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Conserved domains on  [gi|194379270|dbj|BAG63601|]
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unnamed protein product [Homo sapiens]

Protein Classification

PLP-dependent aminotransferase family protein( domain architecture ID 139552)

PLP-dependent aminotransferase family protein may combine pyridoxal phosphate with an alpha-amino acid to form a Schiff base or aldimine intermediate, which then acts as the substrate in a reaction such as a transamination, racemization, or decarboxylation

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) ...
 32-122 2.71e-44

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 PLN02397:

Pssm-ID: 450240  Cd Length: 423  Bit Score: 151.65  E-value: 2.71e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379270  32 WWTHVEMGPPDPILGVTEAFKRDTNSKKMNLGVGAYRDDNGKPYVLPSVRKAEAQIAAKNLDKEYLPIGGLAEFCKdflS 111
Cdd:PLN02397  23 RFEHVEPAPPDPILGVTEAFLADPSPVKLNLGVGAYRTEEGKPVVLNVVRKAEQRLLAGSRNKEYLPIEGLAEFNK---L 99

                         90
                 ....*....|.
gi 194379270 112 SAEMSFCPNQP 122
Cdd:PLN02397 100 SAKLAYGADSP 110
 
Name Accession Description Interval E-value
PLN02397 PLN02397
aspartate transaminase
 32-122 2.71e-44

aspartate transaminase


Pssm-ID: 215222  Cd Length: 423  Bit Score: 151.65  E-value: 2.71e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379270  32 WWTHVEMGPPDPILGVTEAFKRDTNSKKMNLGVGAYRDDNGKPYVLPSVRKAEAQIAAKNLDKEYLPIGGLAEFCKdflS 111
Cdd:PLN02397  23 RFEHVEPAPPDPILGVTEAFLADPSPVKLNLGVGAYRTEEGKPVVLNVVRKAEQRLLAGSRNKEYLPIEGLAEFNK---L 99

                         90
                 ....*....|.
gi 194379270 112 SAEMSFCPNQP 122
Cdd:PLN02397 100 SAKLAYGADSP 110
TyrB COG1448
Aspartate/aromatic aminotransferase [Amino acid transport and metabolism]; Aspartate/aromatic ...
 35-107 2.09e-27

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


Pssm-ID: 441057  Cd Length: 396  Bit Score: 106.33  E-value: 2.09e-27
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 194379270  35 HVEMGPPDPILGVTEAFKRDTNSKKMNLGVGAYRDDNGKPYVLPSVRKAEAQIAAKNLDKEYLPIGGLAEFCK 107
Cdd:COG1448    4 HLEAAPGDPILGLMEAFRADPRPNKVNLGVGVYKDEQGRTPVLRAVKAAEQRLLETETTKSYLPIEGDAAFND 76
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
57-107 7.45e-07

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 48.07  E-value: 7.45e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 194379270   57 SKKMNLGVGAYRDDngkpyVLPSVRKAEAQIAAKNLDKEYLPIGGLAEFCK 107
Cdd:pfam00155   1 TDKINLGSNEYLGD-----TLPAVAKAEKDALAGGTRNLYGPTDGHPELRE 46
 
Name Accession Description Interval E-value
PLN02397 PLN02397
aspartate transaminase
 32-122 2.71e-44

aspartate transaminase


Pssm-ID: 215222  Cd Length: 423  Bit Score: 151.65  E-value: 2.71e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194379270  32 WWTHVEMGPPDPILGVTEAFKRDTNSKKMNLGVGAYRDDNGKPYVLPSVRKAEAQIAAKNLDKEYLPIGGLAEFCKdflS 111
Cdd:PLN02397  23 RFEHVEPAPPDPILGVTEAFLADPSPVKLNLGVGAYRTEEGKPVVLNVVRKAEQRLLAGSRNKEYLPIEGLAEFNK---L 99

                         90
                 ....*....|.
gi 194379270 112 SAEMSFCPNQP 122
Cdd:PLN02397 100 SAKLAYGADSP 110
PTZ00376 PTZ00376
aspartate aminotransferase; Provisional
 32-105 9.47e-38

aspartate aminotransferase; Provisional


Pssm-ID: 240390  Cd Length: 404  Bit Score: 133.90  E-value: 9.47e-38
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194379270  32 WWTHVEMGPPDPILGVTEAFKRDTNSKKMNLGVGAYRDDNGKPYVLPSVRKAEAQIAAKNLDKEYLPIGGLAEF 105
Cdd:PTZ00376   4 LFSQVPLGPPDPILGLAAAFKADPSPSKVNLGIGAYRDENGKPYVLESVRKAEKIIAEKNLDKEYLPIEGLQSF 77
PRK09257 PRK09257
aromatic amino acid transaminase;
35-107 1.49e-27

aromatic amino acid transaminase;


Pssm-ID: 181731  Cd Length: 396  Bit Score: 106.75  E-value: 1.49e-27
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 194379270  35 HVEMGPPDPILGVTEAFKRDTNSKKMNLGVGAYRDDNGKPYVLPSVRKAEAQIAAKNLDKEYLPIGGLAEFCK 107
Cdd:PRK09257   4 HLEAAPADPILGLMEAFRADPRPDKVNLGVGVYKDEQGRTPVLRAVKKAEARLLETETTKNYLPIEGLAAYRQ 76
TyrB COG1448
Aspartate/aromatic aminotransferase [Amino acid transport and metabolism]; Aspartate/aromatic ...
 35-107 2.09e-27

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


Pssm-ID: 441057  Cd Length: 396  Bit Score: 106.33  E-value: 2.09e-27
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 194379270  35 HVEMGPPDPILGVTEAFKRDTNSKKMNLGVGAYRDDNGKPYVLPSVRKAEAQIAAKNLDKEYLPIGGLAEFCK 107
Cdd:COG1448    4 HLEAAPGDPILGLMEAFRADPRPNKVNLGVGVYKDEQGRTPVLRAVKAAEQRLLETETTKSYLPIEGDAAFND 76
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
57-107 7.45e-07

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 48.07  E-value: 7.45e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 194379270   57 SKKMNLGVGAYRDDngkpyVLPSVRKAEAQIAAKNLDKEYLPIGGLAEFCK 107
Cdd:pfam00155   1 TDKINLGSNEYLGD-----TLPAVAKAEKDALAGGTRNLYGPTDGHPELRE 46
 
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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