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Conserved domains on  [gi|1266702897|gb|PHF80427|]
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adenosylmethionine decarboxylase [Bacillus toyonensis]

Protein Classification

S-adenosylmethionine decarboxylase( domain architecture ID 1904481)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK05462 super family cl42185
adenosylmethionine decarboxylase;
4-115 1.60e-52

adenosylmethionine decarboxylase;


The actual alignment was detected with superfamily member TIGR03330:

Pssm-ID: 478009  Cd Length: 112  Bit Score: 160.85  E-value: 1.60e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266702897   4 STFGKHIIVDLWGVDFSLLDDIHFLERHLVVAADHSGAHVLNVSTKEFHPYGVTVLVLLSESHLSIHTYPEKNFAAIDCY 83
Cdd:TIGR03330   1 KTLGRHLIVDLYGCDPEKLDDVEFIEEILLEAAKVAGATLVASHFHKFSPGGVSGVVLLAESHISIHTWPEYGYAAVDVF 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1266702897  84 TCGTTVEPQMAIDYIVNILKPEQIQIKKLIRG 115
Cdd:TIGR03330  81 TCGDHSDPEKAFEYLVEALKPKRVEVRELDRG 112
 
Name Accession Description Interval E-value
SAM_DCase_Bsu TIGR03330
S-adenosylmethionine decarboxylase proenzyme, Bacillus form; Members of this protein family ...
 4-115 1.60e-52

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: 160.85  E-value: 1.60e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266702897   4 STFGKHIIVDLWGVDFSLLDDIHFLERHLVVAADHSGAHVLNVSTKEFHPYGVTVLVLLSESHLSIHTYPEKNFAAIDCY 83
Cdd:TIGR03330   1 KTLGRHLIVDLYGCDPEKLDDVEFIEEILLEAAKVAGATLVASHFHKFSPGGVSGVVLLAESHISIHTWPEYGYAAVDVF 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1266702897  84 TCGTTVEPQMAIDYIVNILKPEQIQIKKLIRG 115
Cdd:TIGR03330  81 TCGDHSDPEKAFEYLVEALKPKRVEVRELDRG 112
SpeD COG1586
S-adenosylmethionine decarboxylase [Amino acid transport and metabolism];
5-118 1.77e-50

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


Pssm-ID: 441194  Cd Length: 118  Bit Score: 155.75  E-value: 1.77e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266702897   5 TFGKHIIVDLWGVDFSLLDDIHFLERHLVVAADHSGAHVLNVSTKEFHPYGVTVLVLLSESHLSIHTYPEKNFAAIDCYT 84
Cdd:COG1586     2 FLGKHLIADLYGCDPELLNDAERLEEILVEAAEAAGATVLGVAFHKFEPQGVSGVVLLAESHISIHTWPEYGYAAVDVFT 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1266702897  85 CGTTVEPQMAIDYIVNILKPEQIQIKKLIRGIGE 118
Cdd:COG1586    82 CGDDIDPEKALEYLKEAFGADKVEVTELKRGFTR 115
AdoMet_dc pfam02675
S-adenosylmethionine decarboxylase; This family contains several S-adenosylmethionine ...
 9-115 1.26e-45

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: 143.42  E-value: 1.26e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266702897   9 HIIVDLWGVDFSLLDDIHFLERHLVVAADHSGAHVLNVSTKEFHPYGVTVLVLLSESHLSIHTYPEKNFAAIDCYTCGTT 88
Cdd:pfam02675   1 HLIVDLYGCDPELLDDAELIEQALREAAEAAGATVVEVVFHKFEPQGVSGVVLLAESHISIHTWPEYGYAAVDVFTCGDH 80

                          90       100
                  ....*....|....*....|....*..
gi 1266702897  89 VEPQMAIDYIVNILKPEQIQIKKLIRG 115
Cdd:pfam02675  81 VDPEKAFEYLKEALGAKRVSVRELDRG 107
PRK05462 PRK05462
adenosylmethionine decarboxylase;
40-115 5.42e-07

adenosylmethionine decarboxylase;


Pssm-ID: 235480  Cd Length: 266  Bit Score: 46.42  E-value: 5.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266702897  40 GAHVLNVSTKEFHPYGVTVLVLLSE---------------------------SHLSIHTYPEKN-------FAA-IDCYT 84
Cdd:PRK05462   62 GANILNIARQDYEPQGASVTILISEepvdpklidksehpgplpetvvahldkSHITVHTYPESHpeggictFRAdIDVST 141

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1266702897  85 CGtTVEPQMAIDYIVNILKPEQIQIKKLIRG 115
Cdd:PRK05462  142 CG-VISPLKALNYLIHSFESDIVTIDYRVRG 171
 
Name Accession Description Interval E-value
SAM_DCase_Bsu TIGR03330
S-adenosylmethionine decarboxylase proenzyme, Bacillus form; Members of this protein family ...
 4-115 1.60e-52

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: 160.85  E-value: 1.60e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266702897   4 STFGKHIIVDLWGVDFSLLDDIHFLERHLVVAADHSGAHVLNVSTKEFHPYGVTVLVLLSESHLSIHTYPEKNFAAIDCY 83
Cdd:TIGR03330   1 KTLGRHLIVDLYGCDPEKLDDVEFIEEILLEAAKVAGATLVASHFHKFSPGGVSGVVLLAESHISIHTWPEYGYAAVDVF 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1266702897  84 TCGTTVEPQMAIDYIVNILKPEQIQIKKLIRG 115
Cdd:TIGR03330  81 TCGDHSDPEKAFEYLVEALKPKRVEVRELDRG 112
SpeD COG1586
S-adenosylmethionine decarboxylase [Amino acid transport and metabolism];
5-118 1.77e-50

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


Pssm-ID: 441194  Cd Length: 118  Bit Score: 155.75  E-value: 1.77e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266702897   5 TFGKHIIVDLWGVDFSLLDDIHFLERHLVVAADHSGAHVLNVSTKEFHPYGVTVLVLLSESHLSIHTYPEKNFAAIDCYT 84
Cdd:COG1586     2 FLGKHLIADLYGCDPELLNDAERLEEILVEAAEAAGATVLGVAFHKFEPQGVSGVVLLAESHISIHTWPEYGYAAVDVFT 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1266702897  85 CGTTVEPQMAIDYIVNILKPEQIQIKKLIRGIGE 118
Cdd:COG1586    82 CGDDIDPEKALEYLKEAFGADKVEVTELKRGFTR 115
AdoMet_dc pfam02675
S-adenosylmethionine decarboxylase; This family contains several S-adenosylmethionine ...
 9-115 1.26e-45

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: 143.42  E-value: 1.26e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266702897   9 HIIVDLWGVDFSLLDDIHFLERHLVVAADHSGAHVLNVSTKEFHPYGVTVLVLLSESHLSIHTYPEKNFAAIDCYTCGTT 88
Cdd:pfam02675   1 HLIVDLYGCDPELLDDAELIEQALREAAEAAGATVVEVVFHKFEPQGVSGVVLLAESHISIHTWPEYGYAAVDVFTCGDH 80

                          90       100
                  ....*....|....*....|....*..
gi 1266702897  89 VEPQMAIDYIVNILKPEQIQIKKLIRG 115
Cdd:pfam02675  81 VDPEKAFEYLKEALGAKRVSVRELDRG 107
PRK05462 PRK05462
adenosylmethionine decarboxylase;
40-115 5.42e-07

adenosylmethionine decarboxylase;


Pssm-ID: 235480  Cd Length: 266  Bit Score: 46.42  E-value: 5.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266702897  40 GAHVLNVSTKEFHPYGVTVLVLLSE---------------------------SHLSIHTYPEKN-------FAA-IDCYT 84
Cdd:PRK05462   62 GANILNIARQDYEPQGASVTILISEepvdpklidksehpgplpetvvahldkSHITVHTYPESHpeggictFRAdIDVST 141

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1266702897  85 CGtTVEPQMAIDYIVNILKPEQIQIKKLIRG 115
Cdd:PRK05462  142 CG-VISPLKALNYLIHSFESDIVTIDYRVRG 171
 
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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