Summary: 4-hydroxyphenylacetate 3-hydroxylase N terminal
4-hydroxyphenylacetate 3-hydroxylase N terminal Provide feedback
HpaB Q57160 encodes part of the 4-hydroxyphenylacetate 3-hydroxylase from Escherichia coli . HpaB is part of a heterodimeric enzyme that also requires HpaC. The enzyme is NADH-dependent and uses FAD as the redox chromophore. This family also includes PvcC O30372 may play a role in one of the proposed hydroxylation steps of pyoverdine chromophore biosynthesis .
Stintzi A, Johnson Z, Stonehouse M, Ochsner U, Meyer JM, Vasil ML, Poole K; , J Bacteriol 1999;181:4118-4124.: The pvc gene cluster of Pseudomonas aeruginosa: role in synthesis of the pyoverdine chromophore and regulation by PtxR and PvdS. PUBMED:10383985 EPMC:10383985
Prieto MA, Garcia JL; , J Biol Chem 1994;269:22823-22829.: Molecular characterization of 4-hydroxyphenylacetate 3-hydroxylase of Escherichia coli. A two-protein component enzyme. PUBMED:8077235 EPMC:8077235
This tab holds annotation information from the InterPro database.
InterPro entry IPR024674
This domain is found in the N terminus of HpaB, which encodes part of the 4-hydroxyphenylacetate 3-hydroxylase from Escherichia coli [PUBMED:8077235]. The enzyme is NADH-dependent and uses FAD as the redox chromophore. The domain is also found in pyoverdin chromophore biosynthetic protein (PvcC), which may play a role in one of the proposed hydroxylation steps of pyoverdine chromophore biosynthesis [PUBMED:10383985] and in 4-hydroxybutyryl-CoA dehydratase (4-BUDH), a key enzyme in the metabolism of gamma-aminobutyrate [PUBMED:8344309].
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Curation and family details
|Seed source:||Pfam-B_3148 (release 6.5)|
|Number in seed:||163|
|Number in full:||302|
|Average length of the domain:||265.00 aa|
|Average identity of full alignment:||33 %|
|Average coverage of the sequence by the domain:||53.79 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 11927849 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||5|
|Download:||download the raw HMM for this family|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the HpaB_N domain has been found. There are 22 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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