta chains arranged as a dimer of alpha/beta heterodimers.1 Publication

Protein-protein interaction databases

STRINGi243274.TM0655.

Structurei

Secondary structure

1
130
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 1412
Helixi17 – 204
Helixi23 – 3715
Beta strandi41 – 488
Beta strandi50 – 523
Beta strandi54 – 607
Beta strandi63 – 708
Helixi71 – 733
Beta strandi75 – 8410
Helixi89 – 10012
Beta strandi103 – 11412
Helixi115 – 1184

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliQ9WZC3.
SMRiQ9WZC3. Positions 2-121.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9WZC3.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1586.
InParanoidiQ9WZC3.
KOiK01611.
OMAiINPWDAC.
OrthoDBiEOG6358J6.

Family and domain databases

Gene3Di3.60.90.10. 1 hit.
HAMAPiMF_00464. AdoMetDC_1.
InterProiIPR003826. AdoMetDC_fam_prok.
IPR016067. S-AdoMet_deCO2ase_core.
IPR017716. S-AdoMet_deCOase_pro-enz.
[Graphical view]
PfamiPF02675. AdoMet_dc. 1 hit.
[Graphical view]
SUPFAMiSSF56276. SSF56276. 1 hit.
TIGRFAMsiTIGR03330. SAM_DCase_Bsu. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9WZC3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKSLGRHLVA EFYECDREVL DNVQLIEQEM KQAAYESGAT IVTSTFHRFL
60 70 80 90 100
PYGVSGVVVI SESHLTIHTW PEYGYAAIDL FTCGEDVDPW KAFEHLKKAL
110 120 130
KAKRVHVVEH ERGRYDEIGI PEDSPHKAAV
Length:130
Mass (Da):14,785
Last modified:November 1, 1999 - v1
Checksum:i7659FE20A2019928
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE000512 Genomic DNA. Translation: AAD35739.1.
PIRiD72348.
RefSeqiNP_228464.1. NC_000853.1.
YP_007977005.1. NC_021214.1.
YP_008990376.1. NC_023151.1.

Genome annotation databases

EnsemblBacteriaiAAD35739; AAD35739; TM_0655.
GeneIDi18092134.
897764.
KEGGitma:TM0655.
tmi:THEMA_01390.
tmm:Tmari_0655.
PATRICi23936224. VBITheMar51294_0665.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE000512 Genomic DNA. Translation: AAD35739.1 .
PIRi D72348.
RefSeqi NP_228464.1. NC_000853.1.
YP_007977005.1. NC_021214.1.
YP_008990376.1. NC_023151.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1TLU X-ray 1.55 A/B 1-130 [» ]
1TMI X-ray 1.70 A/B 1-130 [» ]
1VR7 X-ray 1.20 A/B 1-130 [» ]
3IWB X-ray 2.06 A/C 64-130 [» ]
B/D 1-62 [» ]
3IWC X-ray 1.90 A/C 64-130 [» ]
B/D 1-62 [» ]
3IWD X-ray 1.90 A/C 64-130 [» ]
B/D 1-62 [» ]
ProteinModelPortali Q9WZC3.
SMRi Q9WZC3. Positions 2-121.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 243274.TM0655.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAD35739 ; AAD35739 ; TM_0655 .
GeneIDi 18092134.
897764.
KEGGi tma:TM0655.
tmi:THEMA_01390.
tmm:Tmari_0655.
PATRICi 23936224. VBITheMar51294_0665.

Phylogenomic databases

eggNOGi COG1586.
InParanoidi Q9WZC3.
KOi K01611.
OMAi INPWDAC.
OrthoDBi EOG6358J6.

Enzyme and pathway databases

UniPathwayi UPA00331 ; UER00451 .

Miscellaneous databases

EvolutionaryTracei Q9WZC3.

Family and domain databases

Gene3Di 3.60.90.10. 1 hit.
HAMAPi MF_00464. AdoMetDC_1.
InterProi IPR003826. AdoMetDC_fam_prok.
IPR016067. S-AdoMet_deCO2ase_core.
IPR017716. S-AdoMet_deCOase_pro-enz.
[Graphical view ]
Pfami PF02675. AdoMet_dc. 1 hit.
[Graphical view ]
SUPFAMi SSF56276. SSF56276. 1 hit.
TIGRFAMsi TIGR03330. SAM_DCase_Bsu. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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).

Entry informationi

Entry nameiSPEH_THEMA
AccessioniPrimary (citable) accession number: Q9WZC3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 24, 2001
Last sequence update: November 1, 1999
Last modified: October 29, 2014
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3