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Conserved domains on  [gi|190889082|gb|ACE96088|]
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tryptophan hydroxylase 2, partial [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Biopterin_H super family cl46671
Biopterin-dependent aromatic amino acid hydroxylase; This family includes ...
1-22 7.13e-09

Biopterin-dependent aromatic amino acid hydroxylase; This family includes phenylalanine-4-hydroxylase, the phenylketonuria disease protein.


The actual alignment was detected with superfamily member pfam00351:

Pssm-ID: 459776  Cd Length: 331  Bit Score: 47.15  E-value: 7.13e-09
                          10        20
                  ....*....|....*....|..
gi 190889082    1 GFKDNVYRQRRKYFVDVAMGYK 22
Cdd:pfam00351  30 GFTDPVYRKRRKEIADIAFNYK 51
 
Name Accession Description Interval E-value
Biopterin_H pfam00351
Biopterin-dependent aromatic amino acid hydroxylase; This family includes ...
1-22 7.13e-09

Biopterin-dependent aromatic amino acid hydroxylase; This family includes phenylalanine-4-hydroxylase, the phenylketonuria disease protein.


Pssm-ID: 459776  Cd Length: 331  Bit Score: 47.15  E-value: 7.13e-09
                          10        20
                  ....*....|....*....|..
gi 190889082    1 GFKDNVYRQRRKYFVDVAMGYK 22
Cdd:pfam00351  30 GFTDPVYRKRRKEIADIAFNYK 51
eu_TrpOH cd03346
Eukaryotic tryptophan hydroxylase (TrpOH); a member of the biopterin-dependent aromatic amino ...
1-22 8.01e-09

Eukaryotic tryptophan hydroxylase (TrpOH); a member of the biopterin-dependent aromatic amino acid hydroxylase family of non-heme, iron(II)-dependent enzymes that also includes prokaryotic and eukaryotic phenylalanine-4-hydroxylase (PheOH) and eukaryotic tyrosine hydroxylase (TyrOH). TrpOH oxidizes L-tryptophan to 5-hydroxy-L-tryptophan, the rate-limiting step in the biosynthesis of serotonin (5-hydroxytryptamine), a widely distributed hormone and neurotransmitter.


Pssm-ID: 239462  Cd Length: 287  Bit Score: 47.11  E-value: 8.01e-09
                         10        20
                 ....*....|....*....|..
gi 190889082   1 GFKDNVYRQRRKYFVDVAMGYK 22
Cdd:cd03346   30 GFKDNVYRKRRKYFADVAMNYK 51
Trp_5_monoox TIGR01270
tryptophan 5-monooxygenase, tetrameric; This model describes tryptophan 5-monooxygenase, a ...
1-22 4.61e-08

tryptophan 5-monooxygenase, tetrameric; This model describes tryptophan 5-monooxygenase, a member of the family of tetrameric, biopterin-dependent aromatic amino acid hydroxylases found in metazoans. It is closely related to tetrameric phenylalanine-4-hydroxylase and tyrosine 3-monooxygenase, and more distantly related to the monomeric phenylalanine-4-hydroxylase found in some Gram-negative bacteria. [Energy metabolism, Amino acids and amines]


Pssm-ID: 130337 [Multi-domain]  Cd Length: 464  Bit Score: 44.85  E-value: 4.61e-08
                          10        20
                  ....*....|....*....|..
gi 190889082    1 GFKDNVYRQRRKYFVDVAMGYK 22
Cdd:TIGR01270 159 GFKDTEYRKRRMMFADLALNYK 180
 
Name Accession Description Interval E-value
Biopterin_H pfam00351
Biopterin-dependent aromatic amino acid hydroxylase; This family includes ...
1-22 7.13e-09

Biopterin-dependent aromatic amino acid hydroxylase; This family includes phenylalanine-4-hydroxylase, the phenylketonuria disease protein.


Pssm-ID: 459776  Cd Length: 331  Bit Score: 47.15  E-value: 7.13e-09
                          10        20
                  ....*....|....*....|..
gi 190889082    1 GFKDNVYRQRRKYFVDVAMGYK 22
Cdd:pfam00351  30 GFTDPVYRKRRKEIADIAFNYK 51
eu_TrpOH cd03346
Eukaryotic tryptophan hydroxylase (TrpOH); a member of the biopterin-dependent aromatic amino ...
1-22 8.01e-09

Eukaryotic tryptophan hydroxylase (TrpOH); a member of the biopterin-dependent aromatic amino acid hydroxylase family of non-heme, iron(II)-dependent enzymes that also includes prokaryotic and eukaryotic phenylalanine-4-hydroxylase (PheOH) and eukaryotic tyrosine hydroxylase (TyrOH). TrpOH oxidizes L-tryptophan to 5-hydroxy-L-tryptophan, the rate-limiting step in the biosynthesis of serotonin (5-hydroxytryptamine), a widely distributed hormone and neurotransmitter.


Pssm-ID: 239462  Cd Length: 287  Bit Score: 47.11  E-value: 8.01e-09
                         10        20
                 ....*....|....*....|..
gi 190889082   1 GFKDNVYRQRRKYFVDVAMGYK 22
Cdd:cd03346   30 GFKDNVYRKRRKYFADVAMNYK 51
Trp_5_monoox TIGR01270
tryptophan 5-monooxygenase, tetrameric; This model describes tryptophan 5-monooxygenase, a ...
1-22 4.61e-08

tryptophan 5-monooxygenase, tetrameric; This model describes tryptophan 5-monooxygenase, a member of the family of tetrameric, biopterin-dependent aromatic amino acid hydroxylases found in metazoans. It is closely related to tetrameric phenylalanine-4-hydroxylase and tyrosine 3-monooxygenase, and more distantly related to the monomeric phenylalanine-4-hydroxylase found in some Gram-negative bacteria. [Energy metabolism, Amino acids and amines]


Pssm-ID: 130337 [Multi-domain]  Cd Length: 464  Bit Score: 44.85  E-value: 4.61e-08
                          10        20
                  ....*....|....*....|..
gi 190889082    1 GFKDNVYRQRRKYFVDVAMGYK 22
Cdd:TIGR01270 159 GFKDTEYRKRRMMFADLALNYK 180
Phe4hydrox_tetr TIGR01268
phenylalanine-4-hydroxylase, tetrameric form; This model describes the larger, tetrameric form ...
1-22 2.35e-06

phenylalanine-4-hydroxylase, tetrameric form; This model describes the larger, tetrameric form of phenylalanine-4-hydroxylase, as found in metazoans. The enzyme irreversibly converts phenylalanine to tryosine and is known to be the rate-limiting step in phenylalanine catabolism in some systems. It is closely related to metazoan tyrosine 3-monooxygenase and tryptophan 5-monoxygenase, and more distantly to monomeric phenylalanine-4-hydroxylases of some Gram-negative bacteria. The member of this family from Drosophila has been described as having both phenylalanine-4-hydroxylase and tryptophan 5-monoxygenase activity (. However, a Drosophila member of the tryptophan 5-monoxygenase clade has subsequently been discovered.


Pssm-ID: 130335 [Multi-domain]  Cd Length: 436  Bit Score: 40.20  E-value: 2.35e-06
                          10        20
                  ....*....|....*....|..
gi 190889082    1 GFKDNVYRQRRKYFVDVAMGYK 22
Cdd:TIGR01268 132 GFKDPVYRARRKQFADIAFNYK 153
eu_TyrOH cd03345
Eukaryotic tyrosine hydroxylase (TyrOH); a member of the biopterin-dependent aromatic amino ...
1-22 3.37e-05

Eukaryotic tyrosine hydroxylase (TyrOH); a member of the biopterin-dependent aromatic amino acid hydroxylase family of non-heme, iron(II)-dependent enzymes that also includes prokaryotic and eukaryotic phenylalanine-4-hydroxylase (PheOH) and eukaryotic tryptophan hydroxylase (TrpOH). TyrOH catalyzes the conversion of tyrosine to L-dihydroxyphenylalanine (L-DOPA), the rate-limiting step in the biosynthesis of the catecholamines dopamine, noradrenaline, and adrenaline.


Pssm-ID: 239461  Cd Length: 298  Bit Score: 36.65  E-value: 3.37e-05
                         10        20
                 ....*....|....*....|..
gi 190889082   1 GFKDNVYRQRRKYFVDVAMGYK 22
Cdd:cd03345   29 GFSDKVYRERRKLIAEIAFQYK 50
Tyr_3_monoox TIGR01269
tyrosine 3-monooxygenase, tetrameric; This model describes tyrosine 3-monooxygenase, a member ...
1-22 3.42e-04

tyrosine 3-monooxygenase, tetrameric; This model describes tyrosine 3-monooxygenase, a member of the family of tetrameric, biopterin-dependent aromatic amino acid hydroxylases found in metazoans. It is closely related to tetrameric phenylalanine-4-hydroxylase and tryptophan 5-monooxygenase, and more distantly related to the monomeric phenylalanine-4-hydroxylase found in some Gram-negative bacteria.


Pssm-ID: 130336 [Multi-domain]  Cd Length: 457  Bit Score: 34.14  E-value: 3.42e-04
                          10        20
                  ....*....|....*....|..
gi 190889082    1 GFKDNVYRQRRKYFVDVAMGYK 22
Cdd:TIGR01269 153 GFHDKVYRQRREAIAEIAFQYK 174
 
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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