Summary: Aldehyde ferredoxin oxidoreductase, domains 2 & 3

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Wikipedia: Aldehyde ferredoxin oxidoreductase
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Aldehyde ferredoxin oxidoreductase Edit Wikipedia article

Aldehyde ferredoxin oxidoreductase

Identifiers

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PDB structures

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PMC	articles
PubMed	articles
NCBI	proteins

AFOR_N

structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase

Identifiers

Symbol

AFOR_N

Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe
PDBsum	structure summary

AFOR_C

Identifiers

Symbol

AFOR_C

Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe
PDBsum	structure summary

In enzymology, an aldehyde ferredoxin oxidoreductase (EC 1.2.7.5) is an enzyme that catalyzes the chemical reaction

an aldehyde + H₂O + 2 oxidized ferredoxin $\rightleftharpoons$ an acid + 2 H⁺ + 2 reduced ferredoxin

The 3 substrates of this enzyme are aldehyde, H₂O, and oxidized ferredoxin, whereas its 3 products are acid, H⁺, and reduced ferredoxin.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with an iron-sulfur protein as acceptor. The systematic name of this enzyme class is aldehyde:ferredoxin oxidoreductase. This enzyme is also called AOR.

Enzymes of the aldehyde ferredoxin oxidoreductase (AOR) family contain a tungsten cofactor and an 4Fe4S cluster.^[1]^[2] This family includes AOR, formaldehyde ferredoxin oxidoreductase (FOR), glyceraldehyde-3-phosphate ferredoxin oxidoreductase (GAPOR), all isolated from hyperthermophilic archea;^[1] carboxylic acid reductase found in clostridia;^[3] and hydroxycarboxylate viologen oxidoreductase from Proteus vulgaris, the sole member of the AOR family containing molybdenum.^[4] GAPOR may be involved in glycolysis,^[5] but the functions of the other proteins are not yet clear. AOR has been proposed to be the primary enzyme responsible for oxidising the aldehydes that are produced by the 2-keto acid oxidoreductases.^[6]

[edit] References

^ ^a ^b Kisker C, Schindelin H, Rees DC (1997). "Molybdenum-cofactor-containing enzymes: structure and mechanism". Annu. Rev. Biochem. 66: 233â67. doi:10.1146/annurev.biochem.66.1.233. PMID 9242907.
^ Kletzin A, Adams MW (March 1996). "Tungsten in biological systems". FEMS Microbiol. Rev. 18 (1): 5â63. PMID 8672295.
^ White H, Strobl G, Feicht R, Simon H (September 1989). "Carboxylic acid reductase: a new tungsten enzyme catalyses the reduction of non-activated carboxylic acids to aldehydes". Eur. J. Biochem. 184 (1): 89â96. doi:10.1111/j.1432-1033.1989.tb14993.x. PMID 2550230.
^ Trautwein T, Krauss F, Lottspeich F, Simon H (June 1994). "The (2R)-hydroxycarboxylate-viologen-oxidoreductase from Proteus vulgaris is a molybdenum-containing iron-sulphur protein". Eur. J. Biochem. 222 (3): 1025â32. doi:10.1111/j.1432-1033.1994.tb18954.x. PMID 8026480.
^ Mukund S, Adams MW (April 1995). "Glyceraldehyde-3-phosphate ferredoxin oxidoreductase, a novel tungsten-containing enzyme with a potential glycolytic role in the hyperthermophilic archaeon Pyrococcus furiosus". J. Biol. Chem. 270 (15): 8389â92. doi:10.1074/jbc.270.15.8389. PMID 7721730.
^ Ma K, Hutchins A, Sung SJ, Adams MW (September 1997). "Pyruvate ferredoxin oxidoreductase from the hyperthermophilic archaeon, Pyrococcus furiosus, functions as a CoA-dependent pyruvate decarboxylase". Proc. Natl. Acad. Sci. U.S.A. 94 (18): 9608â13. doi:10.1073/pnas.94.18.9608. PMC 23233. PMID 9275170. //www.ncbi.nlm.nih.gov/pmc/articles/PMC23233/.

[edit] Further reading

^ ^a ^b Kisker C, Schindelin H, Rees DC (1997). "Molybdenum-cofactor-containing enzymes: structure and mechanism". Annu. Rev. Biochem. 66: 233â67. doi:10.1146/annurev.biochem.66.1.233. PMID 9242907.
^ Kletzin A, Adams MW (March 1996). "Tungsten in biological systems". FEMS Microbiol. Rev. 18 (1): 5â63. PMID 8672295.
^ White H, Strobl G, Feicht R, Simon H (September 1989). "Carboxylic acid reductase: a new tungsten enzyme catalyses the reduction of non-activated carboxylic acids to aldehydes". Eur. J. Biochem. 184 (1): 89â96. doi:10.1111/j.1432-1033.1989.tb14993.x. PMID 2550230.
^ Trautwein T, Krauss F, Lottspeich F, Simon H (June 1994). "The (2R)-hydroxycarboxylate-viologen-oxidoreductase from Proteus vulgaris is a molybdenum-containing iron-sulphur protein". Eur. J. Biochem. 222 (3): 1025â32. doi:10.1111/j.1432-1033.1994.tb18954.x. PMID 8026480.
^ Mukund S, Adams MW (April 1995). "Glyceraldehyde-3-phosphate ferredoxin oxidoreductase, a novel tungsten-containing enzyme with a potential glycolytic role in the hyperthermophilic archaeon Pyrococcus furiosus". J. Biol. Chem. 270 (15): 8389â92. doi:10.1074/jbc.270.15.8389. PMID 7721730.
^ Ma K, Hutchins A, Sung SJ, Adams MW (September 1997). "Pyruvate ferredoxin oxidoreductase from the hyperthermophilic archaeon, Pyrococcus furiosus, functions as a CoA-dependent pyruvate decarboxylase". Proc. Natl. Acad. Sci. U.S.A. 94 (18): 9608â13. doi:10.1073/pnas.94.18.9608. PMC 23233. PMID 9275170. //www.ncbi.nlm.nih.gov/pmc/articles/PMC23233/.

Mukund S, Adams MW (1991). "The novel tungsten-iron-sulfur protein of the hyperthermophilic archaebacterium, Pyrococcus furiosus, is an aldehyde ferredoxin oxidoreductase. Evidence for its participation in a unique glycolytic pathway". J. Biol. Chem. 266 (22): 14208â16. PMID 1907273.
Johnson JL, Rajagopalan KV, Mukund S, Adams MW (1993). "Identification of molybdopterin as the organic component of the tungsten cofactor in four enzymes from hyperthermophilic Archaea". J. Biol. Chem. 268 (7): 4848â52. PMID 8444863.
Roy R, Menon AL, Adams MW (2001). "Aldehyde oxidoreductases from Pyrococcus furiosus". Methods Enzymol. 331: 132â44. doi:10.1016/S0076-6879(01)31052-2. PMID 11265456.

This article incorporates text from the public domain Pfam and InterPro IPR013983

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Aldehyde ferredoxin oxidoreductase, domains 2 & 3 Provide feedback

Aldehyde ferredoxin oxidoreductase (AOR) catalyses the reversible oxidation of aldehydes to their corresponding carboxylic acids with their accompanying reduction of the redox protein ferredoxin. This family is composed of two structural domains that bind the tungsten cofactor via DXXGL(C/D) motifs. In addition to maintaining specific binding interactions with the cofactor, another role for domains 2 and 3 may be to regulate substrate access to AOR [1].

Literature references

Chan MK, Mukund S, Kletzin A, Adams MW, Rees DC; , Science 1995;267:1463-1469.: Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase. PUBMED:7878465 EPMC:7878465

External database links

HOMSTRAD:	AFOR
PANDIT:	PF01314
Pseudofam:	PF01314
SCOP:	1aor
SYSTERS:	AFOR_C

This tab holds annotation information from the InterPro database.

InterPro entry IPR001203

Enzymes of the aldehyde ferredoxin oxidoreductase (AOR) family [PUBMED:9242907] contain a tungsten cofactor and an 4Fe4S cluster and catalyse the interconversion of aldehydes to carboxylates [PUBMED:8672295]. This family includes AOR, formaldehyde ferredoxin oxidoreductase (FOR), glyceraldehyde-3-phosphate ferredoxin oxidoreductase (GAPOR), all isolated from hyperthermophilic archea [PUBMED:9242907]; carboxylic acid reductase found in clostridia [PUBMED:2550230]; and hydroxycarboxylate viologen oxidoreductase from Proteus vulgaris, the sole member of the AOR family containing molybdenum [PUBMED:8026480]. GAPOR may be involved in glycolysis [PUBMED:7721730], but the functions of the other proteins are not yet clear. AOR has been proposed to be the primary enzyme responsible for oxidising the aldehydes that are produced by the 2-keto acid oxidoreductases [PUBMED:9275170].

This entry represents the C-terminal region of these enzymes, containing the alpha-helical structural domains 2 and 3 [PUBMED:10024458, PUBMED:7878465].

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Molecular function	electron carrier activity (GO:0009055)
	oxidoreductase activity, acting on the aldehyde or oxo group of donors, iron-sulfur protein as acceptor (GO:0016625)
	iron-sulfur cluster binding (GO:0051536)
	oxidoreductase activity (GO:0016491)
Biological process	oxidation-reduction process (GO:0055114)

Domain organisation

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Alignments

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Alignment types

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RP15/RP35/RP55/RP75: Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
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	Seed (112)	Full (1171)	Representative proteomes				NCBI (982)	Meta (251)
	Seed (112)	Full (1171)	RP15 (220)	RP35 (395)	RP55 (470)	RP75 (535)	NCBI (982)	Meta (251)
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¹Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: available, not generated, — not available.

Format an alignment

	Seed (112)	Full (1171)	Representative proteomes				NCBI (982)	Meta (251)
	Seed (112)	Full (1171)	RP15 (220)	RP35 (395)	RP55 (470)	RP75 (535)	NCBI (982)	Meta (251)
Alignment:
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	Seed (112)	Full (1171)	Representative proteomes				NCBI (982)	Meta (251)
	Seed (112)	Full (1171)	RP15 (220)	RP35 (395)	RP55 (470)	RP75 (535)	NCBI (982)	Meta (251)
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.

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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

Seed source:

Sarah Teichmann

Previous IDs:

AFOR;

Type:

Domain

Author:

Finn RD, Bateman A

Number in seed:

112

Number in full:

1171

Average length of the domain:

383.30 aa

Average identity of full alignment:

27 %

Average coverage of the sequence by the domain:

62.78 %

HMM information

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	19.6	19.6
Trusted cut-off	19.9	21.7
Noise cut-off	19.0	19.5

Model length:

382

Family (HMM) version:

13

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Interactive tree

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Interactions

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AFOR_N

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 AFOR_C domain has been found. There are 10 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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Archea	Eukaryota
Bacteria	Other sequences
Viruses	Unclassified
Viroids	Unclassified sequence

Family: AFOR_C (PF01314)

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Summary: Aldehyde ferredoxin oxidoreductase, domains 2 & 3

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Aldehyde ferredoxin oxidoreductase Edit Wikipedia article

[edit] References

[edit] Further reading

Aldehyde ferredoxin oxidoreductase, domains 2 & 3 Provide feedback

Literature references

External database links

InterPro entry IPR001203

Gene Ontology

Domain organisation

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