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Conserved domains on  [gi|62988861|gb|AAY24248|]
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unknown [Homo sapiens]

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) ...
 51-93 5.47e-03

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 PLN03226:

Pssm-ID: 450240  Cd Length: 475  Bit Score: 34.57  E-value: 5.47e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 62988861   51 GAKLKDRESHQENEDRNSELDQDEEDKESFCRGFPMSGCELET 93
Cdd:PLN03226 428 GKKLKDFKKGLESNDFSKDIEALRAEVEEFATSFPMPGFDKES 470
 
Name Accession Description Interval E-value
PLN03226 PLN03226
serine hydroxymethyltransferase; Provisional
 51-93 5.47e-03

serine hydroxymethyltransferase; Provisional


Pssm-ID: 215639  Cd Length: 475  Bit Score: 34.57  E-value: 5.47e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 62988861   51 GAKLKDRESHQENEDRNSELDQDEEDKESFCRGFPMSGCELET 93
Cdd:PLN03226 428 GKKLKDFKKGLESNDFSKDIEALRAEVEEFATSFPMPGFDKES 470
 
Name Accession Description Interval E-value
PLN03226 PLN03226
serine hydroxymethyltransferase; Provisional
 51-93 5.47e-03

serine hydroxymethyltransferase; Provisional


Pssm-ID: 215639  Cd Length: 475  Bit Score: 34.57  E-value: 5.47e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 62988861   51 GAKLKDRESHQENEDRNSELDQDEEDKESFCRGFPMSGCELET 93
Cdd:PLN03226 428 GKKLKDFKKGLESNDFSKDIEALRAEVEEFATSFPMPGFDKES 470
 
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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