NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|950269995|ref|WP_057306176|]
View 

MULTISPECIES: adenosylmethionine decarboxylase [Paenibacillus]

Protein Classification

S-adenosylmethionine decarboxylase family protein( domain architecture ID 10003985)

S-adenosylmethionine decarboxylase (AdoMetDC) family protein similar to AdoMetDC that catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet)and its paralog, arginine decarboxylase that catalyzes the decarboxylation of L-arginine to agmatine

CATH:  3.60.90.10
EC:  4.1.1.-
Gene Ontology:  GO:0006596|GO:0016831

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
SpeD COG1586
S-adenosylmethionine decarboxylase [Amino acid transport and metabolism];
7-120 1.22e-54

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


:

Pssm-ID: 441194  Cd Length: 118  Bit Score: 166.92  E-value: 1.22e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950269995   7 TFGRHVAVDTWGVDFELLNNADWLQAQMVEAAEVCGATVLSVQSKQFEPQGATVLVMLSESHLSIHTYPERGFAALDCYT 86
Cdd:COG1586    2 FLGKHLIADLYGCDPELLNDAERLEEILVEAAEAAGATVLGVAFHKFEPQGVSGVVLLAESHISIHTWPEYGYAAVDVFT 81

                         90       100       110
                 ....*....|....*....|....*....|....
gi 950269995  87 CGETVDPQLAIDFMVSVLKPETFYAKKLVRGMGE 120
Cdd:COG1586   82 CGDDIDPEKALEYLKEAFGADKVEVTELKRGFTR 115
 
Name Accession Description Interval E-value
SpeD COG1586
S-adenosylmethionine decarboxylase [Amino acid transport and metabolism];
7-120 1.22e-54

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


Pssm-ID: 441194  Cd Length: 118  Bit Score: 166.92  E-value: 1.22e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950269995   7 TFGRHVAVDTWGVDFELLNNADWLQAQMVEAAEVCGATVLSVQSKQFEPQGATVLVMLSESHLSIHTYPERGFAALDCYT 86
Cdd:COG1586    2 FLGKHLIADLYGCDPELLNDAERLEEILVEAAEAAGATVLGVAFHKFEPQGVSGVVLLAESHISIHTWPEYGYAAVDVFT 81

                         90       100       110
                 ....*....|....*....|....*....|....
gi 950269995  87 CGETVDPQLAIDFMVSVLKPETFYAKKLVRGMGE 120
Cdd:COG1586   82 CGDDIDPEKALEYLKEAFGADKVEVTELKRGFTR 115
SAM_DCase_Bsu TIGR03330
S-adenosylmethionine decarboxylase proenzyme, Bacillus form; Members of this protein family ...
 6-117 1.63e-51

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: 158.92  E-value: 1.63e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950269995    6 STFGRHVAVDTWGVDFELLNNADWLQAQMVEAAEVCGATVLSVQSKQFEPQGATVLVMLSESHLSIHTYPERGFAALDCY 85
Cdd:TIGR03330   1 KTLGRHLIVDLYGCDPEKLDDVEFIEEILLEAAKVAGATLVASHFHKFSPGGVSGVVLLAESHISIHTWPEYGYAAVDVF 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 950269995   86 TCGETVDPQLAIDFMVSVLKPETFYAKKLVRG 117
Cdd:TIGR03330  81 TCGDHSDPEKAFEYLVEALKPKRVEVRELDRG 112
AdoMet_dc pfam02675
S-adenosylmethionine decarboxylase; This family contains several S-adenosylmethionine ...
 11-117 1.09e-49

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: 154.21  E-value: 1.09e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950269995   11 HVAVDTWGVDFELLNNADWLQAQMVEAAEVCGATVLSVQSKQFEPQGATVLVMLSESHLSIHTYPERGFAALDCYTCGET 90
Cdd:pfam02675   1 HLIVDLYGCDPELLDDAELIEQALREAAEAAGATVVEVVFHKFEPQGVSGVVLLAESHISIHTWPEYGYAAVDVFTCGDH 80

                          90       100
                  ....*....|....*....|....*..
gi 950269995   91 VDPQLAIDFMVSVLKPETFYAKKLVRG 117
Cdd:pfam02675  81 VDPEKAFEYLKEALGAKRVSVRELDRG 107
PRK05462 PRK05462
adenosylmethionine decarboxylase;
26-118 6.58e-10

adenosylmethionine decarboxylase;


Pssm-ID: 235480  Cd Length: 266  Bit Score: 54.90  E-value: 6.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950269995  26 NADWLQAQMVEAAEVCGATVLSVQSKQFEPQGATVLVMLSE---------------------------SHLSIHTYPE-- 76
Cdd:PRK05462  46 NAERLTEILTEVCSIIGANILNIARQDYEPQGASVTILISEepvdpklidksehpgplpetvvahldkSHITVHTYPEsh 125

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 950269995  77 --RG---FAA-LDCYTCGEtVDPQLAIDFMVSVLKPETFYAKKLVRGM 118
Cdd:PRK05462 126 peGGictFRAdIDVSTCGV-ISPLKALNYLIHSFESDIVTIDYRVRGF 172
 
Name Accession Description Interval E-value
SpeD COG1586
S-adenosylmethionine decarboxylase [Amino acid transport and metabolism];
7-120 1.22e-54

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


Pssm-ID: 441194  Cd Length: 118  Bit Score: 166.92  E-value: 1.22e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950269995   7 TFGRHVAVDTWGVDFELLNNADWLQAQMVEAAEVCGATVLSVQSKQFEPQGATVLVMLSESHLSIHTYPERGFAALDCYT 86
Cdd:COG1586    2 FLGKHLIADLYGCDPELLNDAERLEEILVEAAEAAGATVLGVAFHKFEPQGVSGVVLLAESHISIHTWPEYGYAAVDVFT 81

                         90       100       110
                 ....*....|....*....|....*....|....
gi 950269995  87 CGETVDPQLAIDFMVSVLKPETFYAKKLVRGMGE 120
Cdd:COG1586   82 CGDDIDPEKALEYLKEAFGADKVEVTELKRGFTR 115
SAM_DCase_Bsu TIGR03330
S-adenosylmethionine decarboxylase proenzyme, Bacillus form; Members of this protein family ...
 6-117 1.63e-51

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: 158.92  E-value: 1.63e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950269995    6 STFGRHVAVDTWGVDFELLNNADWLQAQMVEAAEVCGATVLSVQSKQFEPQGATVLVMLSESHLSIHTYPERGFAALDCY 85
Cdd:TIGR03330   1 KTLGRHLIVDLYGCDPEKLDDVEFIEEILLEAAKVAGATLVASHFHKFSPGGVSGVVLLAESHISIHTWPEYGYAAVDVF 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 950269995   86 TCGETVDPQLAIDFMVSVLKPETFYAKKLVRG 117
Cdd:TIGR03330  81 TCGDHSDPEKAFEYLVEALKPKRVEVRELDRG 112
AdoMet_dc pfam02675
S-adenosylmethionine decarboxylase; This family contains several S-adenosylmethionine ...
 11-117 1.09e-49

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: 154.21  E-value: 1.09e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950269995   11 HVAVDTWGVDFELLNNADWLQAQMVEAAEVCGATVLSVQSKQFEPQGATVLVMLSESHLSIHTYPERGFAALDCYTCGET 90
Cdd:pfam02675   1 HLIVDLYGCDPELLDDAELIEQALREAAEAAGATVVEVVFHKFEPQGVSGVVLLAESHISIHTWPEYGYAAVDVFTCGDH 80

                          90       100
                  ....*....|....*....|....*..
gi 950269995   91 VDPQLAIDFMVSVLKPETFYAKKLVRG 117
Cdd:pfam02675  81 VDPEKAFEYLKEALGAKRVSVRELDRG 107
PRK05462 PRK05462
adenosylmethionine decarboxylase;
26-118 6.58e-10

adenosylmethionine decarboxylase;


Pssm-ID: 235480  Cd Length: 266  Bit Score: 54.90  E-value: 6.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 950269995  26 NADWLQAQMVEAAEVCGATVLSVQSKQFEPQGATVLVMLSE---------------------------SHLSIHTYPE-- 76
Cdd:PRK05462  46 NAERLTEILTEVCSIIGANILNIARQDYEPQGASVTILISEepvdpklidksehpgplpetvvahldkSHITVHTYPEsh 125

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 950269995  77 --RG---FAA-LDCYTCGEtVDPQLAIDFMVSVLKPETFYAKKLVRGM 118
Cdd:PRK05462 126 peGGictFRAdIDVSTCGV-ISPLKALNYLIHSFESDIVTIDYRVRGF 172
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH