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Conserved domains on  [gi|2538877491|ref|WP_295158837|]
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adenosylmethionine decarboxylase [Selenomonas sp. AE3005]

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
SCOP:  3001051

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SpeD COG1586
S-adenosylmethionine decarboxylase [Amino acid transport and metabolism];
2-119 6.59e-31

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


:

Pssm-ID: 441194  Cd Length: 118  Bit Score: 107.60  E-value: 6.59e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538877491   2 KILARHLTADLFNCQNHQLNDNELIKDMLVNLIQKFEMQLIRlsmealDSSH-------TVyMAVLGQGHITMHVYPELK 74
Cdd:COG1586     1 KFLGKHLIADLYGCDPELLNDAERLEEILVEAAEAAGATVLG------VAFHkfepqgvSG-VVLLAESHISIHTWPEYG 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2538877491  75 YVSLDIFLCQENAEPDKLGQAVRNYFKPDKTKTTVLKRGDFGTAK 119
Cdd:COG1586    74 YAAVDVFTCGDDIDPEKALEYLKEAFGADKVEVTELKRGFTRDIK 118
 
Name Accession Description Interval E-value
SpeD COG1586
S-adenosylmethionine decarboxylase [Amino acid transport and metabolism];
2-119 6.59e-31

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


Pssm-ID: 441194  Cd Length: 118  Bit Score: 107.60  E-value: 6.59e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538877491   2 KILARHLTADLFNCQNHQLNDNELIKDMLVNLIQKFEMQLIRlsmealDSSH-------TVyMAVLGQGHITMHVYPELK 74
Cdd:COG1586     1 KFLGKHLIADLYGCDPELLNDAERLEEILVEAAEAAGATVLG------VAFHkfepqgvSG-VVLLAESHISIHTWPEYG 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2538877491  75 YVSLDIFLCQENAEPDKLGQAVRNYFKPDKTKTTVLKRGDFGTAK 119
Cdd:COG1586    74 YAAVDVFTCGDDIDPEKALEYLKEAFGADKVEVTELKRGFTRDIK 118
AdoMet_dc pfam02675
S-adenosylmethionine decarboxylase; This family contains several S-adenosylmethionine ...
 7-113 2.32e-24

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: 90.27  E-value: 2.32e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538877491   7 HLTADLFNCQNHQLNDNELIKDMLVNLIQKFEMQLIRlsmealDSSH-------TVyMAVLGQGHITMHVYPELKYVSLD 79
Cdd:pfam02675   1 HLIVDLYGCDPELLDDAELIEQALREAAEAAGATVVE------VVFHkfepqgvSG-VVLLAESHISIHTWPEYGYAAVD 73

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2538877491  80 IFLCQENAEPDKLGQAVRNYFKPDKTKTTVLKRG 113
Cdd:pfam02675  74 VFTCGDHVDPEKAFEYLKEALGAKRVSVRELDRG 107
SAM_DCase_Bsu TIGR03330
S-adenosylmethionine decarboxylase proenzyme, Bacillus form; Members of this protein family ...
 2-113 5.49e-18

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: 74.18  E-value: 5.49e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538877491   2 KILARHLTADLFNCQNHQLNDNELIKDMLVNLIQKFEMQLIrlsmealdSSHTVY--------MAVLGQGHITMHVYPEL 73
Cdd:TIGR03330   1 KTLGRHLIVDLYGCDPEKLDDVEFIEEILLEAAKVAGATLV--------ASHFHKfspggvsgVVLLAESHISIHTWPEY 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2538877491  74 KYVSLDIFLCQENAEPDKLGQAVRNYFKPDKTKTTVLKRG 113
Cdd:TIGR03330  73 GYAAVDVFTCGDHSDPEKAFEYLVEALKPKRVEVRELDRG 112
 
Name Accession Description Interval E-value
SpeD COG1586
S-adenosylmethionine decarboxylase [Amino acid transport and metabolism];
2-119 6.59e-31

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


Pssm-ID: 441194  Cd Length: 118  Bit Score: 107.60  E-value: 6.59e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538877491   2 KILARHLTADLFNCQNHQLNDNELIKDMLVNLIQKFEMQLIRlsmealDSSH-------TVyMAVLGQGHITMHVYPELK 74
Cdd:COG1586     1 KFLGKHLIADLYGCDPELLNDAERLEEILVEAAEAAGATVLG------VAFHkfepqgvSG-VVLLAESHISIHTWPEYG 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2538877491  75 YVSLDIFLCQENAEPDKLGQAVRNYFKPDKTKTTVLKRGDFGTAK 119
Cdd:COG1586    74 YAAVDVFTCGDDIDPEKALEYLKEAFGADKVEVTELKRGFTRDIK 118
AdoMet_dc pfam02675
S-adenosylmethionine decarboxylase; This family contains several S-adenosylmethionine ...
 7-113 2.32e-24

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: 90.27  E-value: 2.32e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538877491   7 HLTADLFNCQNHQLNDNELIKDMLVNLIQKFEMQLIRlsmealDSSH-------TVyMAVLGQGHITMHVYPELKYVSLD 79
Cdd:pfam02675   1 HLIVDLYGCDPELLDDAELIEQALREAAEAAGATVVE------VVFHkfepqgvSG-VVLLAESHISIHTWPEYGYAAVD 73

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2538877491  80 IFLCQENAEPDKLGQAVRNYFKPDKTKTTVLKRG 113
Cdd:pfam02675  74 VFTCGDHVDPEKAFEYLKEALGAKRVSVRELDRG 107
SAM_DCase_Bsu TIGR03330
S-adenosylmethionine decarboxylase proenzyme, Bacillus form; Members of this protein family ...
 2-113 5.49e-18

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: 74.18  E-value: 5.49e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2538877491   2 KILARHLTADLFNCQNHQLNDNELIKDMLVNLIQKFEMQLIrlsmealdSSHTVY--------MAVLGQGHITMHVYPEL 73
Cdd:TIGR03330   1 KTLGRHLIVDLYGCDPEKLDDVEFIEEILLEAAKVAGATLV--------ASHFHKfspggvsgVVLLAESHISIHTWPEY 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2538877491  74 KYVSLDIFLCQENAEPDKLGQAVRNYFKPDKTKTTVLKRG 113
Cdd:TIGR03330  73 GYAAVDVFTCGDHSDPEKAFEYLVEALKPKRVEVRELDRG 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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