SMART: Ald_Xan_dh_C domain annotation

Ald_Xan_dh_C Aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain

SMART accession number:	SM01008
Description:	Aldehyde oxidase 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 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 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.
Interpro abstract (IPR000674):	Aldehyde oxidase (EC 1.2.3.1) 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 1.1.1.204) 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 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 sulphydryl groups. The aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain is an evolutionary conserved protein domain [(PUBMED:7502041), (PUBMED:10430865)].
Family alignment:	View or

There are 2933 Ald_Xan_dh_C domains in 2933 proteins in SMART's nrdb database.

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Evolution (species in which this domain is found)
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This tree shows only several representative species. The complete taxonomic breakdown of all proteins with Ald_Xan_dh_C domain is also avaliable.

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Go to specific node: Anopheles gambiae, Arabidopsis thaliana, Caenorhabditis elegans, Drosophila melanogaster, Homo sapiens, Mus musculus, Rattus norvegicus, Takifugu rubripes
Cellular role (predicted cellular role)
Cellular role: metabolism
Literature (relevant references for this domain)
Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Dobbek H, Gremer L, Meyer O, Huber R
- Crystal structure and mechanism of CO dehydrogenase, a molybdo iron-sulfurflavoprotein containing S-selanylcysteine.
- Proc Natl Acad Sci U S A. 1999; 96: 8884-9
- Display abstract
- CO dehydrogenase from the aerobic bacterium Oligotropha carboxidovoranscatalyzes the oxidation of CO with H(2)O, yielding CO(2), two electrons,and two H(+). Its crystal structure in the air-oxidized form has beendetermined to 2.2 A. The active site of the enzyme, which containsmolybdenum with three oxygen ligands, molybdopterin-cytosine dinucleotideand S-selanylcysteine, delivers the electrons to an intramolecularelectron transport chain composed of two types of [2Fe-2S] clusters andflavin-adenine dinucleotide. CO dehydrogenase is composed of an 88.7-kDamolybdoprotein (L), a 30. 2-kDa flavoprotein (M), and a 17.8-kDairon-sulfur protein (S). It is organized as a dimer of LMS heterotrimersand resembles xanthine dehydrogenase/oxidase in many, but not all,aspects. A mechanism based on a structure with the bound suicide-substratecyanide is suggested and displays the necessity of S-selanylcysteine forthe catalyzed reaction.
- Romao MJ et al.
- Crystal structure of the xanthine oxidase-related aldehyde oxido-reductasefrom D. gigas.
- Science. 1995; 270: 1170-6
- Display abstract
- The crystal structure of the aldehyde oxido-reductase (Mop) from thesulfate reducing anaerobic Gram-negative bacterium Desulfovibrio gigas hasbeen determined at 2.25 A resolution by multiple isomorphous replacementand refined. The protein, a homodimer of 907 amino acid residues subunits,is a member of the xanthine oxidase family. The protein contains amolybdopterin cofactor (Mo-co) and two different [2Fe-2S] centers. It isfolded into four domains of which the first two bind the iron sulfurcenters and the last two are involved in Mo-co binding. Mo-co is amolybdenum molybdopterin cytosine dinucleotide. Molybdopterin forms atricyclic system with the pterin bicycle annealed to a pyran ring. Themolybdopterin dinucleotide is deeply buried in the protein. Thecis-dithiolene group of the pyran ring binds the molybdenum, which iscoordinated by three more (oxygen) ligands.
Structure (3D structures containing this domain)

3D Structures of Ald_Xan_dh_C domains in PDB

PDB code	Main view	Title
1dgj		Crystal structure of the aldehyde oxidoreductase from desulfovibrio desulfuricans atcc 27774
1ffu		Carbon monoxide dehydrogenase from hydrogenophaga pseudoflava which lacks the mo-pyranopterin moiety of the molybdenum cofactor
1ffv		Carbon monoxide dehydrogenase from hydrogenophaga pseudoflava
1fiq		Crystal structure of xanthine oxidase from bovine milk
1fo4		Crystal structure of xanthine dehydrogenase isolated from bovine milk
1jro		Crystal structure of xanthine dehydrogenase from rhodobacter capsulatus
1jrp		Crystal structure of xanthine dehydrogenase inhibited by alloxanthine from rhodobacter capsulatus
1n5w		Crystal structure of the cu,mo-co dehydrogenase (codh); oxidized form
1n5x		Xanthine dehydrogenase from bovine milk with inhibitor tei- bound
1n60		Crystal structure of the cu,mo-co dehydrogenase (codh); cyanide-inactivated form
1n61		Crystal structure of the cu,mo-co dehydrogenase (codh); dithionite reduced state
1n62		Crystal structure of the mo,cu-co dehydrogenase (codh), n- butylisocyanide-bound state
1n63		Crystal structure of the cu,mo-co dehydrogenase (codh); carbon monoxide reduced state
1rm6		Structure of 4-hydroxybenzoyl-coa reductase from thauera aromatica
1sb3		Structure of 4-hydroxybenzoyl-coa reductase from thauera aromatica
1sij		Crystal structure of the aldehyde dehydrogenase (a.k.a. aor or mop) of desulfovibrio gigas covalently bound to [aso3]-
1t3q		Crystal structure of quinoline 2-oxidoreductase from pseudomonas putida 86
1v97		Crystal structure of bovine milk xanthine dehydrogenase fyx- bound form
1vdv		Bovine milk xanthine dehydrogenase y-700 bound form
1vlb		Structure refinement of the aldehyde oxidoreductase from desulfovibrio gigas at 1.28 a
1wyg		Crystal structure of a rat xanthine dehydrogenase triple mutant (c535a, c992r and c1324s)
1zcs		Crystal structure of the arsenite-inhibited and reduced form of aldehyde oxidoreductase from desulfovibrio gigas
1zxi		Reconstituted co dehydrogenase from oligotropha carboxidovorans
2ckj		Human milk xanthine oxidoreductase
2e1q		Crystal structure of human xanthine oxidoreductase mutant, glu803val
2e3t		Crystal structure of rat xanthine oxidoreductase mutant (w335a and f336l)
2w3r		Crystal structure of xanthine dehydrogenase (desulfo form) from rhodobacter capsulatus in complex with hypoxanthine
2w3s		Crystal structure of xanthine dehydrogenase (desulfo form) from rhodobacter capsulatus in complex with xanthine
2w54		Crystal structure of xanthine dehydrogenase from rhodobacter capsulatus in complex with bound inhibitor pterin-6-aldehyde
2w55		Crystal structure of xanthine dehydrogenase (e232q variant) from rhodobacter capsulatus in complex with hypoxanthine
3b9j		Structure of xanthine oxidase with 2-hydroxy-6-methylpurine
3bdj		Crystal structure of bovine milk xanthine dehydrogenase with a covalently bound oxipurinol inhibitor
3etr		Crystal structure of xanthine oxidase in complex with lumazine
3eub		Crystal structure of desulfo-xanthine oxidase with xanthine
3fah		Glycerol inhibited form of aldehyde oxidoreductase from desulfovibrio gigas
3fc4		Ethylene glycol inhibited form of aldehyde oxidoreductase from desulfovibrio gigas
3hrd		Crystal structure of nicotinate dehydrogenase

Links (links to other resources describing this domain)
PFAM Ald_Xan_dh_C
INTERPRO IPR000674

PFAM	Ald_Xan_dh_C
INTERPRO	IPR000674