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114  structures 1902  species 5  interactions 5239  sequences 77  architectures

Family: Ald_Xan_dh_C (PF01315)

Summary: Aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain

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This is the Wikipedia entry entitled "Aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain". More...

Aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain Edit Wikipedia article

Aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain
Identifiers
Symbol Ald_Xan_dh_C
Pfam PF01315
InterPro IPR000674
SCOP 1alo
SUPERFAMILY 1alo

The aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain is an evolutionary conserved protein domain.

Aldehyde oxidase (EC 1.2.3.1) catalyzes the conversion of an aldehyde in the presence of oxygen and water to an acid and hydrogen peroxide. The enzyme is a homodimer, and requires FAD, molybdenum and two 2FE-2S clusters as cofactors. Xanthine dehydrogenase (EC 1.1.1.204) catalyzes the hydrogenation of xanthine to urate, and also requires FAD, molybdenum and two 2FE-2S clusters as cofactors. This activity is often found in a bifunctional enzyme with xanthine oxidase (EC 1.1.3.22) activity too. The enzyme can be converted from the dehydrogenase form to the oxidase form irreversibly by proteolysis or reversibly through oxidation of sulfhydryl groups.

Human proteins containing this domain[edit]

Further reading[edit]

This article incorporates text from the public domain Pfam and InterPro IPR000674


This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain Provide feedback

No Pfam abstract.

Literature references

  1. Romao MJ, Archer M, Moura I, Moura JJ, LeGall J, Engh R, Schneider M, Hof P, Huber R; , Science 1995;270:1170-1176.: Crystal structure of the xanthine oxidase-related aldehyde oxido-reductase from D. gigas. PUBMED:7502041 EPMC:7502041

  2. Dobbek H, Gremer L, Meyer O, Huber R; , Proc Natl Acad Sci U S A 1999;96:8884-8889.: Crystal structure and mechanism of CO dehydrogenase, a molybdo iron-sulfur flavoprotein containing S-selanylcysteine. PUBMED:10430865 EPMC:10430865


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR000674

Aldehyde oxidase (EC) catalyses the conversion of an aldehyde in the presence of oxygen and water to an acid and hydrogen peroxide. The enzyme is a homodimer, and requires FAD, molybdenum and two 2FE-2S clusters as cofactors. Xanthine dehydrogenase (EC) catalyses the hydrogenation of xanthine to urate, and also requires FAD, molybdenum and two 2FE-2S clusters as cofactors. This activity is often found in a bifunctional enzyme with xanthine oxidase (EC) activity too. The enzyme can be converted from the dehydrogenase form to the oxidase form irreversibly by proteolysis or reversibly through oxidation of sulphydryl groups.

The aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain is an evolutionary conserved protein domain [PUBMED:7502041, PUBMED:10430865].

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Alignments

We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...

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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

  Seed
(30)
Full
(5239)
Representative proteomes NCBI
(4735)
Meta
(2068)
RP15
(567)
RP35
(1035)
RP55
(1411)
RP75
(1766)
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Format an alignment

  Seed
(30)
Full
(5239)
Representative proteomes NCBI
(4735)
Meta
(2068)
RP15
(567)
RP35
(1035)
RP55
(1411)
RP75
(1766)
Alignment:
Format:
Order:
Sequence:
Gaps:
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(30)
Full
(5239)
Representative proteomes NCBI
(4735)
Meta
(2068)
RP15
(567)
RP35
(1035)
RP55
(1411)
RP75
(1766)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download   Download  

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

External links

MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...

Trees

This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

Note: You can also download the data file for the tree.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Sarah Teichmann
Previous IDs: none
Type: Domain
Author: Bateman A, Griffiths-Jones SR
Number in seed: 30
Number in full: 5239
Average length of the domain: 108.20 aa
Average identity of full alignment: 30 %
Average coverage of the sequence by the domain: 12.95 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 20.6 20.6
Trusted cut-off 20.6 20.6
Noise cut-off 20.5 20.5
Model length: 111
Family (HMM) version: 17
Download: download the raw HMM for this family

Species distribution

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Interactions

There are 5 interactions for this family. More...

Ald_Xan_dh_C Fer2_2 Ald_Xan_dh_C2 Fer2 FAD_binding_5

Structures

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 Ald_Xan_dh_C domain has been found. There are 114 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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