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Conserved domains on  [gi|442624848|ref|NP_001259791|]
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S-adenosylmethionine synthetase, isoform L [Drosophila melanogaster]

Protein Classification

S-adenosylmethionine synthetase N-terminal domain-containing protein( domain architecture ID 10450534)

S-adenosylmethionine synthetase (MAT) N-terminal domain-containing protein; MAT catalyzes the two-step reaction which synthesizes S-adenosylmethionine (SAM or AdoMet), pyrophosphate (PPi), and orthophosphate (Pi) from ATP and L-methionine

Gene Ontology:  GO:0006556
PubMed:  8611562

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
S-AdoMet_synt_N pfam00438
S-adenosylmethionine synthetase, N-terminal domain; The three domains of S-adenosylmethionine ...
 28-111 7.16e-60

S-adenosylmethionine synthetase, N-terminal domain; The three domains of S-adenosylmethionine synthetase have the same alpha+beta fold.


:

Pssm-ID: 459810 [Multi-domain]  Cd Length: 98  Bit Score: 179.47  E-value: 7.16e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624848   28 TFLFTSESVGEGHPDKMCDQISDAILDAHLKQDPNAKVACETVAKTGMILLCGEITSKAVVDYQKVVRETVQHIGYDDSS 107
Cdd:pfam00438   1 KYLFTSESVTEGHPDKVCDQISDAILDAFLAQDPNSRVACETLVTTGLVVVAGEITTKAYVDIEKIVRDTIKEIGYDDAE 80


                  ....
gi 442624848  108 KGYH 111
Cdd:pfam00438  81 YGFD 84
 
Name Accession Description Interval E-value
S-AdoMet_synt_N pfam00438
S-adenosylmethionine synthetase, N-terminal domain; The three domains of S-adenosylmethionine ...
 28-111 7.16e-60

S-adenosylmethionine synthetase, N-terminal domain; The three domains of S-adenosylmethionine synthetase have the same alpha+beta fold.


Pssm-ID: 459810 [Multi-domain]  Cd Length: 98  Bit Score: 179.47  E-value: 7.16e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624848   28 TFLFTSESVGEGHPDKMCDQISDAILDAHLKQDPNAKVACETVAKTGMILLCGEITSKAVVDYQKVVRETVQHIGYDDSS 107
Cdd:pfam00438   1 KYLFTSESVTEGHPDKVCDQISDAILDAFLAQDPNSRVACETLVTTGLVVVAGEITTKAYVDIEKIVRDTIKEIGYDDAE 80


                  ....
gi 442624848  108 KGYH 111
Cdd:pfam00438  81 YGFD 84
S-AdoMet_synt cd18079
S-adenosylmethionine synthetase; S-adenosylmethionine synthetase (EC 2.5.1.6), also known as ...
 30-111 3.05e-56

S-adenosylmethionine synthetase; S-adenosylmethionine synthetase (EC 2.5.1.6), also known as methionine adenosyltransferase, catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP in two steps, the formation of AdoMet and hydrolysis of the tripolyphosphate, which occurs prior to release of the product from the enzyme, which consists of three structural domains that have a similar alpha+beta fold.


Pssm-ID: 350837  Cd Length: 371  Bit Score: 179.14  E-value: 3.05e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624848  30 LFTSESVGEGHPDKMCDQISDAILDAHLKQDPNAKVACETVAKTGMILLCGEITSKAVVDYQKVVRETVQHIGYDDSSKG 109
Cdd:cd18079    1 LFTSESVTEGHPDKICDQISDAILDACLAQDPNSRVACETLVTTGLVIIAGEITTKAYVDIEKIVREVIKEIGYDDSDFG 80


                 ..
gi 442624848 110 YH 111
Cdd:cd18079   81 FD 82
PTZ00104 PTZ00104
S-adenosylmethionine synthase; Provisional
 28-109 1.28e-53

S-adenosylmethionine synthase; Provisional


Pssm-ID: 240268  Cd Length: 398  Bit Score: 173.28  E-value: 1.28e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624848  28 TFLFTSESVGEGHPDKMCDQISDAILDAHLKQDPNAKVACETVAKTGMILLCGEITSKAVVDYQKVVRETVQHIGYDDSS 107
Cdd:PTZ00104  10 HFLFTSESVSEGHPDKLCDQISDAVLDACLAQDPLSKVACETCAKTGMVMVFGEITTKAVVDYQKVVRDTVKEIGYDDTE 89


                 ..
gi 442624848 108 KG 109
Cdd:PTZ00104  90 KG 91
MetK COG0192
S-adenosylmethionine synthetase [Coenzyme transport and metabolism]; S-adenosylmethionine ...
 29-111 5.35e-53

S-adenosylmethionine synthetase [Coenzyme transport and metabolism]; S-adenosylmethionine synthetase is part of the Pathway/BioSystem: Methionine biosynthesis


Pssm-ID: 439962 [Multi-domain]  Cd Length: 384  Bit Score: 171.36  E-value: 5.35e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624848  29 FLFTSESVGEGHPDKMCDQISDAILDAHLKQDPNAKVACETVAKTGMILLCGEITSKAVVDYQKVVRETVQHIGYDDSSK 108
Cdd:COG0192    2 YLFTSESVTEGHPDKVCDQISDAILDAILAQDPNARVACETLVTTGLVVVAGEITTSAYVDIPEIVRETIKEIGYTSSEY 81


                 ...
gi 442624848 109 GYH 111
Cdd:COG0192   82 GFD 84
metK TIGR01034
S-adenosylmethionine synthetase; Tandem isozymes of this S-adenosylmethionine synthetase in E. ...
 30-110 1.60e-48

S-adenosylmethionine synthetase; Tandem isozymes of this S-adenosylmethionine synthetase in E. coli are designated MetK and MetX. [Central intermediary metabolism, Other]


Pssm-ID: 273406  Cd Length: 377  Bit Score: 159.45  E-value: 1.60e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624848   30 LFTSESVGEGHPDKMCDQISDAILDAHLKQDPNAKVACETVAKTGMILLCGEITSKAVVDYQKVVRETVQHIGYDDSSKG 109
Cdd:TIGR01034   1 LFTSESVSEGHPDKIADQISDAVLDAILKQDPKSKVACETFVKTGLVLIGGEITTSAYVDIQEVARNTIKDIGYTDSDYG 80


                  .
gi 442624848  110 Y 110
Cdd:TIGR01034  81 F 81
 
Name Accession Description Interval E-value
S-AdoMet_synt_N pfam00438
S-adenosylmethionine synthetase, N-terminal domain; The three domains of S-adenosylmethionine ...
 28-111 7.16e-60

S-adenosylmethionine synthetase, N-terminal domain; The three domains of S-adenosylmethionine synthetase have the same alpha+beta fold.


Pssm-ID: 459810 [Multi-domain]  Cd Length: 98  Bit Score: 179.47  E-value: 7.16e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624848   28 TFLFTSESVGEGHPDKMCDQISDAILDAHLKQDPNAKVACETVAKTGMILLCGEITSKAVVDYQKVVRETVQHIGYDDSS 107
Cdd:pfam00438   1 KYLFTSESVTEGHPDKVCDQISDAILDAFLAQDPNSRVACETLVTTGLVVVAGEITTKAYVDIEKIVRDTIKEIGYDDAE 80


                  ....
gi 442624848  108 KGYH 111
Cdd:pfam00438  81 YGFD 84
S-AdoMet_synt cd18079
S-adenosylmethionine synthetase; S-adenosylmethionine synthetase (EC 2.5.1.6), also known as ...
 30-111 3.05e-56

S-adenosylmethionine synthetase; S-adenosylmethionine synthetase (EC 2.5.1.6), also known as methionine adenosyltransferase, catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP in two steps, the formation of AdoMet and hydrolysis of the tripolyphosphate, which occurs prior to release of the product from the enzyme, which consists of three structural domains that have a similar alpha+beta fold.


Pssm-ID: 350837  Cd Length: 371  Bit Score: 179.14  E-value: 3.05e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624848  30 LFTSESVGEGHPDKMCDQISDAILDAHLKQDPNAKVACETVAKTGMILLCGEITSKAVVDYQKVVRETVQHIGYDDSSKG 109
Cdd:cd18079    1 LFTSESVTEGHPDKICDQISDAILDACLAQDPNSRVACETLVTTGLVIIAGEITTKAYVDIEKIVREVIKEIGYDDSDFG 80


                 ..
gi 442624848 110 YH 111
Cdd:cd18079   81 FD 82
PTZ00104 PTZ00104
S-adenosylmethionine synthase; Provisional
 28-109 1.28e-53

S-adenosylmethionine synthase; Provisional


Pssm-ID: 240268  Cd Length: 398  Bit Score: 173.28  E-value: 1.28e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624848  28 TFLFTSESVGEGHPDKMCDQISDAILDAHLKQDPNAKVACETVAKTGMILLCGEITSKAVVDYQKVVRETVQHIGYDDSS 107
Cdd:PTZ00104  10 HFLFTSESVSEGHPDKLCDQISDAVLDACLAQDPLSKVACETCAKTGMVMVFGEITTKAVVDYQKVVRDTVKEIGYDDTE 89


                 ..
gi 442624848 108 KG 109
Cdd:PTZ00104  90 KG 91
MetK COG0192
S-adenosylmethionine synthetase [Coenzyme transport and metabolism]; S-adenosylmethionine ...
 29-111 5.35e-53

S-adenosylmethionine synthetase [Coenzyme transport and metabolism]; S-adenosylmethionine synthetase is part of the Pathway/BioSystem: Methionine biosynthesis


Pssm-ID: 439962 [Multi-domain]  Cd Length: 384  Bit Score: 171.36  E-value: 5.35e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624848  29 FLFTSESVGEGHPDKMCDQISDAILDAHLKQDPNAKVACETVAKTGMILLCGEITSKAVVDYQKVVRETVQHIGYDDSSK 108
Cdd:COG0192    2 YLFTSESVTEGHPDKVCDQISDAILDAILAQDPNARVACETLVTTGLVVVAGEITTSAYVDIPEIVRETIKEIGYTSSEY 81


                 ...
gi 442624848 109 GYH 111
Cdd:COG0192   82 GFD 84
metK TIGR01034
S-adenosylmethionine synthetase; Tandem isozymes of this S-adenosylmethionine synthetase in E. ...
 30-110 1.60e-48

S-adenosylmethionine synthetase; Tandem isozymes of this S-adenosylmethionine synthetase in E. coli are designated MetK and MetX. [Central intermediary metabolism, Other]


Pssm-ID: 273406  Cd Length: 377  Bit Score: 159.45  E-value: 1.60e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624848   30 LFTSESVGEGHPDKMCDQISDAILDAHLKQDPNAKVACETVAKTGMILLCGEITSKAVVDYQKVVRETVQHIGYDDSSKG 109
Cdd:TIGR01034   1 LFTSESVSEGHPDKIADQISDAVLDAILKQDPKSKVACETFVKTGLVLIGGEITTSAYVDIQEVARNTIKDIGYTDSDYG 80


                  .
gi 442624848  110 Y 110
Cdd:TIGR01034  81 F 81
PLN02243 PLN02243
S-adenosylmethionine synthase
 28-109 1.64e-41

S-adenosylmethionine synthase


Pssm-ID: 177886 [Multi-domain]  Cd Length: 386  Bit Score: 141.50  E-value: 1.64e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442624848  28 TFLFTSESVGEGHPDKMCDQISDAILDAHLKQDPNAKVACETVAKTGMILLCGEITSKAVVDYQKVVRETVQHIGYDDSS 107
Cdd:PLN02243   3 TFLFTSESVNEGHPDKLCDQISDAVLDACLAQDPDSKVACETCTKTNMVMVFGEITTKAKVDYEKIVRDTCREIGFVSDD 82


                 ..
gi 442624848 108 KG 109
Cdd:PLN02243  83 VG 84
 
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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