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Conserved domains on  [gi|2228748666|ref|WP_246907322|]
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adenosylmethionine decarboxylase [Desulfatitalea alkaliphila]

Protein Classification

S-adenosylmethionine decarboxylase( domain architecture ID 10496445)

S-adenosylmethionine decarboxylase 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

CATH:  3.60.90.10
EC:  4.1.1.50
Gene Symbol:  speD
Gene Ontology:  GO:0004014|GO:0008295
PubMed:  11526206|3316212
SCOP:  3001051

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AdoMet_dc pfam02675
S-adenosylmethionine decarboxylase; This family contains several S-adenosylmethionine ...
 8-114 4.60e-52

S-adenosylmethionine decarboxylase; This family contains several S-adenosylmethionine decarboxylase proteins from bacterial and archaebacterial species. S-adenosylmethionine decarboxylase (AdoMetDC), a key enzyme in the biosynthesis of spermidine and spermine, is first synthesized as a proenzyme, which is cleaved post translationally to form alpha and beta subunits. The alpha subunit contains a covalently bound pyruvoyl group derived from serine that is essential for activity.


:

Pssm-ID: 460648  Cd Length: 107  Bit Score: 160.37  E-value: 4.60e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228748666   8 HCILELFECPSELLDDEQFICRAINSAAEASGSTLLTLSSHKFSPQGVTALGLLAESHISIHTWPETGYAAVDAFTCGTH 87
Cdd:pfam02675   1 HLIVDLYGCDPELLDDAELIEQALREAAEAAGATVVEVVFHKFEPQGVSGVVLLAESHISIHTWPEYGYAAVDVFTCGDH 80

                          90       100
                  ....*....|....*....|....*..
gi 2228748666  88 CDPVAACRLLTGLLEAKRQARTVLQRG 114
Cdd:pfam02675  81 VDPEKAFEYLKEALGAKRVSVRELDRG 107
 
Name Accession Description Interval E-value
AdoMet_dc pfam02675
S-adenosylmethionine decarboxylase; This family contains several S-adenosylmethionine ...
 8-114 4.60e-52

S-adenosylmethionine decarboxylase; This family contains several S-adenosylmethionine decarboxylase proteins from bacterial and archaebacterial species. S-adenosylmethionine decarboxylase (AdoMetDC), a key enzyme in the biosynthesis of spermidine and spermine, is first synthesized as a proenzyme, which is cleaved post translationally to form alpha and beta subunits. The alpha subunit contains a covalently bound pyruvoyl group derived from serine that is essential for activity.


Pssm-ID: 460648  Cd Length: 107  Bit Score: 160.37  E-value: 4.60e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228748666   8 HCILELFECPSELLDDEQFICRAINSAAEASGSTLLTLSSHKFSPQGVTALGLLAESHISIHTWPETGYAAVDAFTCGTH 87
Cdd:pfam02675   1 HLIVDLYGCDPELLDDAELIEQALREAAEAAGATVVEVVFHKFEPQGVSGVVLLAESHISIHTWPEYGYAAVDVFTCGDH 80

                          90       100
                  ....*....|....*....|....*..
gi 2228748666  88 CDPVAACRLLTGLLEAKRQARTVLQRG 114
Cdd:pfam02675  81 VDPEKAFEYLKEALGAKRVSVRELDRG 107
SpeD COG1586
S-adenosylmethionine decarboxylase [Amino acid transport and metabolism];
6-118 2.00e-50

S-adenosylmethionine decarboxylase [Amino acid transport and metabolism];


Pssm-ID: 441194  Cd Length: 118  Bit Score: 156.52  E-value: 2.00e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228748666   6 GKHCILELFECPSELLDDEQFICRAINSAAEASGSTLLTLSSHKFSPQGVTALGLLAESHISIHTWPETGYAAVDAFTCG 85
Cdd:COG1586     4 GKHLIADLYGCDPELLNDAERLEEILVEAAEAAGATVLGVAFHKFEPQGVSGVVLLAESHISIHTWPEYGYAAVDVFTCG 83

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2228748666  86 THCDPVAACRLLTGLLEAKRQARTVLQRGRGVP 118
Cdd:COG1586    84 DDIDPEKALEYLKEAFGADKVEVTELKRGFTRD 116
SAM_DCase_Bsu TIGR03330
S-adenosylmethionine decarboxylase proenzyme, Bacillus form; Members of this protein family ...
 4-114 3.19e-50

S-adenosylmethionine decarboxylase proenzyme, Bacillus form; Members of this protein family are the single chain precursor of the two chains of the mature S-adenosylmethionine decarboxylase as found in Methanocaldococcus jannaschii, Bacillus subtilis, and a wide range of other species. It differs substantially in architecture from the form as found in Escherichia coli, and lacks any extended homology to the eukaryotic form (TIGR00535). [Central intermediary metabolism, Polyamine biosynthesis]


Pssm-ID: 274523  Cd Length: 112  Bit Score: 155.84  E-value: 3.19e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228748666   4 TTGKHCILELFECPSELLDDEQFICRAINSAAEASGSTLLTLSSHKFSPQGVTALGLLAESHISIHTWPETGYAAVDAFT 83
Cdd:TIGR03330   2 TLGRHLIVDLYGCDPEKLDDVEFIEEILLEAAKVAGATLVASHFHKFSPGGVSGVVLLAESHISIHTWPEYGYAAVDVFT 81

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2228748666  84 CGTHCDPVAACRLLTGLLEAKRQARTVLQRG 114
Cdd:TIGR03330  82 CGDHSDPEKAFEYLVEALKPKRVEVRELDRG 112
 
Name Accession Description Interval E-value
AdoMet_dc pfam02675
S-adenosylmethionine decarboxylase; This family contains several S-adenosylmethionine ...
 8-114 4.60e-52

S-adenosylmethionine decarboxylase; This family contains several S-adenosylmethionine decarboxylase proteins from bacterial and archaebacterial species. S-adenosylmethionine decarboxylase (AdoMetDC), a key enzyme in the biosynthesis of spermidine and spermine, is first synthesized as a proenzyme, which is cleaved post translationally to form alpha and beta subunits. The alpha subunit contains a covalently bound pyruvoyl group derived from serine that is essential for activity.


Pssm-ID: 460648  Cd Length: 107  Bit Score: 160.37  E-value: 4.60e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228748666   8 HCILELFECPSELLDDEQFICRAINSAAEASGSTLLTLSSHKFSPQGVTALGLLAESHISIHTWPETGYAAVDAFTCGTH 87
Cdd:pfam02675   1 HLIVDLYGCDPELLDDAELIEQALREAAEAAGATVVEVVFHKFEPQGVSGVVLLAESHISIHTWPEYGYAAVDVFTCGDH 80

                          90       100
                  ....*....|....*....|....*..
gi 2228748666  88 CDPVAACRLLTGLLEAKRQARTVLQRG 114
Cdd:pfam02675  81 VDPEKAFEYLKEALGAKRVSVRELDRG 107
SpeD COG1586
S-adenosylmethionine decarboxylase [Amino acid transport and metabolism];
6-118 2.00e-50

S-adenosylmethionine decarboxylase [Amino acid transport and metabolism];


Pssm-ID: 441194  Cd Length: 118  Bit Score: 156.52  E-value: 2.00e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228748666   6 GKHCILELFECPSELLDDEQFICRAINSAAEASGSTLLTLSSHKFSPQGVTALGLLAESHISIHTWPETGYAAVDAFTCG 85
Cdd:COG1586     4 GKHLIADLYGCDPELLNDAERLEEILVEAAEAAGATVLGVAFHKFEPQGVSGVVLLAESHISIHTWPEYGYAAVDVFTCG 83

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2228748666  86 THCDPVAACRLLTGLLEAKRQARTVLQRGRGVP 118
Cdd:COG1586    84 DDIDPEKALEYLKEAFGADKVEVTELKRGFTRD 116
SAM_DCase_Bsu TIGR03330
S-adenosylmethionine decarboxylase proenzyme, Bacillus form; Members of this protein family ...
 4-114 3.19e-50

S-adenosylmethionine decarboxylase proenzyme, Bacillus form; Members of this protein family are the single chain precursor of the two chains of the mature S-adenosylmethionine decarboxylase as found in Methanocaldococcus jannaschii, Bacillus subtilis, and a wide range of other species. It differs substantially in architecture from the form as found in Escherichia coli, and lacks any extended homology to the eukaryotic form (TIGR00535). [Central intermediary metabolism, Polyamine biosynthesis]


Pssm-ID: 274523  Cd Length: 112  Bit Score: 155.84  E-value: 3.19e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2228748666   4 TTGKHCILELFECPSELLDDEQFICRAINSAAEASGSTLLTLSSHKFSPQGVTALGLLAESHISIHTWPETGYAAVDAFT 83
Cdd:TIGR03330   2 TLGRHLIVDLYGCDPEKLDDVEFIEEILLEAAKVAGATLVASHFHKFSPGGVSGVVLLAESHISIHTWPEYGYAAVDVFT 81

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2228748666  84 CGTHCDPVAACRLLTGLLEAKRQARTVLQRG 114
Cdd:TIGR03330  82 CGDHSDPEKAFEYLVEALKPKRVEVRELDRG 112
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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