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Reviewed, UniProtKB/Swiss-Prot Q51739 (AOR_PYRFU)

Last modified December 15, 2009. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Tungsten-containing aldehyde ferredoxin oxidoreductase
    EC=1.2.7.5
Gene names
Name: aor
Ordered Locus Names: PF0346
OrganismPyrococcus furiosus [Complete proteome] [HAMAP]
Taxonomic identifier2261 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus

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Protein attributes

Sequence length605 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Catalyzes the oxidation of aldehydes to their corresponding carboxylic acids. May have a pyroglycolytic (saccharolytic) role.

Catalytic activity

An aldehyde + H2O + 2 oxidized ferredoxin = an acid + 2 H+ + 2 reduced ferredoxin.

Cofactor

Binds 1 4Fe-4S cluster per subunit.

Binds 1 tungstopterin cofactor per subunit.

Enzyme regulation

Inhibited by arsenite, iodoacetate and cyanide.

Subunit structure

Homodimer.

Miscellaneous

A significant amount of formaldehyde ferredoxin oxidoreductase activity has been observed.

Sequence similarities

Belongs to the AOR/FOR family.

Biophysicochemical properties

Kinetic parameters:

Significant activity only with aliphatic and aromatic aldehydes and only at low concentration (0.5 mM).

KM=0.72 mM for formaldehyde

Vmax=295 µmol/min/mg enzyme with formaldehyde as substrate

pH dependence:

Optimum pH is above 10.

Temperature dependence:

Optimum temperature is above 90 degrees Celsius.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 605605Tungsten-containing aldehyde ferredoxin oxidoreductase
PRO_0000064606

Sites

Metal binding2881Iron-sulfur (4Fe-4S)
Metal binding2911Iron-sulfur (4Fe-4S)
Metal binding2951Iron-sulfur (4Fe-4S)
Metal binding4941Iron-sulfur (4Fe-4S)

Secondary structure

1 ................................................................................................................. 605
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q51739-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 86254EDF6756C00D

FASTA60566,631
        10         20         30         40         50         60 
MYGNWGRFIR VNLSTGDIKV EEYDEELAKK WLGSRGLAIY LLLKEMDPTV DPLSPENKLI 

        70         80         90        100        110        120 
IAAGPLTGTS APTGGRYNVV TKSPLTGFIT MANSGGYFGA ELKFAGYDAI VVEGKAEKPV 

       130        140        150        160        170        180 
YIYIKDEHIE IRDASHIWGK KVSETEATIR KEVGSEKVKI ASIGPAGENL VKFAAIMNDG 

       190        200        210        220        230        240 
HRAAGRGGVG AVMGSKNLKA IAVEGSKTVP IADKQKFMLV VREKVNKLRN DPVAGGGLPK 

       250        260        270        280        290        300 
YGTAVLVNII NENGLYPVKN FQTGVYPYAY EQSGEAMAAK YLVRNKPCYA CPIGCGRVNR 

       310        320        330        340        350        360 
LPTVGETEGP EYESVWALGA NLGINDLASI IEANHMCDEL GLDTISTGGT LATAMELYEK 

       370        380        390        400        410        420 
GHIKDEELGD APPFRWGNTE VLHYYIEKIA KREGFGDKLA EGSYRLAESY GHPELSMTVK 

       430        440        450        460        470        480 
KLELPAYDPR GAEGHGLGYA TNNRGGCHIK NYMISPEILG YPYKMDPHDV SDDKIKMLIL 

       490        500        510        520        530        540 
FQDLTALIDS AGLCLFTTFG LGADDYRDLL NAALGWDFTT EDYLKIGERI WNAERLFNLK 

       550        560        570        580        590        600 
AGLDPARDDT LPKRFLEEPM PEGPNKGHTV RLKEMLPRYY KLRGWTEDGK IPKEKLEELG 


IAEFY

« Hide

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References

« Hide 'large scale' references
[1]"Molecular characterization of the genes encoding the tungsten-containing aldehyde ferredoxin oxidoreductase from Pyrococcus furiosus and formaldehyde ferredoxin oxidoreductase from Thermococcus litoralis."
Kletzin A., Mukund S., Kelley-Crouse T.L., Chan M.K.S., Rees D.C., Adams M.W.W.
J. Bacteriol. 177:4817-4819(1995) [PubMed: 7642512] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
[2]"The complete sequence of the Pyrococcus furiosus genome."
Weiss R.B., Dunn D.M., Robb F.T., Brown J.R.
Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
[3]"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."
Mukund S., Adams M.W.W.
J. Biol. Chem. 266:14208-14216(1991) [PubMed: 1907273] [Abstract]
Cited for: CHARACTERIZATION.
Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
[4]"Characterization of a novel tungsten-containing formaldehyde ferredoxin oxidoreductase from the hyperthermophilic archaeon, Thermococcus litoralis. A role for tungsten in peptide catabolism."
Mukund S., Adams M.W.W.
J. Biol. Chem. 268:13592-13600(1993) [PubMed: 8390467] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-26, BIOPHYSICOCHEMICAL PROPERTIES, CHARACTERIZATION.
[5]"Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase."
Chan M.K.S., Mukund S., Kletzin A., Adams M.W.W., Rees D.C.
Science 267:1463-1469(1995) [PubMed: 7878465] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X79777 Genomic DNA. Translation: CAA56170.1.
AE009950 Genomic DNA. Translation: AAL80470.1.
RefSeqNP_578075.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AORX-ray2.30A/B1-605[»]
ModBaseSearch...

Genome annotation databases

GeneID1468181.
GenomeReviewsGene locus PF0346 in contig AE009950_GR.
KEGGpfu:PF0346.
NMPDRfig|186497.1.peg.352.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG496827.
OMACTIACGR.

Enzyme and pathway databases

BRENDA1.2.7.5. 321.

Family and domain databases

InterProIPR013985. Ald_Fedxn_OxRdtase_3.
IPR013983. Ald_Fedxn_OxRdtase_N.
IPR001203. OxRdtase_Ald_Fedxn_C.
[Graphical view]
Gene3DG3DSA:1.10.599.10. Oxred_Ald_Fedxn_3. 1 hit.
G3DSA:3.60.9.10. Oxred_Ald_Fedxn_N. 1 hit.
PfamPF01314. AFOR_C. 1 hit.
PF02730. AFOR_N. 1 hit.
[Graphical view]
SMARTSM00790. AFOR_N. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameAOR_PYRFU
AccessionPrimary (citable) accession number: Q51739
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: December 15, 2009
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents