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Aromatic aminoacid monoxygenases, catalytic and oligomerization domains superfamily
SCOP classification
Superfamily statistics
Functional annotation
| General category | coiled coil |
| Detailed category | This is a complex coiled arrangement. The details of which will appear on this page shortly (some coiled coil details are being checked before they are included on the site). If you want to see examples of the states please click here here. If you require further details urgently please contact Owen Rackham |
Document: Function annotation of SCOP domain superfamilies
Enzyme Commission (EC) (show details)
Highlighted in gray are those with FDR_all>0.001
Document: EC annotation of SCOP domains
Disease Ontology (DO) (show details)
Highlighted in gray are those with FDR_all>0.001
Document: DO annotation of SCOP domains
Mouse Phenotype (MP) (show details)
Highlighted in gray are those with FDR_all>0.001
Document: MP annotation of SCOP domains
Worm Phenotype (WP) (show details)
Highlighted in gray are those with FDR_all>0.001
Document: WP annotation of SCOP domains
Fly Phenotype (FP) (show details)
Highlighted in gray are those with FDR_all>0.001
Document: FP annotation of SCOP domains
Zebrafish Anatomy (ZA) (show details)
Highlighted in gray are those with FDR_all>0.001
Document: ZA annotation of SCOP domains
Xenopus Anatomy (XA) (show details)
Highlighted in gray are those with FDR_all>0.001
Document: XA annotation of SCOP domains
Enzyme Commission (EC) (show details)
Highlighted in gray are those with FDR_all>0.001
Document: EC annotation of SCOP domains
InterPro annotation
| Cross references | IPR001273 SSF56534 Protein matches |
| Abstract | Phenylalanine, tyrosine and tryptophan hydroxylases constitute a family of
tetrahydrobiopterin-dependent aromatic amino acid hydroxylases, all of which are
rate-limiting catalysts for important metabolic pathways [ 3475690]. The proteins
are structurally and functionally related, each containing iron, and catalysing ring
hydroxylation of aromatic amino acids, using tetra-hydrobiopterin (BH4) as a substrate.
All are regulated by phosphorylation at serines in their N-termini. It has been suggested
that the proteins each contain a conserved C-terminal catalytic (C) domain and an unrelated N-terminal regulatory (R) domain. It is possible that the R domains arose from
genes that were recruited from different sources to combine with the common gene for the
catalytic core. Thus, by combining with the same C domain, the proteins acquired
the unique regulatory properties of the separate R domains.
A variety of enzymes belong to this family that includes, phenylalanine-4-hydroxylase from Chromobacterium violaceum where it is copper-dependent; it is
iron-dependent in Pseudomonas aeruginosa, phenylalanine-4-hydroxylase catalyzes the conversion of phenylalanine to tyrosine.
In humans, deficiencies are the cause of phenylketonuria, the most common inborn error
of amino acid metabolism [9406548], tryptophan 5-hydroxylase catalyzes the rate-limiting step in serotonin biosynthesis:
the conversion of tryptophan to 3-hydroxy-anthranilate and tyrosine 3-hydroxylase catalyzes the rate limiting step in catecholamine biosynthesis:
the conversion of tyrosine to 3,4-dihydroxy-L-phenylalanine. |
InterPro database
PDBeMotif information about ligands, sequence and structure motifs
PDBeMotif resource
Jump to [ Top of page · SCOP classification · InterPro annotation · PDBeMotif links · Functional annotation · Enzyme Commission (EC) · Disease Ontology (DO) · Mouse Phenotype (MP) · Worm Phenotype (WP) · Fly Phenotype (FP) · Zebrafish Anatomy (ZA) · Xenopus Anatomy (XA) · Enzyme Commission (EC) ]
Internal database links
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Browse genome assignments for this superfamily. The SUPERFAMILY hidden Markov model library has been used to carry
out SCOP domain assignments to all genomes at the superfamily level.
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Alignments of sequences to 7 models
in this superfamily are available by clicking on the 'Alignments' icon above. PDB sequences less than 40% identical
are shown by default, but any other sequence(s) may be aligned. Select PDB sequences, genome sequences, or paste in or upload your own sequences.
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Browse and view proteins in genomes which have
different domain combinations including a Aromatic aminoacid monoxygenases, catalytic and oligomerization domains domain.
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Examine the distribution of domain superfamilies, or families, across the major taxonomic kingdoms or genomes within a kingdom. This gives an immediate impression of how superfamilies, or families, are restricted to certain kingdoms of life.
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Explore domain occurrence network where nodes represent genomes and edges are domain architectures (shared between genomes) containing the superfamily of interest.
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There are 7 hidden Markov models representing the Aromatic aminoacid monoxygenases, catalytic and oligomerization domains superfamily. Information on how the models are built, and plots showing hydrophobicity, match emmission probabilities and insertion/deletion probabilities can be inspected.
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Jump to [ Top of page · SCOP classification · InterPro annotation · PDBeMotif links · Functional annotation · Enzyme Commission (EC) · Disease Ontology (DO) · Mouse Phenotype (MP) · Worm Phenotype (WP) · Fly Phenotype (FP) · Zebrafish Anatomy (ZA) · Xenopus Anatomy (XA) · Enzyme Commission (EC) · Internal database links ]
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