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Conserved domains on  [gi|281314353|gb|ADA60040|]
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unknown, partial [Lycium chilense]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AAT_I super family cl18945
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 1-39 2.94e-12

Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).


The actual alignment was detected with superfamily member PRK07550:

Pssm-ID: 450240 [Multi-domain]  Cd Length: 386  Bit Score: 57.66  E-value: 2.94e-12
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 281314353   1 GANQAFVNVALTLCDAGDSVVMFAPYYFNSYMSFQMTGV 39
Cdd:PRK07550  98 GCNQAFWAAMVTLAGAGDEVILPLPWYFNHKMWLDMLGI 136
 
Name Accession Description Interval E-value
PRK07550 PRK07550
aminotransferase;
1-39 2.94e-12

aminotransferase;


Pssm-ID: 181026 [Multi-domain]  Cd Length: 386  Bit Score: 57.66  E-value: 2.94e-12
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 281314353   1 GANQAFVNVALTLCDAGDSVVMFAPYYFNSYMSFQMTGV 39
Cdd:PRK07550  98 GCNQAFWAAMVTLAGAGDEVILPLPWYFNHKMWLDMLGI 136
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 1-39 1.21e-07

Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Pyridoxal phosphate combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. The major groups in this CD corresponds to Aspartate aminotransferase a, b and c, Tyrosine, Alanine, Aromatic-amino-acid, Glutamine phenylpyruvate, 1-Aminocyclopropane-1-carboxylate synthase, Histidinol-phosphate, gene products of malY and cobC, Valine-pyruvate aminotransferase and Rhizopine catabolism regulatory protein.


Pssm-ID: 99734 [Multi-domain]  Cd Length: 350  Bit Score: 44.64  E-value: 1.21e-07
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 281314353   1 GANQAFVNVALTLCDAGDSVVMFAPYYFNSYMSFQMTGV 39
Cdd:cd00609   67 GAQEALSLLLRALLNPGDEVLVPDPTYPGYEAAARLAGA 105
AspB COG0436
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ...
 1-38 2.54e-07

Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; Aspartate/methionine/tyrosine aminotransferase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


Pssm-ID: 440205 [Multi-domain]  Cd Length: 387  Bit Score: 43.58  E-value: 2.54e-07
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 281314353   1 GANQAFVNVALTLCDAGDSVVMFAPYYFNSYMSFQMTG 38
Cdd:COG0436   98 GAKEALALALLALLNPGDEVLVPDPGYPSYRAAVRLAG 135
 
Name Accession Description Interval E-value
PRK07550 PRK07550
aminotransferase;
1-39 2.94e-12

aminotransferase;


Pssm-ID: 181026 [Multi-domain]  Cd Length: 386  Bit Score: 57.66  E-value: 2.94e-12
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 281314353   1 GANQAFVNVALTLCDAGDSVVMFAPYYFNSYMSFQMTGV 39
Cdd:PRK07550  98 GCNQAFWAAMVTLAGAGDEVILPLPWYFNHKMWLDMLGI 136
PRK05957 PRK05957
pyridoxal phosphate-dependent aminotransferase;
1-38 7.24e-11

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 235654  Cd Length: 389  Bit Score: 53.92  E-value: 7.24e-11
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 281314353   1 GANQAFVNVALTLCDAGDSVVMFAPYYFNSYMSFQMTG 38
Cdd:PRK05957  97 GSNMAFMNAILAITDPGDEIILNTPYYFNHEMAITMAG 134
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 1-39 1.21e-07

Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Pyridoxal phosphate combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. The major groups in this CD corresponds to Aspartate aminotransferase a, b and c, Tyrosine, Alanine, Aromatic-amino-acid, Glutamine phenylpyruvate, 1-Aminocyclopropane-1-carboxylate synthase, Histidinol-phosphate, gene products of malY and cobC, Valine-pyruvate aminotransferase and Rhizopine catabolism regulatory protein.


Pssm-ID: 99734 [Multi-domain]  Cd Length: 350  Bit Score: 44.64  E-value: 1.21e-07
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 281314353   1 GANQAFVNVALTLCDAGDSVVMFAPYYFNSYMSFQMTGV 39
Cdd:cd00609   67 GAQEALSLLLRALLNPGDEVLVPDPTYPGYEAAARLAGA 105
AspB COG0436
Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; ...
 1-38 2.54e-07

Aspartate/methionine/tyrosine aminotransferase [Amino acid transport and metabolism]; Aspartate/methionine/tyrosine aminotransferase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


Pssm-ID: 440205 [Multi-domain]  Cd Length: 387  Bit Score: 43.58  E-value: 2.54e-07
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 281314353   1 GANQAFVNVALTLCDAGDSVVMFAPYYFNSYMSFQMTG 38
Cdd:COG0436   98 GAKEALALALLALLNPGDEVLVPDPGYPSYRAAVRLAG 135
PRK05764 PRK05764
aspartate aminotransferase; Provisional
 1-27 1.69e-05

aspartate aminotransferase; Provisional


Pssm-ID: 235596  Cd Length: 393  Bit Score: 38.57  E-value: 1.69e-05
                         10        20
                 ....*....|....*....|....*..
gi 281314353   1 GANQAFVNVALTLCDAGDSVVMFAPYY 27
Cdd:PRK05764  99 GAKQALYNAFMALLDPGDEVIIPAPYW 125
PRK07568 PRK07568
pyridoxal phosphate-dependent aminotransferase;
1-39 1.39e-04

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 181036  Cd Length: 397  Bit Score: 35.98  E-value: 1.39e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 281314353   1 GANQAFVNVALTLCDAGDSVVMFAPYYFNsYMSF-QMTGV 39
Cdd:PRK07568  96 GGSEAILFAMMAICDPGDEILVPEPFYAN-YNGFaTSAGV 134
PLN00175 PLN00175
aminotransferase family protein; Provisional
 1-38 3.70e-03

aminotransferase family protein; Provisional


Pssm-ID: 215089 [Multi-domain]  Cd Length: 413  Bit Score: 32.14  E-value: 3.70e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 281314353   1 GANQAFVNVALTLCDAGDSVVMFAPYYFNSYMSFQMTG 38
Cdd:PLN00175 123 GCTEAIAATILGLINPGDEVILFAPFYDSYEATLSMAG 160
 
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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